-
Notifications
You must be signed in to change notification settings - Fork 0
/
6w63.pdb
8179 lines (8179 loc) · 647 KB
/
6w63.pdb
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105
106
107
108
109
110
111
112
113
114
115
116
117
118
119
120
121
122
123
124
125
126
127
128
129
130
131
132
133
134
135
136
137
138
139
140
141
142
143
144
145
146
147
148
149
150
151
152
153
154
155
156
157
158
159
160
161
162
163
164
165
166
167
168
169
170
171
172
173
174
175
176
177
178
179
180
181
182
183
184
185
186
187
188
189
190
191
192
193
194
195
196
197
198
199
200
201
202
203
204
205
206
207
208
209
210
211
212
213
214
215
216
217
218
219
220
221
222
223
224
225
226
227
228
229
230
231
232
233
234
235
236
237
238
239
240
241
242
243
244
245
246
247
248
249
250
251
252
253
254
255
256
257
258
259
260
261
262
263
264
265
266
267
268
269
270
271
272
273
274
275
276
277
278
279
280
281
282
283
284
285
286
287
288
289
290
291
292
293
294
295
296
297
298
299
300
301
302
303
304
305
306
307
308
309
310
311
312
313
314
315
316
317
318
319
320
321
322
323
324
325
326
327
328
329
330
331
332
333
334
335
336
337
338
339
340
341
342
343
344
345
346
347
348
349
350
351
352
353
354
355
356
357
358
359
360
361
362
363
364
365
366
367
368
369
370
371
372
373
374
375
376
377
378
379
380
381
382
383
384
385
386
387
388
389
390
391
392
393
394
395
396
397
398
399
400
401
402
403
404
405
406
407
408
409
410
411
412
413
414
415
416
417
418
419
420
421
422
423
424
425
426
427
428
429
430
431
432
433
434
435
436
437
438
439
440
441
442
443
444
445
446
447
448
449
450
451
452
453
454
455
456
457
458
459
460
461
462
463
464
465
466
467
468
469
470
471
472
473
474
475
476
477
478
479
480
481
482
483
484
485
486
487
488
489
490
491
492
493
494
495
496
497
498
499
500
501
502
503
504
505
506
507
508
509
510
511
512
513
514
515
516
517
518
519
520
521
522
523
524
525
526
527
528
529
530
531
532
533
534
535
536
537
538
539
540
541
542
543
544
545
546
547
548
549
550
551
552
553
554
555
556
557
558
559
560
561
562
563
564
565
566
567
568
569
570
571
572
573
574
575
576
577
578
579
580
581
582
583
584
585
586
587
588
589
590
591
592
593
594
595
596
597
598
599
600
601
602
603
604
605
606
607
608
609
610
611
612
613
614
615
616
617
618
619
620
621
622
623
624
625
626
627
628
629
630
631
632
633
634
635
636
637
638
639
640
641
642
643
644
645
646
647
648
649
650
651
652
653
654
655
656
657
658
659
660
661
662
663
664
665
666
667
668
669
670
671
672
673
674
675
676
677
678
679
680
681
682
683
684
685
686
687
688
689
690
691
692
693
694
695
696
697
698
699
700
701
702
703
704
705
706
707
708
709
710
711
712
713
714
715
716
717
718
719
720
721
722
723
724
725
726
727
728
729
730
731
732
733
734
735
736
737
738
739
740
741
742
743
744
745
746
747
748
749
750
751
752
753
754
755
756
757
758
759
760
761
762
763
764
765
766
767
768
769
770
771
772
773
774
775
776
777
778
779
780
781
782
783
784
785
786
787
788
789
790
791
792
793
794
795
796
797
798
799
800
801
802
803
804
805
806
807
808
809
810
811
812
813
814
815
816
817
818
819
820
821
822
823
824
825
826
827
828
829
830
831
832
833
834
835
836
837
838
839
840
841
842
843
844
845
846
847
848
849
850
851
852
853
854
855
856
857
858
859
860
861
862
863
864
865
866
867
868
869
870
871
872
873
874
875
876
877
878
879
880
881
882
883
884
885
886
887
888
889
890
891
892
893
894
895
896
897
898
899
900
901
902
903
904
905
906
907
908
909
910
911
912
913
914
915
916
917
918
919
920
921
922
923
924
925
926
927
928
929
930
931
932
933
934
935
936
937
938
939
940
941
942
943
944
945
946
947
948
949
950
951
952
953
954
955
956
957
958
959
960
961
962
963
964
965
966
967
968
969
970
971
972
973
974
975
976
977
978
979
980
981
982
983
984
985
986
987
988
989
990
991
992
993
994
995
996
997
998
999
1000
HEADER VIRAL PROTEIN/INHIBITOR 16-MAR-20 6W63
TITLE STRUCTURE OF COVID-19 MAIN PROTEASE BOUND TO POTENT BROAD-SPECTRUM
TITLE 2 NON-COVALENT INHIBITOR X77
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3C-LIKE PROTEINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 3CL-PRO, 3CLP;
COMPND 5 EC: 3.4.22.69;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 3 2;
SOURCE 4 ORGANISM_COMMON: 2019-NCOV;
SOURCE 5 ORGANISM_TAXID: 2697049;
SOURCE 6 GENE: REP, 1A-1B;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS COVID-19, SARS, SARS-COV-2, SARS-COV, MAIN PROTEASE, 3C-LIKE
KEYWDS 2 PROTEASE, 3CL PROTEASE, 3CLPRO, MPRO, BROAD-SPECTRUM, INHIBITOR,
KEYWDS 3 PROTEINASE, NON-COVALENT, REVERSIBLE, STRUCTURAL GENOMICS, CENTER
KEYWDS 4 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, ANTIVIRAL
KEYWDS 5 PROTEIN, VIRAL PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.D.MESECAR,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 2 (CSGID)
REVDAT 3 18-OCT-23 6W63 1 REMARK
REVDAT 2 06-MAY-20 6W63 1 COMPND SOURCE DBREF
REVDAT 1 25-MAR-20 6W63 0
JRNL AUTH A.D.MESECAR
JRNL TITL A TAXONOMICALLY-DRIVEN APPROACH TO DEVELOPMENT OF POTENT,
JRNL TITL 2 BROAD-SPECTRUM INHIBITORS OF CORONAVIRUS MAIN PROTEASE
JRNL TITL 3 INCLUDING SARS-COV-2 (COVID-19)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 18507
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1852
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.9100 - 4.9300 0.99 1393 157 0.1517 0.2062
REMARK 3 2 4.9300 - 3.9200 0.99 1322 147 0.1139 0.1570
REMARK 3 3 3.9200 - 3.4200 1.00 1297 144 0.1333 0.1951
REMARK 3 4 3.4200 - 3.1100 1.00 1298 144 0.1532 0.2316
REMARK 3 5 3.1100 - 2.8900 1.00 1278 141 0.1646 0.2308
REMARK 3 6 2.8900 - 2.7200 1.00 1300 145 0.1737 0.3322
REMARK 3 7 2.7200 - 2.5800 1.00 1262 141 0.1713 0.2516
REMARK 3 8 2.5800 - 2.4700 1.00 1278 141 0.1598 0.2497
REMARK 3 9 2.4700 - 2.3700 1.00 1259 141 0.1555 0.2286
REMARK 3 10 2.3700 - 2.2900 1.00 1274 140 0.1588 0.2461
REMARK 3 11 2.2900 - 2.2200 1.00 1265 141 0.1581 0.2417
REMARK 3 12 2.2200 - 2.1600 0.98 1234 137 0.1685 0.2654
REMARK 3 13 2.1600 - 2.1000 0.94 1195 133 0.1854 0.2436
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.205
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.857
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 2448
REMARK 3 ANGLE : 1.094 3329
REMARK 3 CHIRALITY : 0.057 372
REMARK 3 PLANARITY : 0.008 431
REMARK 3 DIHEDRAL : 15.084 1424
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2957 18.9092 -26.0227
REMARK 3 T TENSOR
REMARK 3 T11: 0.1252 T22: 0.1215
REMARK 3 T33: 0.1310 T12: -0.0005
REMARK 3 T13: 0.0105 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.5120 L22: 0.1053
REMARK 3 L33: 0.4330 L12: 0.0651
REMARK 3 L13: 0.4390 L23: -0.0145
REMARK 3 S TENSOR
REMARK 3 S11: -0.0185 S12: 0.0001 S13: -0.0445
REMARK 3 S21: -0.0061 S22: 0.0178 S23: 0.0150
REMARK 3 S31: 0.0328 S32: -0.0025 S33: 0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6W63 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-20.
REMARK 100 THE DEPOSITION ID IS D_1000247699.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18549
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 6LU7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3 MM DTT, 1% MPD, 80MM KCL, 50 MM MES
REMARK 280 PH 6.0, 16% PEG 10K 2UL PROTEIN ( 125 UM 3CLPRO, 25 MM HEPES PH
REMARK 280 7.5, 2.5 MM DTT, 1% DMSO, 400 UM 077) + 1 UL RESERVOIR, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 22.52500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.92000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.52500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.92000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 63.84000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 543 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 699 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 713 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 769 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 306
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H ALA A 193 O HOH A 505 1.48
REMARK 500 OD1 ASP A 155 O HOH A 501 2.02
REMARK 500 O HOH A 732 O HOH A 757 2.04
REMARK 500 O HOH A 644 O HOH A 727 2.08
REMARK 500 O HOH A 614 O HOH A 652 2.11
REMARK 500 OE2 GLU A 240 O HOH A 502 2.12
REMARK 500 OE1 GLU A 55 O HOH A 503 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 592 O HOH A 666 4554 1.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 44 CB CYS A 44 SG -0.106
REMARK 500 CYS A 128 CB CYS A 128 SG -0.109
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 33 -128.50 48.84
REMARK 500 ASN A 51 72.32 -152.85
REMARK 500 ASN A 84 -124.79 50.39
REMARK 500 TYR A 154 -101.14 76.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 781 DISTANCE = 6.26 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue X77 A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-51000.103 RELATED DB: TARGETTRACK
DBREF 6W63 A 1 306 UNP P0DTD1 R1AB_SARS2 3264 3569
SEQRES 1 A 306 SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL
SEQRES 2 A 306 GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR
SEQRES 3 A 306 LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO
SEQRES 4 A 306 ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO
SEQRES 5 A 306 ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN
SEQRES 6 A 306 PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE
SEQRES 7 A 306 GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL
SEQRES 8 A 306 ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL
SEQRES 9 A 306 ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS
SEQRES 10 A 306 TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET
SEQRES 11 A 306 ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY
SEQRES 12 A 306 SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS
SEQRES 13 A 306 VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR
SEQRES 14 A 306 GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR
SEQRES 15 A 306 GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY
SEQRES 16 A 306 THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU
SEQRES 17 A 306 TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN
SEQRES 18 A 306 ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA
SEQRES 19 A 306 MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL
SEQRES 20 A 306 ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA
SEQRES 21 A 306 VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN
SEQRES 22 A 306 ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU
SEQRES 23 A 306 LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN
SEQRES 24 A 306 CYS SER GLY VAL THR PHE GLN
HET X77 A 401 66
HETNAM X77 N-(4-TERT-BUTYLPHENYL)-N-[(1R)-2-(CYCLOHEXYLAMINO)-2-
HETNAM 2 X77 OXO-1-(PYRIDIN-3-YL)ETHYL]-1H-IMIDAZOLE-4-CARBOXAMIDE
FORMUL 2 X77 C27 H33 N5 O2
FORMUL 3 HOH *281(H2 O)
HELIX 1 AA1 SER A 10 GLY A 15 1 6
HELIX 2 AA2 HIS A 41 CYS A 44 5 4
HELIX 3 AA3 ASN A 53 ARG A 60 1 8
HELIX 4 AA4 SER A 62 PHE A 66 5 5
HELIX 5 AA5 ILE A 200 ASN A 214 1 15
HELIX 6 AA6 THR A 226 TYR A 237 1 12
HELIX 7 AA7 THR A 243 LEU A 250 1 8
HELIX 8 AA8 LEU A 250 GLY A 258 1 9
HELIX 9 AA9 ALA A 260 GLY A 275 1 16
HELIX 10 AB1 THR A 292 CYS A 300 1 9
SHEET 1 AA1 7 VAL A 73 LEU A 75 0
SHEET 2 AA1 7 LEU A 67 ALA A 70 -1 N ALA A 70 O VAL A 73
SHEET 3 AA1 7 MET A 17 CYS A 22 -1 N THR A 21 O LEU A 67
SHEET 4 AA1 7 THR A 25 LEU A 32 -1 O LEU A 27 N VAL A 20
SHEET 5 AA1 7 VAL A 35 PRO A 39 -1 O TYR A 37 N LEU A 30
SHEET 6 AA1 7 VAL A 86 VAL A 91 -1 O LEU A 87 N CYS A 38
SHEET 7 AA1 7 VAL A 77 GLN A 83 -1 N ILE A 78 O LYS A 90
SHEET 1 AA2 5 TYR A 101 PHE A 103 0
SHEET 2 AA2 5 CYS A 156 GLU A 166 1 O PHE A 159 N LYS A 102
SHEET 3 AA2 5 VAL A 148 ASP A 153 -1 N GLY A 149 O TYR A 161
SHEET 4 AA2 5 THR A 111 TYR A 118 -1 N SER A 113 O PHE A 150
SHEET 5 AA2 5 SER A 121 ALA A 129 -1 O TYR A 126 N VAL A 114
SHEET 1 AA3 3 TYR A 101 PHE A 103 0
SHEET 2 AA3 3 CYS A 156 GLU A 166 1 O PHE A 159 N LYS A 102
SHEET 3 AA3 3 HIS A 172 THR A 175 -1 O ALA A 173 N MET A 165
SITE 1 AC1 17 THR A 25 THR A 26 HIS A 41 PHE A 140
SITE 2 AC1 17 LEU A 141 ASN A 142 GLY A 143 SER A 144
SITE 3 AC1 17 CYS A 145 HIS A 163 HIS A 164 MET A 165
SITE 4 AC1 17 GLU A 166 GLY A 251 HOH A 518 HOH A 600
SITE 5 AC1 17 HOH A 671
CRYST1 45.050 63.840 106.588 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.022198 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015664 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009382 0.00000
ATOM 1 N SER A 1 15.713 38.032 -22.313 1.00 39.55 N
ANISOU 1 N SER A 1 5046 4997 4984 -235 -442 334 N
ATOM 2 CA SER A 1 15.198 37.322 -21.121 1.00 26.86 C
ANISOU 2 CA SER A 1 3450 3368 3388 -178 -402 288 C
ATOM 3 C SER A 1 13.679 37.410 -21.009 1.00 25.13 C
ANISOU 3 C SER A 1 3248 3113 3188 -148 -405 251 C
ATOM 4 O SER A 1 12.980 37.891 -21.925 1.00 21.95 O
ANISOU 4 O SER A 1 2847 2702 2791 -168 -431 257 O
ATOM 5 CB SER A 1 15.869 37.867 -19.862 1.00 43.51 C
ANISOU 5 CB SER A 1 5575 5450 5507 -164 -432 291 C
ATOM 6 OG SER A 1 15.792 39.268 -19.773 1.00 44.46 O
ANISOU 6 OG SER A 1 5718 5530 5646 -181 -509 307 O
ATOM 7 H1 SER A 1 15.104 38.003 -22.961 1.00 47.47 H
ATOM 8 H2 SER A 1 15.883 38.880 -22.103 1.00 47.47 H
ATOM 9 H3 SER A 1 16.461 37.639 -22.591 1.00 47.47 H
ATOM 10 HA SER A 1 15.414 36.380 -21.199 1.00 32.24 H
ATOM 11 HB2 SER A 1 15.429 37.484 -19.087 1.00 52.22 H
ATOM 12 HB3 SER A 1 16.804 37.609 -19.874 1.00 52.22 H
ATOM 13 HG SER A 1 16.447 39.564 -19.338 1.00 53.37 H
ATOM 14 N GLY A 2 13.166 36.900 -19.901 1.00 21.77 N
ANISOU 14 N GLY A 2 2831 2671 2770 -101 -376 213 N
ATOM 15 CA GLY A 2 11.737 36.732 -19.706 1.00 26.23 C
ANISOU 15 CA GLY A 2 3404 3215 3347 -68 -365 174 C
ATOM 16 C GLY A 2 11.288 35.302 -19.983 1.00 21.76 C
ANISOU 16 C GLY A 2 2821 2678 2769 -54 -296 156 C
ATOM 17 O GLY A 2 12.022 34.471 -20.519 1.00 26.30 O
ANISOU 17 O GLY A 2 3378 3288 3328 -70 -260 171 O
ATOM 18 H GLY A 2 13.638 36.638 -19.232 1.00 26.13 H
ATOM 19 HA2 GLY A 2 11.508 36.954 -18.790 1.00 31.48 H
ATOM 20 HA3 GLY A 2 11.257 37.326 -20.304 1.00 31.48 H
ATOM 21 N PHE A 3 10.050 35.003 -19.593 1.00 24.77 N
ANISOU 21 N PHE A 3 3207 3046 3158 -22 -279 122 N
ATOM 22 CA PHE A 3 9.510 33.665 -19.811 1.00 29.60 C
ANISOU 22 CA PHE A 3 3806 3680 3762 -10 -220 106 C
ATOM 23 C PHE A 3 7.999 33.727 -19.923 1.00 28.96 C
ANISOU 23 C PHE A 3 3727 3584 3690 9 -220 79 C
ATOM 24 O PHE A 3 7.318 34.232 -19.028 1.00 33.78 O
ANISOU 24 O PHE A 3 4348 4176 4311 37 -239 55 O
ATOM 25 CB PHE A 3 9.886 32.694 -18.689 1.00 28.47 C
ANISOU 25 CB PHE A 3 3658 3547 3612 16 -179 94 C
ATOM 26 CG PHE A 3 9.918 31.247 -19.138 1.00 33.75 C
ANISOU 26 CG PHE A 3 4310 4241 4271 16 -126 91 C
ATOM 27 CD1 PHE A 3 10.900 30.800 -20.012 1.00 29.96 C
ANISOU 27 CD1 PHE A 3 3817 3787 3780 -8 -112 111 C
ATOM 28 CD2 PHE A 3 8.957 30.346 -18.707 1.00 24.72 C
ANISOU 28 CD2 PHE A 3 3165 3097 3130 39 -93 69 C
ATOM 29 CE1 PHE A 3 10.933 29.461 -20.432 1.00 36.09 C
ANISOU 29 CE1 PHE A 3 4580 4583 4549 -4 -69 103 C
ATOM 30 CE2 PHE A 3 8.973 29.025 -19.121 1.00 28.56 C
ANISOU 30 CE2 PHE A 3 3640 3600 3611 38 -52 66 C
ATOM 31 CZ PHE A 3 9.958 28.571 -19.978 1.00 24.59 C
ANISOU 31 CZ PHE A 3 3126 3118 3100 19 -41 81 C
ATOM 32 H PHE A 3 9.513 35.550 -19.206 1.00 29.73 H
ATOM 33 HA PHE A 3 9.875 33.336 -20.647 1.00 35.53 H
ATOM 34 HB2 PHE A 3 10.769 32.923 -18.359 1.00 34.17 H
ATOM 35 HB3 PHE A 3 9.234 32.771 -17.975 1.00 34.17 H
ATOM 36 HD1 PHE A 3 11.544 31.395 -20.323 1.00 35.96 H
ATOM 37 HD2 PHE A 3 8.289 30.635 -18.129 1.00 29.67 H
ATOM 38 HE1 PHE A 3 11.600 29.169 -21.010 1.00 43.32 H
ATOM 39 HE2 PHE A 3 8.316 28.439 -18.821 1.00 34.28 H
ATOM 40 HZ PHE A 3 9.972 27.682 -20.248 1.00 29.52 H
ATOM 41 N ARG A 4 7.481 33.195 -21.017 1.00 25.67 N
ANISOU 41 N ARG A 4 3302 3181 3271 -7 -200 81 N
ATOM 42 CA ARG A 4 6.061 33.255 -21.277 1.00 23.55 C
ANISOU 42 CA ARG A 4 3035 2901 3012 6 -201 59 C
ATOM 43 C ARG A 4 5.556 31.904 -21.771 1.00 27.05 C
ANISOU 43 C ARG A 4 3465 3365 3447 7 -149 51 C
ATOM 44 O ARG A 4 6.291 31.103 -22.354 1.00 18.26 O
ANISOU 44 O ARG A 4 2342 2274 2323 -10 -122 64 O
ATOM 45 CB ARG A 4 5.758 34.342 -22.318 1.00 25.69 C
ANISOU 45 CB ARG A 4 3312 3156 3292 -20 -251 72 C
ATOM 46 CG ARG A 4 5.867 35.764 -21.802 1.00 36.07 C
ANISOU 46 CG ARG A 4 4644 4438 4622 -16 -315 73 C
ATOM 47 CD ARG A 4 4.478 36.305 -21.448 1.00 40.40 C
ANISOU 47 CD ARG A 4 5199 4963 5188 16 -338 39 C
ATOM 48 NE ARG A 4 4.481 37.730 -21.126 1.00 48.64 N
ANISOU 48 NE ARG A 4 6261 5970 6251 22 -410 35 N
ATOM 49 CZ ARG A 4 3.484 38.359 -20.499 1.00 33.50 C
ANISOU 49 CZ ARG A 4 4350 4030 4348 60 -439 -2 C
ATOM 50 NH1 ARG A 4 2.404 37.694 -20.110 1.00 42.15 N
ANISOU 50 NH1 ARG A 4 5434 5143 5439 91 -400 -35 N
ATOM 51 NH2 ARG A 4 3.568 39.646 -20.246 1.00 30.56 N
ANISOU 51 NH2 ARG A 4 3996 3621 3996 66 -511 -7 N
ATOM 52 H ARG A 4 7.938 32.793 -21.625 1.00 30.81 H
ATOM 53 HA ARG A 4 5.589 33.451 -20.453 1.00 28.27 H
ATOM 54 HB2 ARG A 4 6.386 34.249 -23.051 1.00 30.84 H
ATOM 55 HB3 ARG A 4 4.852 34.217 -22.638 1.00 30.84 H
ATOM 56 HG2 ARG A 4 6.419 35.781 -21.005 1.00 43.29 H
ATOM 57 HG3 ARG A 4 6.256 36.331 -22.487 1.00 43.29 H
ATOM 58 HD2 ARG A 4 3.886 36.172 -22.206 1.00 48.49 H
ATOM 59 HD3 ARG A 4 4.141 35.825 -20.676 1.00 48.49 H
ATOM 60 HE ARG A 4 5.169 38.193 -21.354 1.00 58.38 H
ATOM 61 HH11 ARG A 4 2.342 36.849 -20.261 1.00 50.59 H
ATOM 62 HH12 ARG A 4 1.767 38.107 -19.707 1.00 50.59 H
ATOM 63 HH21 ARG A 4 4.267 40.087 -20.485 1.00 36.69 H
ATOM 64 HH22 ARG A 4 2.923 40.048 -19.843 1.00 36.69 H
ATOM 65 N LYS A 5 4.270 31.679 -21.564 1.00 22.11 N
ANISOU 65 N LYS A 5 2838 2734 2828 27 -139 28 N
ATOM 66 CA LYS A 5 3.594 30.583 -22.246 1.00 25.57 C
ANISOU 66 CA LYS A 5 3267 3186 3263 22 -102 23 C
ATOM 67 C LYS A 5 3.570 30.907 -23.735 1.00 18.74 C
ANISOU 67 C LYS A 5 2400 2324 2397 -10 -117 38 C
ATOM 68 O LYS A 5 2.833 31.784 -24.185 1.00 30.86 O
ANISOU 68 O LYS A 5 3940 3843 3942 -15 -151 35 O
ATOM 69 CB LYS A 5 2.191 30.379 -21.696 1.00 37.63 C
ANISOU 69 CB LYS A 5 4792 4711 4796 47 -92 -2 C
ATOM 70 CG LYS A 5 1.739 28.916 -21.791 1.00 53.53 C
ANISOU 70 CG LYS A 5 6795 6740 6804 48 -46 -5 C
ATOM 71 CD LYS A 5 1.062 28.464 -20.520 1.00 55.62 C
ANISOU 71 CD LYS A 5 7054 7012 7065 74 -28 -20 C
ATOM 72 CE LYS A 5 1.843 27.372 -19.855 1.00 52.04 C
ANISOU 72 CE LYS A 5 6598 6569 6605 76 2 -11 C
ATOM 73 NZ LYS A 5 1.204 27.059 -18.568 1.00 60.07 N
ANISOU 73 NZ LYS A 5 7608 7599 7616 97 15 -22 N
ATOM 74 H LYS A 5 3.768 32.141 -21.040 1.00 26.54 H
ATOM 75 HA LYS A 5 4.075 29.753 -22.101 1.00 30.70 H
ATOM 76 HB2 LYS A 5 2.175 30.641 -20.762 1.00 45.17 H
ATOM 77 HB3 LYS A 5 1.568 30.922 -22.204 1.00 45.17 H
ATOM 78 HG2 LYS A 5 1.109 28.821 -22.523 1.00 64.24 H
ATOM 79 HG3 LYS A 5 2.512 28.350 -21.944 1.00 64.24 H
ATOM 80 HD2 LYS A 5 0.997 29.212 -19.905 1.00 66.75 H
ATOM 81 HD3 LYS A 5 0.177 28.126 -20.727 1.00 66.75 H
ATOM 82 HE2 LYS A 5 1.843 26.577 -20.411 1.00 62.46 H
ATOM 83 HE3 LYS A 5 2.754 27.664 -19.694 1.00 62.46 H
ATOM 84 HZ1 LYS A 5 1.621 26.376 -18.179 1.00 72.09 H
ATOM 85 HZ2 LYS A 5 1.243 27.766 -18.029 1.00 72.09 H
ATOM 86 HZ3 LYS A 5 0.350 26.841 -18.697 1.00 72.09 H
ATOM 87 N MET A 6 4.417 30.236 -24.485 1.00 21.91 N
ANISOU 87 N MET A 6 2793 2747 2786 -30 -97 52 N
ATOM 88 CA MET A 6 4.680 30.567 -25.875 1.00 22.60 C
ANISOU 88 CA MET A 6 2874 2847 2865 -64 -112 71 C
ATOM 89 C MET A 6 4.177 29.428 -26.749 1.00 29.08 C
ANISOU 89 C MET A 6 3685 3684 3679 -68 -76 61 C
ATOM 90 O MET A 6 4.514 28.258 -26.510 1.00 20.25 O
ANISOU 90 O MET A 6 2560 2579 2555 -55 -40 51 O
ATOM 91 CB MET A 6 6.180 30.794 -26.071 1.00 23.13 C
ANISOU 91 CB MET A 6 2934 2936 2917 -85 -119 95 C
ATOM 92 CG MET A 6 6.608 31.147 -27.472 1.00 33.71 C
ANISOU 92 CG MET A 6 4264 4302 4241 -125 -135 118 C
ATOM 93 SD MET A 6 8.356 31.585 -27.521 1.00 49.44 S
ANISOU 93 SD MET A 6 6245 6325 6215 -151 -150 150 S
ATOM 94 CE MET A 6 8.429 32.914 -26.331 1.00 37.49 C
ANISOU 94 CE MET A 6 4753 4769 4722 -143 -200 160 C
ATOM 95 H MET A 6 4.869 29.561 -24.204 1.00 26.30 H
ATOM 96 HA MET A 6 4.217 31.379 -26.133 1.00 27.13 H
ATOM 97 HB2 MET A 6 6.456 31.523 -25.494 1.00 27.76 H
ATOM 98 HB3 MET A 6 6.646 29.981 -25.824 1.00 27.76 H
ATOM 99 HG2 MET A 6 6.466 30.384 -28.055 1.00 40.46 H
ATOM 100 HG3 MET A 6 6.092 31.905 -27.786 1.00 40.46 H
ATOM 101 HE1 MET A 6 9.187 33.483 -26.539 1.00 44.99 H
ATOM 102 HE2 MET A 6 7.607 33.427 -26.379 1.00 44.99 H
ATOM 103 HE3 MET A 6 8.533 32.538 -25.443 1.00 44.99 H
ATOM 104 N ALA A 7 3.362 29.772 -27.741 1.00 21.87 N
ANISOU 104 N ALA A 7 2772 2768 2768 -85 -91 62 N
ATOM 105 CA ALA A 7 2.837 28.804 -28.685 1.00 22.69 C
ANISOU 105 CA ALA A 7 2868 2888 2866 -91 -64 53 C
ATOM 106 C ALA A 7 3.639 28.833 -29.976 1.00 21.13 C
ANISOU 106 C ALA A 7 2659 2724 2647 -124 -67 70 C
ATOM 107 O ALA A 7 4.336 29.795 -30.269 1.00 18.97 O
ANISOU 107 O ALA A 7 2383 2459 2365 -149 -97 94 O
ATOM 108 CB ALA A 7 1.375 29.094 -29.005 1.00 18.47 C
ANISOU 108 CB ALA A 7 2339 2333 2344 -90 -76 44 C
ATOM 109 H ALA A 7 3.097 30.577 -27.886 1.00 26.25 H
ATOM 110 HA ALA A 7 2.899 27.919 -28.293 1.00 27.24 H
ATOM 111 HB1 ALA A 7 1.254 29.077 -29.968 1.00 22.17 H
ATOM 112 HB2 ALA A 7 0.820 28.416 -28.590 1.00 22.17 H
ATOM 113 HB3 ALA A 7 1.144 29.970 -28.658 1.00 22.17 H
ATOM 114 N PHE A 8 3.500 27.782 -30.763 1.00 17.58 N
ANISOU 114 N PHE A 8 2199 2294 2186 -125 -38 58 N
ATOM 115 CA PHE A 8 4.097 27.786 -32.088 1.00 17.77 C
ANISOU 115 CA PHE A 8 2208 2358 2186 -156 -40 70 C
ATOM 116 C PHE A 8 3.360 28.748 -33.016 1.00 18.67 C
ANISOU 116 C PHE A 8 2325 2468 2300 -186 -73 86 C
ATOM 117 O PHE A 8 2.157 28.956 -32.881 1.00 20.71 O
ANISOU 117 O PHE A 8 2595 2694 2578 -178 -83 78 O
ATOM 118 CB PHE A 8 4.085 26.391 -32.697 1.00 19.90 C
ANISOU 118 CB PHE A 8 2467 2650 2445 -144 -4 46 C
ATOM 119 CG PHE A 8 5.050 25.466 -32.066 1.00 22.94 C
ANISOU 119 CG PHE A 8 2844 3045 2825 -120 22 33 C
ATOM 120 CD1 PHE A 8 6.402 25.550 -32.355 1.00 23.40 C
ANISOU 120 CD1 PHE A 8 2885 3146 2860 -130 23 42 C
ATOM 121 CD2 PHE A 8 4.618 24.499 -31.183 1.00 23.46 C
ANISOU 121 CD2 PHE A 8 2920 3083 2910 -89 42 13 C
ATOM 122 CE1 PHE A 8 7.302 24.683 -31.742 1.00 27.87 C
ANISOU 122 CE1 PHE A 8 3444 3720 3424 -105 45 28 C
ATOM 123 CE2 PHE A 8 5.520 23.631 -30.578 1.00 26.87 C
ANISOU 123 CE2 PHE A 8 3347 3521 3340 -67 61 2 C
ATOM 124 CZ PHE A 8 6.848 23.728 -30.860 1.00 27.04 C
ANISOU 124 CZ PHE A 8 3352 3580 3341 -73 62 7 C
ATOM 125 H PHE A 8 3.072 27.064 -30.561 1.00 21.11 H
ATOM 126 HA PHE A 8 5.019 28.079 -32.011 1.00 21.34 H
ATOM 127 HB2 PHE A 8 3.199 26.011 -32.593 1.00 23.89 H
ATOM 128 HB3 PHE A 8 4.309 26.458 -33.638 1.00 23.89 H
ATOM 129 HD1 PHE A 8 6.709 26.186 -32.959 1.00 28.09 H
ATOM 130 HD2 PHE A 8 3.711 24.426 -30.989 1.00 28.16 H
ATOM 131 HE1 PHE A 8 8.210 24.749 -31.928 1.00 33.45 H
ATOM 132 HE2 PHE A 8 5.217 22.984 -29.982 1.00 32.25 H
ATOM 133 HZ PHE A 8 7.452 23.147 -30.456 1.00 32.46 H
ATOM 134 N PRO A 9 4.069 29.375 -33.953 1.00 19.39 N
ANISOU 134 N PRO A 9 2404 2594 2370 -223 -94 112 N
ATOM 135 CA PRO A 9 3.375 30.186 -34.965 1.00 21.45 C
ANISOU 135 CA PRO A 9 2667 2854 2629 -257 -127 130 C
ATOM 136 C PRO A 9 2.391 29.302 -35.711 1.00 23.50 C
ANISOU 136 C PRO A 9 2925 3116 2888 -251 -102 107 C
ATOM 137 O PRO A 9 2.683 28.151 -36.022 1.00 18.95 O
ANISOU 137 O PRO A 9 2338 2566 2297 -238 -66 86 O
ATOM 138 CB PRO A 9 4.502 30.697 -35.864 1.00 26.70 C
ANISOU 138 CB PRO A 9 3313 3571 3262 -300 -144 162 C
ATOM 139 CG PRO A 9 5.785 30.408 -35.094 1.00 26.92 C
ANISOU 139 CG PRO A 9 3331 3619 3280 -286 -127 163 C
ATOM 140 CD PRO A 9 5.498 29.198 -34.276 1.00 29.21 C
ANISOU 140 CD PRO A 9 3628 3889 3584 -238 -84 124 C
ATOM 141 HA PRO A 9 2.926 30.954 -34.579 1.00 25.75 H
ATOM 142 HB2 PRO A 9 4.491 30.223 -36.710 1.00 32.05 H
ATOM 143 HB3 PRO A 9 4.396 31.650 -36.017 1.00 32.05 H
ATOM 144 HG2 PRO A 9 6.510 30.239 -35.716 1.00 32.32 H
ATOM 145 HG3 PRO A 9 6.005 31.163 -34.527 1.00 32.32 H
ATOM 146 HD2 PRO A 9 5.643 28.387 -34.787 1.00 35.07 H
ATOM 147 HD3 PRO A 9 6.039 29.184 -33.471 1.00 35.07 H
ATOM 148 N SER A 10 1.200 29.830 -35.937 1.00 16.47 N
ANISOU 148 N SER A 10 2047 2195 2017 -256 -125 108 N
ATOM 149 CA SER A 10 0.076 29.038 -36.392 1.00 21.27 C
ANISOU 149 CA SER A 10 2657 2792 2631 -245 -105 86 C
ATOM 150 C SER A 10 -0.209 29.157 -37.890 1.00 19.53 C
ANISOU 150 C SER A 10 2428 2600 2392 -282 -116 97 C
ATOM 151 O SER A 10 -1.188 28.581 -38.357 1.00 19.13 O
ANISOU 151 O SER A 10 2380 2541 2348 -276 -104 81 O
ATOM 152 CB SER A 10 -1.164 29.462 -35.629 1.00 17.87 C
ANISOU 152 CB SER A 10 2244 2314 2234 -224 -120 76 C
ATOM 153 OG SER A 10 -1.455 30.833 -35.901 1.00 22.78 O
ANISOU 153 OG SER A 10 2872 2918 2866 -248 -171 98 O
ATOM 154 H SER A 10 1.017 30.664 -35.830 1.00 19.78 H
ATOM 155 HA SER A 10 0.273 28.105 -36.213 1.00 25.53 H
ATOM 156 HB2 SER A 10 -1.914 28.914 -35.908 1.00 21.46 H
ATOM 157 HB3 SER A 10 -1.008 29.350 -34.678 1.00 21.46 H
ATOM 158 HG SER A 10 -2.286 30.956 -35.899 1.00 27.35 H
ATOM 159 N GLY A 11 0.594 29.892 -38.647 1.00 30.99 N
ANISOU 159 N GLY A 11 3868 4087 3820 -321 -140 127 N
ATOM 160 CA GLY A 11 0.239 30.149 -40.039 1.00 26.35 C
ANISOU 160 CA GLY A 11 3272 3527 3214 -360 -157 143 C
ATOM 161 C GLY A 11 0.076 28.884 -40.864 1.00 26.35 C
ANISOU 161 C GLY A 11 3259 3560 3192 -353 -117 116 C
ATOM 162 O GLY A 11 -0.810 28.795 -41.725 1.00 20.58 O
ANISOU 162 O GLY A 11 2531 2828 2461 -367 -122 113 O
ATOM 163 H GLY A 11 1.334 30.248 -38.391 1.00 37.20 H
ATOM 164 HA2 GLY A 11 -0.598 30.638 -40.067 1.00 31.64 H
ATOM 165 HA3 GLY A 11 0.933 30.689 -40.448 1.00 31.64 H
ATOM 166 N LYS A 12 0.937 27.897 -40.636 1.00 18.26 N
ANISOU 166 N LYS A 12 2223 2565 2151 -330 -80 94 N
ATOM 167 CA LYS A 12 0.847 26.684 -41.436 1.00 21.27 C
ANISOU 167 CA LYS A 12 2592 2977 2512 -319 -48 63 C
ATOM 168 C LYS A 12 -0.433 25.919 -41.145 1.00 30.63 C
ANISOU 168 C LYS A 12 3796 4114 3728 -290 -34 36 C
ATOM 169 O LYS A 12 -0.998 25.299 -42.056 1.00 25.47 O
ANISOU 169 O LYS A 12 3140 3473 3065 -295 -26 20 O
ATOM 170 CB LYS A 12 2.052 25.784 -41.200 1.00 20.96 C
ANISOU 170 CB LYS A 12 2536 2975 2452 -295 -17 42 C
ATOM 171 CG LYS A 12 3.392 26.332 -41.663 1.00 27.15 C
ANISOU 171 CG LYS A 12 3293 3825 3197 -324 -25 65 C
ATOM 172 CD LYS A 12 4.520 25.437 -41.133 1.00 40.52 C
ANISOU 172 CD LYS A 12 4973 5545 4879 -290 5 39 C
ATOM 173 CE LYS A 12 5.842 25.649 -41.861 1.00 52.09 C
ANISOU 173 CE LYS A 12 6401 7094 6295 -315 6 52 C
ATOM 174 NZ LYS A 12 6.561 26.840 -41.352 1.00 67.84 N
ANISOU 174 NZ LYS A 12 8394 9094 8289 -344 -20 96 N
ATOM 175 H LYS A 12 1.561 27.903 -40.044 1.00 21.92 H
ATOM 176 HA LYS A 12 0.852 26.941 -42.371 1.00 25.53 H
ATOM 177 HB2 LYS A 12 2.124 25.618 -40.247 1.00 25.16 H
ATOM 178 HB3 LYS A 12 1.904 24.950 -41.672 1.00 25.16 H
ATOM 179 HG2 LYS A 12 3.428 26.340 -42.633 1.00 32.59 H
ATOM 180 HG3 LYS A 12 3.518 27.231 -41.320 1.00 32.59 H
ATOM 181 HD2 LYS A 12 4.663 25.632 -40.194 1.00 48.64 H
ATOM 182 HD3 LYS A 12 4.264 24.508 -41.245 1.00 48.64 H
ATOM 183 HE2 LYS A 12 6.408 24.872 -41.730 1.00 62.51 H
ATOM 184 HE3 LYS A 12 5.670 25.779 -42.807 1.00 62.51 H
ATOM 185 HZ1 LYS A 12 7.437 26.686 -41.345 1.00 81.42 H
ATOM 186 HZ2 LYS A 12 6.394 27.542 -41.873 1.00 81.42 H
ATOM 187 HZ3 LYS A 12 6.294 27.025 -40.523 1.00 81.42 H
ATOM 188 N VAL A 13 -0.905 25.937 -39.897 1.00 25.17 N
ANISOU 188 N VAL A 13 3121 3371 3070 -263 -33 32 N
ATOM 189 CA VAL A 13 -2.154 25.247 -39.576 1.00 24.53 C
ANISOU 189 CA VAL A 13 3055 3249 3016 -240 -22 11 C
ATOM 190 C VAL A 13 -3.370 26.056 -40.036 1.00 15.82 C
ANISOU 190 C VAL A 13 1961 2124 1928 -260 -50 25 C
ATOM 191 O VAL A 13 -4.379 25.478 -40.468 1.00 18.69 O
ANISOU 191 O VAL A 13 2328 2473 2299 -257 -43 12 O
ATOM 192 CB VAL A 13 -2.220 24.937 -38.068 1.00 16.34 C
ANISOU 192 CB VAL A 13 2028 2175 2004 -205 -9 2 C
ATOM 193 CG1 VAL A 13 -3.485 24.193 -37.727 1.00 20.96 C
ANISOU 193 CG1 VAL A 13 2623 2726 2612 -186 1 -14 C
ATOM 194 CG2 VAL A 13 -1.055 24.117 -37.639 1.00 18.24 C
ANISOU 194 CG2 VAL A 13 2261 2435 2233 -185 14 -12 C
ATOM 195 H VAL A 13 -0.531 26.334 -39.232 1.00 30.21 H
ATOM 196 HA VAL A 13 -2.163 24.405 -40.057 1.00 29.44 H
ATOM 197 HB VAL A 13 -2.206 25.783 -37.594 1.00 19.61 H
ATOM 198 HG11 VAL A 13 -3.435 23.890 -36.807 1.00 25.16 H
ATOM 199 HG12 VAL A 13 -4.241 24.789 -37.838 1.00 25.16 H
ATOM 200 HG13 VAL A 13 -3.573 23.432 -38.322 1.00 25.16 H
ATOM 201 HG21 VAL A 13 -1.362 23.423 -37.036 1.00 21.89 H
ATOM 202 HG22 VAL A 13 -0.645 23.717 -38.422 1.00 21.89 H
ATOM 203 HG23 VAL A 13 -0.416 24.689 -37.187 1.00 21.89 H
ATOM 204 N GLU A 14 -3.319 27.389 -39.917 1.00 21.12 N
ANISOU 204 N GLU A 14 2635 2785 2604 -280 -85 52 N
ATOM 205 CA GLU A 14 -4.408 28.235 -40.404 1.00 23.94 C
ANISOU 205 CA GLU A 14 3000 3120 2976 -300 -118 66 C
ATOM 206 C GLU A 14 -4.795 27.891 -41.840 1.00 22.29 C
ANISOU 206 C GLU A 14 2784 2938 2748 -328 -117 66 C
ATOM 207 O GLU A 14 -5.973 27.774 -42.161 1.00 17.00 O
ANISOU 207 O GLU A 14 2120 2245 2092 -327 -122 60 O
ATOM 208 CB GLU A 14 -4.013 29.726 -40.316 1.00 25.55 C
ANISOU 208 CB GLU A 14 3207 3316 3185 -325 -165 98 C
ATOM 209 CG GLU A 14 -3.854 30.237 -38.866 1.00 25.20 C
ANISOU 209 CG GLU A 14 3173 3238 3164 -296 -174 94 C
ATOM 210 CD GLU A 14 -3.272 31.661 -38.774 1.00 23.31 C
ANISOU 210 CD GLU A 14 2938 2991 2929 -320 -225 125 C
ATOM 211 OE1 GLU A 14 -3.777 32.564 -39.463 1.00 23.02 O
ANISOU 211 OE1 GLU A 14 2905 2941 2899 -348 -269 145 O
ATOM 212 OE2 GLU A 14 -2.317 31.868 -37.989 1.00 19.24 O
ANISOU 212 OE2 GLU A 14 2422 2478 2411 -311 -225 131 O
ATOM 213 H GLU A 14 -2.669 27.825 -39.560 1.00 25.35 H
ATOM 214 HA GLU A 14 -5.178 28.084 -39.833 1.00 28.74 H
ATOM 215 HB2 GLU A 14 -3.165 29.852 -40.770 1.00 30.67 H
ATOM 216 HB3 GLU A 14 -4.701 30.258 -40.745 1.00 30.67 H
ATOM 217 HG2 GLU A 14 -4.726 30.245 -38.440 1.00 30.25 H
ATOM 218 HG3 GLU A 14 -3.257 29.641 -38.388 1.00 30.25 H
ATOM 219 N GLY A 15 -3.816 27.763 -42.733 1.00 22.53 N
ANISOU 219 N GLY A 15 2798 3020 2742 -353 -112 75 N
ATOM 220 CA GLY A 15 -4.183 27.449 -44.103 1.00 25.97 C
ANISOU 220 CA GLY A 15 3226 3486 3155 -378 -111 74 C
ATOM 221 C GLY A 15 -4.820 26.090 -44.295 1.00 20.83 C
ANISOU 221 C GLY A 15 2578 2830 2508 -352 -79 38 C
ATOM 222 O GLY A 15 -5.224 25.757 -45.414 1.00 19.92 O
ANISOU 222 O GLY A 15 2457 2736 2375 -370 -78 32 O
ATOM 223 H GLY A 15 -2.975 27.851 -42.574 1.00 27.05 H
ATOM 224 HA2 GLY A 15 -4.811 28.118 -44.418 1.00 31.17 H
ATOM 225 HA3 GLY A 15 -3.384 27.482 -44.653 1.00 31.17 H
ATOM 226 N CYS A 16 -4.953 25.300 -43.236 1.00 18.12 N
ANISOU 226 N CYS A 16 2243 2456 2186 -312 -55 14 N
ATOM 227 CA CYS A 16 -5.579 23.981 -43.338 1.00 20.80 C
ANISOU 227 CA CYS A 16 2587 2782 2533 -289 -30 -16 C
ATOM 228 C CYS A 16 -6.979 23.908 -42.738 1.00 20.19 C
ANISOU 228 C CYS A 16 2524 2654 2491 -276 -35 -18 C
ATOM 229 O CYS A 16 -7.601 22.846 -42.780 1.00 20.59 O
ANISOU 229 O CYS A 16 2581 2691 2552 -260 -19 -38 O
ATOM 230 CB CYS A 16 -4.695 22.946 -42.652 1.00 20.56 C
ANISOU 230 CB CYS A 16 2553 2758 2499 -256 -2 -40 C
ATOM 231 SG CYS A 16 -3.059 22.734 -43.375 1.00 23.56 S
ANISOU 231 SG CYS A 16 2910 3206 2834 -263 9 -48 S
ATOM 232 H CYS A 16 -4.688 25.505 -42.444 1.00 21.75 H
ATOM 233 HA CYS A 16 -5.659 23.762 -44.280 1.00 24.97 H
ATOM 234 HB2 CYS A 16 -4.572 23.213 -41.728 1.00 24.68 H
ATOM 235 HB3 CYS A 16 -5.144 22.087 -42.692 1.00 24.68 H
ATOM 236 HG CYS A 16 -2.712 23.772 -43.866 1.00 28.28 H
ATOM 237 N MET A 17 -7.480 24.968 -42.136 1.00 24.47 N
ANISOU 237 N MET A 17 3074 3171 3055 -279 -57 0 N
ATOM 238 CA MET A 17 -8.752 24.873 -41.430 1.00 20.50 C
ANISOU 238 CA MET A 17 2578 2627 2582 -261 -58 -5 C
ATOM 239 C MET A 17 -9.910 25.117 -42.391 1.00 16.51 C
ANISOU 239 C MET A 17 2076 2116 2084 -282 -76 0 C
ATOM 240 O MET A 17 -9.885 26.063 -43.184 1.00 18.75 O
ANISOU 240 O MET A 17 2357 2409 2358 -311 -104 19 O
ATOM 241 CB MET A 17 -8.813 25.859 -40.267 1.00 20.11 C
ANISOU 241 CB MET A 17 2532 2555 2553 -247 -75 5 C
ATOM 242 CG MET A 17 -7.732 25.620 -39.221 1.00 22.29 C
ANISOU 242 CG MET A 17 2808 2836 2826 -225 -57 1 C
ATOM 243 SD MET A 17 -7.648 23.914 -38.598 1.00 20.86 S
ANISOU 243 SD MET A 17 2627 2652 2647 -197 -17 -23 S
ATOM 244 CE MET A 17 -9.336 23.728 -37.987 1.00 19.22 C
ANISOU 244 CE MET A 17 2423 2414 2467 -184 -18 -26 C
ATOM 245 H MET A 17 -7.111 25.745 -42.120 1.00 29.38 H
ATOM 246 HA MET A 17 -8.831 23.979 -41.063 1.00 24.61 H
ATOM 247 HB2 MET A 17 -8.701 26.759 -40.612 1.00 24.14 H
ATOM 248 HB3 MET A 17 -9.675 25.776 -39.830 1.00 24.14 H
ATOM 249 HG2 MET A 17 -6.870 25.831 -39.613 1.00 26.76 H
ATOM 250 HG3 MET A 17 -7.902 26.200 -38.462 1.00 26.76 H
ATOM 251 HE1 MET A 17 -9.311 23.323 -37.106 1.00 23.08 H
ATOM 252 HE2 MET A 17 -9.752 24.603 -37.936 1.00 23.08 H
ATOM 253 HE3 MET A 17 -9.833 23.161 -38.597 1.00 23.08 H
ATOM 254 N VAL A 18 -10.908 24.236 -42.329 1.00 19.40 N
ANISOU 254 N VAL A 18 2445 2464 2463 -270 -63 -14 N
ATOM 255 CA VAL A 18 -12.138 24.385 -43.085 1.00 23.22 C
ANISOU 255 CA VAL A 18 2930 2937 2956 -286 -79 -10 C
ATOM 256 C VAL A 18 -13.315 24.204 -42.136 1.00 17.34 C
ANISOU 256 C VAL A 18 2186 2163 2240 -265 -76 -14 C
ATOM 257 O VAL A 18 -13.187 23.769 -40.989 1.00 16.32 O
ANISOU 257 O VAL A 18 2055 2026 2118 -240 -58 -21 O
ATOM 258 CB VAL A 18 -12.254 23.390 -44.285 1.00 17.86 C
ANISOU 258 CB VAL A 18 2251 2274 2259 -301 -68 -22 C
ATOM 259 CG1 VAL A 18 -11.143 23.609 -45.295 1.00 22.05 C
ANISOU 259 CG1 VAL A 18 2775 2846 2756 -324 -71 -18 C
ATOM 260 CG2 VAL A 18 -12.229 21.928 -43.805 1.00 23.32 C
ANISOU 260 CG2 VAL A 18 2946 2957 2955 -276 -40 -43 C
ATOM 261 H VAL A 18 -10.889 23.528 -41.840 1.00 23.29 H
ATOM 262 HA VAL A 18 -12.164 25.285 -43.447 1.00 27.88 H
ATOM 263 HB VAL A 18 -13.105 23.561 -44.719 1.00 21.44 H
ATOM 264 HG11 VAL A 18 -11.405 23.215 -46.142 1.00 26.47 H
ATOM 265 HG12 VAL A 18 -10.999 24.562 -45.404 1.00 26.47 H
ATOM 266 HG13 VAL A 18 -10.333 23.187 -44.970 1.00 26.47 H
ATOM 267 HG21 VAL A 18 -12.587 21.359 -44.505 1.00 27.99 H
ATOM 268 HG22 VAL A 18 -11.313 21.675 -43.610 1.00 27.99 H
ATOM 269 HG23 VAL A 18 -12.771 21.849 -43.005 1.00 27.99 H
ATOM 270 N GLN A 19 -14.471 24.546 -42.651 1.00 17.02 N
ANISOU 270 N GLN A 19 2144 2111 2210 -277 -93 -10 N
ATOM 271 CA GLN A 19 -15.757 24.373 -42.010 1.00 26.25 C
ANISOU 271 CA GLN A 19 3310 3262 3403 -261 -92 -13 C
ATOM 272 C GLN A 19 -16.437 23.138 -42.578 1.00 21.80 C
ANISOU 272 C GLN A 19 2748 2697 2838 -269 -78 -20 C
ATOM 273 O GLN A 19 -16.493 22.965 -43.801 1.00 26.80 O
ANISOU 273 O GLN A 19 3386 3337 3460 -292 -85 -19 O
ATOM 274 CB GLN A 19 -16.591 25.614 -42.295 1.00 27.13 C
ANISOU 274 CB GLN A 19 3418 3362 3529 -270 -127 -4 C
ATOM 275 CG GLN A 19 -17.910 25.661 -41.686 1.00 30.46 C
ANISOU 275 CG GLN A 19 3831 3773 3972 -253 -131 -10 C
ATOM 276 CD GLN A 19 -18.569 26.992 -41.953 1.00 34.59 C
ANISOU 276 CD GLN A 19 4351 4283 4510 -256 -171 -5 C
ATOM 277 OE1 GLN A 19 -18.030 27.850 -42.683 1.00 43.90 O
ANISOU 277 OE1 GLN A 19 5537 5458 5684 -278 -200 7 O
ATOM 278 NE2 GLN A 19 -19.724 27.184 -41.358 1.00 38.23 N
ANISOU 278 NE2 GLN A 19 4799 4738 4990 -237 -177 -13 N
ATOM 279 H GLN A 19 -14.544 24.907 -43.428 1.00 20.43 H
ATOM 280 HA GLN A 19 -15.667 24.244 -41.053 1.00 31.51 H
ATOM 281 HB2 GLN A 19 -16.101 26.387 -41.972 1.00 32.57 H
ATOM 282 HB3 GLN A 19 -16.718 25.678 -43.254 1.00 32.57 H
ATOM 283 HG2 GLN A 19 -18.466 24.960 -42.062 1.00 36.57 H
ATOM 284 HG3 GLN A 19 -17.829 25.542 -40.727 1.00 36.57 H
ATOM 285 HE21 GLN A 19 -20.056 26.571 -40.855 1.00 45.89 H
ATOM 286 HE22 GLN A 19 -20.148 27.924 -41.471 1.00 45.89 H
ATOM 287 N VAL A 20 -16.952 22.278 -41.701 1.00 27.63 N
ANISOU 287 N VAL A 20 3483 3428 3588 -252 -60 -24 N
ATOM 288 CA VAL A 20 -17.688 21.090 -42.125 1.00 18.93 C
ANISOU 288 CA VAL A 20 2384 2319 2490 -260 -52 -28 C
ATOM 289 C VAL A 20 -19.095 21.165 -41.559 1.00 25.29 C
ANISOU 289 C VAL A 20 3177 3118 3314 -255 -57 -20 C
ATOM 290 O VAL A 20 -19.284 21.333 -40.348 1.00 22.69 O
ANISOU 290 O VAL A 20 2837 2792 2992 -236 -50 -18 O
ATOM 291 CB VAL A 20 -16.986 19.794 -41.709 1.00 23.84 C
ANISOU 291 CB VAL A 20 3012 2939 3108 -249 -32 -36 C
ATOM 292 CG1 VAL A 20 -17.753 18.588 -42.221 1.00 18.90 C
ANISOU 292 CG1 VAL A 20 2392 2301 2489 -259 -32 -39 C
ATOM 293 CG2 VAL A 20 -15.568 19.825 -42.227 1.00 19.54 C
ANISOU 293 CG2 VAL A 20 2474 2407 2542 -249 -27 -47 C
ATOM 294 H VAL A 20 -16.886 22.366 -40.848 1.00 33.17 H
ATOM 295 HA VAL A 20 -17.754 21.091 -43.092 1.00 22.72 H
ATOM 296 HB VAL A 20 -16.959 19.714 -40.743 1.00 28.62 H
ATOM 297 HG11 VAL A 20 -17.578 17.832 -41.640 1.00 22.69 H
ATOM 298 HG12 VAL A 20 -18.701 18.794 -42.220 1.00 22.69 H
ATOM 299 HG13 VAL A 20 -17.460 18.387 -43.124 1.00 22.69 H
ATOM 300 HG21 VAL A 20 -15.091 19.051 -41.888 1.00 23.45 H
ATOM 301 HG22 VAL A 20 -15.585 19.804 -43.196 1.00 23.45 H
ATOM 302 HG23 VAL A 20 -15.138 20.638 -41.921 1.00 23.45 H
ATOM 303 N THR A 21 -20.078 21.055 -42.435 1.00 25.76 N
ANISOU 303 N THR A 21 3237 3173 3379 -273 -69 -16 N
ATOM 304 CA THR A 21 -21.477 21.115 -42.055 1.00 28.18 C
ANISOU 304 CA THR A 21 3528 3478 3701 -272 -75 -9 C
ATOM 305 C THR A 21 -22.181 19.841 -42.509 1.00 35.75 C
ANISOU 305 C THR A 21 4492 4430 4664 -288 -71 -5 C
ATOM 306 O THR A 21 -21.951 19.332 -43.615 1.00 28.71 O
ANISOU 306 O THR A 21 3614 3530 3764 -305 -76 -10 O
ATOM 307 CB THR A 21 -22.161 22.352 -42.651 1.00 34.23 C
ANISOU 307 CB THR A 21 4289 4243 4475 -279 -101 -7 C
ATOM 308 OG1 THR A 21 -21.585 23.537 -42.088 1.00 32.58 O
ANISOU 308 OG1 THR A 21 4076 4036 4266 -262 -112 -10 O
ATOM 309 CG2 THR A 21 -23.623 22.346 -42.336 1.00 35.79 C
ANISOU 309 CG2 THR A 21 4469 4444 4688 -276 -107 -2 C
ATOM 310 H THR A 21 -19.953 20.942 -43.279 1.00 30.93 H
ATOM 311 HA THR A 21 -21.556 21.173 -41.090 1.00 33.82 H
ATOM 312 HB THR A 21 -22.044 22.347 -43.614 1.00 41.09 H
ATOM 313 HG1 THR A 21 -21.064 23.895 -42.642 1.00 39.10 H
ATOM 314 HG21 THR A 21 -23.963 23.255 -42.326 1.00 42.96 H
ATOM 315 HG22 THR A 21 -24.105 21.836 -43.005 1.00 42.96 H
ATOM 316 HG23 THR A 21 -23.773 21.945 -41.466 1.00 42.96 H
ATOM 317 N CYS A 22 -23.017 19.317 -41.631 1.00 35.75 N
ANISOU 317 N CYS A 22 4477 4433 4672 -283 -64 4 N
ATOM 318 CA CYS A 22 -23.796 18.113 -41.911 1.00 24.56 C
ANISOU 318 CA CYS A 22 3062 3008 3262 -300 -65 14 C
ATOM 319 C CYS A 22 -25.114 18.328 -41.177 1.00 43.34 C
ANISOU 319 C CYS A 22 5415 5404 5650 -299 -67 28 C
ATOM 320 O CYS A 22 -25.141 18.363 -39.938 1.00 39.66 O
ANISOU 320 O CYS A 22 4932 4956 5182 -283 -55 33 O
ATOM 321 CB CYS A 22 -23.050 16.861 -41.441 1.00 26.48 C
ANISOU 321 CB CYS A 22 3318 3242 3504 -298 -54 14 C
ATOM 322 SG CYS A 22 -23.543 15.327 -42.194 1.00 54.57 S
ANISOU 322 SG CYS A 22 6890 6775 7069 -321 -67 19 S
ATOM 323 H CYS A 22 -23.157 19.642 -40.847 1.00 42.91 H
ATOM 324 HA CYS A 22 -23.967 17.993 -42.858 1.00 29.48 H
ATOM 325 HB2 CYS A 22 -22.106 16.982 -41.631 1.00 31.79 H
ATOM 326 HB3 CYS A 22 -23.187 16.768 -40.486 1.00 31.79 H
ATOM 327 HG CYS A 22 -24.459 14.864 -41.572 1.00 65.49 H
ATOM 328 N GLY A 23 -26.182 18.559 -41.938 1.00 43.87 N
ANISOU 328 N GLY A 23 5475 5471 5724 -314 -82 33 N
ATOM 329 CA GLY A 23 -27.448 18.947 -41.342 1.00 36.29 C
ANISOU 329 CA GLY A 23 4485 4533 4771 -310 -86 42 C
ATOM 330 C GLY A 23 -27.356 20.299 -40.667 1.00 50.69 C
ANISOU 330 C GLY A 23 6292 6374 6594 -281 -87 29 C
ATOM 331 O GLY A 23 -26.992 21.308 -41.284 1.00 62.11 O
ANISOU 331 O GLY A 23 7747 7808 8042 -276 -102 17 O
ATOM 332 H GLY A 23 -26.199 18.497 -42.796 1.00 52.66 H
ATOM 333 HA2 GLY A 23 -28.130 18.992 -42.031 1.00 43.56 H
ATOM 334 HA3 GLY A 23 -27.711 18.289 -40.680 1.00 43.56 H
ATOM 335 N THR A 24 -27.689 20.343 -39.379 1.00 60.68 N
ANISOU 335 N THR A 24 7532 7669 7855 -263 -76 31 N
ATOM 336 CA THR A 24 -27.646 21.585 -38.619 1.00 71.42 C
ANISOU 336 CA THR A 24 8874 9047 9214 -230 -80 14 C
ATOM 337 C THR A 24 -26.338 21.765 -37.863 1.00 59.80 C
ANISOU 337 C THR A 24 7415 7574 7735 -212 -67 5 C
ATOM 338 O THR A 24 -26.065 22.870 -37.383 1.00 61.06 O
ANISOU 338 O THR A 24 7566 7738 7894 -185 -76 -12 O
ATOM 339 CB THR A 24 -28.815 21.644 -37.619 1.00 78.55 C
ANISOU 339 CB THR A 24 9737 9994 10114 -217 -74 16 C
ATOM 340 OG1 THR A 24 -28.786 22.880 -36.880 1.00 69.96 O
ANISOU 340 OG1 THR A 24 8630 8925 9025 -179 -82 -8 O
ATOM 341 CG2 THR A 24 -28.720 20.482 -36.647 1.00 86.10 C
ANISOU 341 CG2 THR A 24 10683 10973 11057 -226 -51 36 C
ATOM 342 H THR A 24 -27.944 19.660 -38.922 1.00 72.83 H
ATOM 343 HA THR A 24 -27.746 22.327 -39.235 1.00 85.71 H
ATOM 344 HB THR A 24 -29.653 21.590 -38.104 1.00 94.27 H
ATOM 345 HG1 THR A 24 -29.391 22.881 -36.297 1.00 83.96 H
ATOM 346 HG21 THR A 24 -29.533 20.422 -36.121 1.00103.33 H
ATOM 347 HG22 THR A 24 -28.599 19.651 -37.133 1.00103.33 H
ATOM 348 HG23 THR A 24 -27.967 20.609 -36.049 1.00103.33 H
ATOM 349 N THR A 25 -25.541 20.715 -37.735 1.00 40.45 N
ANISOU 349 N THR A 25 4981 5112 5277 -224 -50 15 N
ATOM 350 CA THR A 25 -24.313 20.791 -36.961 1.00 39.03 C
ANISOU 350 CA THR A 25 4810 4932 5089 -207 -38 9 C
ATOM 351 C THR A 25 -23.192 21.341 -37.831 1.00 24.50 C
ANISOU 351 C THR A 25 2996 3064 3248 -209 -47 -2 C
ATOM 352 O THR A 25 -22.942 20.837 -38.929 1.00 30.92 O
ANISOU 352 O THR A 25 3829 3858 4062 -230 -51 1 O
ATOM 353 CB THR A 25 -23.909 19.417 -36.432 1.00 42.61 C
ANISOU 353 CB THR A 25 5269 5384 5537 -219 -20 25 C
ATOM 354 OG1 THR A 25 -25.018 18.815 -35.767 1.00 44.66 O
ANISOU 354 OG1 THR A 25 5503 5671 5794 -228 -15 42 O
ATOM 355 CG2 THR A 25 -22.732 19.548 -35.464 1.00 44.59 C
ANISOU 355 CG2 THR A 25 5525 5638 5779 -199 -7 18 C
ATOM 356 H THR A 25 -25.689 19.945 -38.088 1.00 48.55 H
ATOM 357 HA THR A 25 -24.458 21.380 -36.204 1.00 46.85 H
ATOM 358 HB THR A 25 -23.636 18.848 -37.168 1.00 51.14 H
ATOM 359 HG1 THR A 25 -24.872 17.997 -35.648 1.00 53.60 H
ATOM 360 HG21 THR A 25 -22.881 18.992 -34.683 1.00 53.52 H
ATOM 361 HG22 THR A 25 -21.912 19.267 -35.899 1.00 53.52 H
ATOM 362 HG23 THR A 25 -22.637 20.471 -35.180 1.00 53.52 H
ATOM 363 N THR A 26 -22.508 22.367 -37.342 1.00 23.62 N
ANISOU 363 N THR A 26 2885 2955 3135 -187 -52 -14 N
ATOM 364 CA THR A 26 -21.283 22.817 -37.985 1.00 20.81 C
ANISOU 364 CA THR A 26 2552 2580 2775 -191 -59 -19 C
ATOM 365 C THR A 26 -20.122 22.618 -37.030 1.00 23.60 C
ANISOU 365 C THR A 26 2910 2938 3119 -176 -42 -22 C
ATOM 366 O THR A 26 -20.263 22.793 -35.815 1.00 28.11 O
ANISOU 366 O THR A 26 3465 3525 3688 -154 -34 -25 O
ATOM 367 CB THR A 26 -21.362 24.293 -38.400 1.00 30.43 C
ANISOU 367 CB THR A 26 3770 3792 4001 -185 -89 -28 C
ATOM 368 OG1 THR A 26 -22.231 24.424 -39.526 1.00 41.56 O
ANISOU 368 OG1 THR A 26 5180 5192 5418 -205 -107 -23 O
ATOM 369 CG2 THR A 26 -19.997 24.831 -38.818 1.00 42.31 C
ANISOU 369 CG2 THR A 26 5294 5284 5499 -191 -97 -28 C
ATOM 370 H THR A 26 -22.734 22.813 -36.643 1.00 28.35 H
ATOM 371 HA THR A 26 -21.130 22.294 -38.788 1.00 24.98 H
ATOM 372 HB THR A 26 -21.686 24.804 -37.642 1.00 36.53 H