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1FTM.pdb
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HEADER MEMBRANE PROTEIN 12-SEP-00 1FTM
TITLE CRYSTAL STRUCTURE OF THE GLUR2 LIGAND BINDING CORE (S1S2J)
TITLE 2 IN COMPLEX WITH AMPA AT 1.7 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR SUBUNIT 2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: GLUR2-FLOP LIGAND BINDING CORE (S1S2J);
COMPND 5 SYNONYM: GLUR-2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET30B
KEYWDS AMPA RECEPTOR, GLUR2, S1S2, LIGAND-BINDING CORE, AGONIST,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.GOUAUX,N.ARMSTRONG
REVDAT 2 24-FEB-09 1FTM 1 VERSN
REVDAT 1 01-NOV-00 1FTM 0
JRNL AUTH N.ARMSTRONG,E.GOUAUX
JRNL TITL MECHANISMS FOR ACTIVATION AND ANTAGONISM OF AN
JRNL TITL 2 AMPA-SENSITIVE GLUTAMATE RECEPTOR: CRYSTAL
JRNL TITL 3 STRUCTURES OF THE GLUR2 LIGAND BINDING CORE.
JRNL REF NEURON V. 28 165 2000
JRNL REFN ISSN 0896-6273
JRNL PMID 11086992
JRNL DOI 10.1016/S0896-6273(00)00094-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.Q.CHEN,Y.SUN,R.JIN,E.GOUAUX
REMARK 1 TITL PROBING THE LIGAND BINDING DOMAIN OF THE GLUR2
REMARK 1 TITL 2 RECEPTOR BY PROTEOLYSIS AND DELETION MUTAGENESIS
REMARK 1 TITL 3 DEFINES DOMAIN BOUNDARIES AND YIELDS A
REMARK 1 TITL 4 CRYSTALLIZABLE CONSTRUCT
REMARK 1 REF PROTEIN SCI. V. 7 2623 1998
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 90858
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 9073
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5866
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.45
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FTM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB011890.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-99
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91073
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 5.530
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.03
REMARK 200 R MERGE FOR SHELL (I) : 0.10800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 8000 0.2 M ZINC ACETATE
REMARK 280 0.1 M CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 56.90000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.58500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.58500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -181.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 56.90000
REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 81.58500
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 94.36000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 170.70000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 81.58500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 94.36000
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 GLY A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 3
REMARK 465 GLY A 262
REMARK 465 SER A 263
REMARK 465 GLY B 1
REMARK 465 ALA B 2
REMARK 465 ASN B 3
REMARK 465 GLY B 262
REMARK 465 SER B 263
REMARK 465 GLY C 1
REMARK 465 ALA C 2
REMARK 465 ASN C 3
REMARK 465 GLY C 262
REMARK 465 SER C 263
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 4 CB CG CD CE NZ
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 ALA A 66 CB
REMARK 470 ASP A 67 CB CG OD1 OD2
REMARK 470 THR A 68 OG1 CG2
REMARK 470 GLU A 122 CB CG CD OE1 OE2
REMARK 470 THR A 131 CB OG1 CG2
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 ILE A 152 CD1
REMARK 470 ALA A 153 CB
REMARK 470 ASP A 156 CB CG OD1 OD2
REMARK 470 ARG A 172 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 183 CG CD CE NZ
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 CYS A 261 O
REMARK 470 LYS B 4 CG CD CE NZ
REMARK 470 GLU B 27 CG CD OE1 OE2
REMARK 470 ALA B 66 CB
REMARK 470 ASP B 67 CB CG OD1 OD2
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 GLU B 125 CG CD OE1 OE2
REMARK 470 LYS B 151 CG CD CE NZ
REMARK 470 LYS B 157 CG CD CE NZ
REMARK 470 LYS B 183 CG CD CE NZ
REMARK 470 CYS B 261 O
REMARK 470 LYS C 4 CG CD CE NZ
REMARK 470 LYS C 21 CG CD CE NZ
REMARK 470 GLU C 24 CG CD OE1 OE2
REMARK 470 MET C 25 CG SD CE
REMARK 470 GLU C 27 CG CD OE1 OE2
REMARK 470 GLU C 30 CG CD OE1 OE2
REMARK 470 ASP C 67 CG OD1 OD2
REMARK 470 GLU C 122 CG CD OE1 OE2
REMARK 470 GLU C 125 CB CG CD OE1 OE2
REMARK 470 GLN C 130 CB CG CD OE1 NE2
REMARK 470 GLU C 132 CG CD OE1 OE2
REMARK 470 ARG C 149 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 151 CG CD CE NZ
REMARK 470 ALA C 153 CB
REMARK 470 LYS C 157 CG CD CE NZ
REMARK 470 ARG C 163 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 172 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 183 CG CD CE NZ
REMARK 470 LYS C 185 CG CD CE NZ
REMARK 470 LYS C 187 CG CD CE NZ
REMARK 470 GLN C 244 CG CD OE1 NE2
REMARK 470 LYS C 249 CG CD CE NZ
REMARK 470 LYS C 258 CB CG CD CE NZ
REMARK 470 CYS C 261 O
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 ALA A 66 -84.73 -35.12
REMARK 500 PRO A 205 22.41 -77.89
REMARK 500 PRO C 120 47.90 -65.19
REMARK 500 ALA C 153 -59.19 -26.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 422 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 NE2
REMARK 620 2 GLU B 166 OE1 83.8
REMARK 620 3 GLU B 166 OE2 118.0 53.6
REMARK 620 4 GLU A 42 OE1 95.0 142.8 96.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 423 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 23 NE2
REMARK 620 2 HOH B 554 O 102.3
REMARK 620 3 GLU B 30 OE2 118.0 111.6
REMARK 620 4 HIS C 23 NE2 107.7 112.4 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 425 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 NE2
REMARK 620 2 GLU B 42 OE1 92.4
REMARK 620 3 HOH A 435 O 116.9 111.0
REMARK 620 4 GLU A 166 OE2 113.6 104.5 115.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 424 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 65 OD2
REMARK 620 2 ASP C 65 OD1 51.1
REMARK 620 3 HOH A 517 O 101.1 100.9
REMARK 620 4 HIS A 23 NE2 102.5 151.8 93.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 426 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 46 NE2
REMARK 620 2 GLU C 42 OE1 103.5
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 422
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 423
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 424
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 425
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 426
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMQ C 427
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMQ A 428
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMQ B 429
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GR2 RELATED DB: PDB
REMARK 900 GLUR2 S1S2I IN COMPLEX WITH THE PARTIAL AGONIST KAINATE
REMARK 900 RELATED ID: 1FTJ RELATED DB: PDB
REMARK 900 GLUR2 S1S2J IN COMPLEX WITH THE FULL AGONIST GLUTAMATE
REMARK 900 RELATED ID: 1FTK RELATED DB: PDB
REMARK 900 GLUR2 S1S2I IN COMPLEX WITH THE PARTIAL AGONIST KAINATE AT
REMARK 900 PH 6.5 AND 1.6 A RESOLUTION
REMARK 900 RELATED ID: 1FTL RELATED DB: PDB
REMARK 900 GLUR2 S1S2J IN COMPLEX WITH THE ANTAGONIST DNQX
REMARK 900 RELATED ID: 1FTO RELATED DB: PDB
REMARK 900 GLUR2 LIGAND BINDING CORE (S1S2J) IN THE APO STATE
REMARK 900 RELATED ID: 1FW0 RELATED DB: PDB
REMARK 900 GLUR2 LIGAND BINDING CORE (S1S2J) IN COMPLEX WITH KAINATE
DBREF 1FTM A 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 1FTM A 120 263 UNP P19491 GRIA2_RAT 653 796
DBREF 1FTM B 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 1FTM B 120 263 UNP P19491 GRIA2_RAT 653 796
DBREF 1FTM C 3 117 UNP P19491 GRIA2_RAT 413 527
DBREF 1FTM C 120 263 UNP P19491 GRIA2_RAT 653 796
SEQADV 1FTM GLY A 1 UNP P19491 CLONING ARTIFACT
SEQADV 1FTM ALA A 2 UNP P19491 CLONING ARTIFACT
SEQADV 1FTM GLY B 1 UNP P19491 CLONING ARTIFACT
SEQADV 1FTM ALA B 2 UNP P19491 CLONING ARTIFACT
SEQADV 1FTM GLY C 1 UNP P19491 CLONING ARTIFACT
SEQADV 1FTM ALA C 2 UNP P19491 CLONING ARTIFACT
SEQADV 1FTM GLY A 118 UNP P19491 LINKER
SEQADV 1FTM THR A 119 UNP P19491 LINKER
SEQADV 1FTM GLY B 118 UNP P19491 LINKER
SEQADV 1FTM THR B 119 UNP P19491 LINKER
SEQADV 1FTM GLY C 118 UNP P19491 LINKER
SEQADV 1FTM THR C 119 UNP P19491 LINKER
SEQRES 1 A 263 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 A 263 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 A 263 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 A 263 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 A 263 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 A 263 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 A 263 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 A 263 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 A 263 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 A 263 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 A 263 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 A 263 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 A 263 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 A 263 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 A 263 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 A 263 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 A 263 MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 A 263 ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL
SEQRES 19 A 263 ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU
SEQRES 20 A 263 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 A 263 CYS GLY SER
SEQRES 1 B 263 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 B 263 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 B 263 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 B 263 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 B 263 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 B 263 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 B 263 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 B 263 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 B 263 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 B 263 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 B 263 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 B 263 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 B 263 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 B 263 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 B 263 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 B 263 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 B 263 MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 B 263 ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL
SEQRES 19 B 263 ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU
SEQRES 20 B 263 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 B 263 CYS GLY SER
SEQRES 1 C 263 GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU
SEQRES 2 C 263 SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU
SEQRES 3 C 263 GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU
SEQRES 4 C 263 ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS
SEQRES 5 C 263 LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP
SEQRES 6 C 263 ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU
SEQRES 7 C 263 VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR
SEQRES 8 C 263 ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS
SEQRES 9 C 263 PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS
SEQRES 10 C 263 GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN
SEQRES 11 C 263 THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR
SEQRES 12 C 263 LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP
SEQRES 13 C 263 LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL
SEQRES 14 C 263 PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG
SEQRES 15 C 263 LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR
SEQRES 16 C 263 MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR
SEQRES 17 C 263 MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY
SEQRES 18 C 263 ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL
SEQRES 19 C 263 ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU
SEQRES 20 C 263 ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU
SEQRES 21 C 263 CYS GLY SER
HET ZN A 422 1
HET ZN B 423 1
HET ZN C 424 1
HET ZN B 425 1
HET ZN C 426 1
HET AMQ C 427 13
HET AMQ A 428 13
HET AMQ B 429 13
HETNAM ZN ZINC ION
HETNAM AMQ (S)-ALPHA-AMINO-3-HYDROXY-5-METHYL-4-
HETNAM 2 AMQ ISOXAZOLEPROPIONIC ACID
HETSYN AMQ AMPA
FORMUL 4 ZN 5(ZN 2+)
FORMUL 9 AMQ 3(C7 H10 N2 O4)
FORMUL 12 HOH *420(H2 O)
HELIX 1 1 ASN A 22 LEU A 26 5 5
HELIX 2 2 GLU A 27 GLU A 30 5 4
HELIX 3 3 GLY A 34 GLY A 48 1 15
HELIX 4 4 ASN A 72 TYR A 80 1 9
HELIX 5 5 THR A 93 GLU A 98 1 6
HELIX 6 6 SER A 123 LYS A 129 1 7
HELIX 7 7 GLY A 141 SER A 150 1 10
HELIX 8 8 ILE A 152 ALA A 165 1 14
HELIX 9 9 THR A 173 SER A 184 1 12
HELIX 10 10 SER A 194 GLN A 202 1 9
HELIX 11 11 LEU A 230 GLN A 244 1 15
HELIX 12 12 GLY A 245 TYR A 256 1 12
HELIX 13 13 GLY B 28 GLU B 30 5 3
HELIX 14 14 GLY B 34 GLY B 48 1 15
HELIX 15 15 ASN B 72 TYR B 80 1 9
HELIX 16 16 THR B 93 GLU B 98 1 6
HELIX 17 17 SER B 123 LYS B 129 1 7
HELIX 18 18 GLY B 141 SER B 150 1 10
HELIX 19 19 ILE B 152 ALA B 165 1 14
HELIX 20 20 THR B 173 SER B 184 1 12
HELIX 21 21 SER B 194 GLN B 202 1 9
HELIX 22 22 LEU B 230 GLN B 244 1 15
HELIX 23 23 GLY B 245 TYR B 256 1 12
HELIX 24 24 ASN C 22 LEU C 26 5 5
HELIX 25 25 GLU C 27 GLU C 30 5 4
HELIX 26 26 GLY C 34 GLY C 48 1 15
HELIX 27 27 ASN C 72 TYR C 80 1 9
HELIX 28 28 THR C 93 GLU C 98 1 6
HELIX 29 29 SER C 123 LYS C 129 1 7
HELIX 30 30 GLY C 141 ARG C 149 1 9
HELIX 31 31 ILE C 152 ALA C 165 1 14
HELIX 32 32 THR C 173 SER C 184 1 12
HELIX 33 33 SER C 194 GLN C 202 1 9
HELIX 34 34 LEU C 230 GLN C 244 1 15
HELIX 35 35 GLY C 245 TYR C 256 1 12
SHEET 1 A 3 TYR A 51 ILE A 55 0
SHEET 2 A 3 VAL A 6 THR A 10 1 O VAL A 6 N LYS A 52
SHEET 3 A 3 ILE A 85 ALA A 86 1 O ILE A 85 N THR A 9
SHEET 1 B 2 MET A 18 MET A 19 0
SHEET 2 B 2 TYR A 32 GLU A 33 -1 N GLU A 33 O MET A 18
SHEET 1 C 2 ILE A 100 PHE A 102 0
SHEET 2 C 2 ALA A 223 PRO A 225 -1 O THR A 224 N ASP A 101
SHEET 1 D 2 MET A 107 LEU A 109 0
SHEET 2 D 2 LYS A 218 TYR A 220 -1 N LYS A 218 O LEU A 109
SHEET 1 E 4 ALA A 134 GLY A 136 0
SHEET 2 E 4 TYR A 188 GLU A 193 1 N ALA A 189 O ALA A 134
SHEET 3 E 4 ILE A 111 LYS A 116 -1 N SER A 112 O LEU A 192
SHEET 4 E 4 THR A 208 VAL A 211 -1 O MET A 209 N ILE A 115
SHEET 1 F 3 TYR B 51 ILE B 55 0
SHEET 2 F 3 VAL B 6 THR B 10 1 O VAL B 6 N LYS B 52
SHEET 3 F 3 ILE B 85 ALA B 86 1 O ILE B 85 N THR B 9
SHEET 1 G 2 MET B 18 MET B 19 0
SHEET 2 G 2 TYR B 32 GLU B 33 -1 O GLU B 33 N MET B 18
SHEET 1 H 2 ILE B 100 PHE B 102 0
SHEET 2 H 2 ALA B 223 PRO B 225 -1 O THR B 224 N ASP B 101
SHEET 1 I 2 MET B 107 LEU B 109 0
SHEET 2 I 2 LYS B 218 TYR B 220 -1 N LYS B 218 O LEU B 109
SHEET 1 J 4 ALA B 134 THR B 137 0
SHEET 2 J 4 TYR B 188 GLU B 193 1 N ALA B 189 O ALA B 134
SHEET 3 J 4 ILE B 111 LYS B 116 -1 N SER B 112 O LEU B 192
SHEET 4 J 4 THR B 208 VAL B 211 -1 O MET B 209 N ILE B 115
SHEET 1 K 3 TYR C 51 ILE C 55 0
SHEET 2 K 3 VAL C 6 THR C 10 1 O VAL C 6 N LYS C 52
SHEET 3 K 3 ILE C 85 ALA C 86 1 O ILE C 85 N THR C 9
SHEET 1 L 2 MET C 18 MET C 19 0
SHEET 2 L 2 TYR C 32 GLU C 33 -1 N GLU C 33 O MET C 18
SHEET 1 M 2 ILE C 100 PHE C 102 0
SHEET 2 M 2 ALA C 223 PRO C 225 -1 O THR C 224 N ASP C 101
SHEET 1 N 2 MET C 107 LEU C 109 0
SHEET 2 N 2 LYS C 218 TYR C 220 -1 N LYS C 218 O LEU C 109
SHEET 1 O 4 ALA C 134 GLY C 136 0
SHEET 2 O 4 TYR C 188 GLU C 193 1 N ALA C 189 O ALA C 134
SHEET 3 O 4 ILE C 111 LYS C 116 -1 N SER C 112 O LEU C 192
SHEET 4 O 4 THR C 208 VAL C 211 -1 O MET C 209 N ILE C 115
SSBOND 1 CYS A 206 CYS A 261 1555 1555 2.03
SSBOND 2 CYS B 206 CYS B 261 1555 1555 2.34
SSBOND 3 CYS C 206 CYS C 261 1555 1555 2.39
LINK ZN ZN A 422 NE2 HIS A 46 1555 1555 2.17
LINK ZN ZN A 422 OE1 GLU B 166 1555 1555 2.66
LINK ZN ZN A 422 OE2 GLU B 166 1555 1555 2.05
LINK ZN ZN A 422 OE1 GLU A 42 1555 1555 2.04
LINK ZN ZN B 423 NE2 HIS B 23 1555 1555 2.14
LINK ZN ZN B 423 O HOH B 554 1555 1555 2.33
LINK ZN ZN B 423 OE2 GLU B 30 1555 1555 2.19
LINK ZN ZN B 425 NE2 HIS B 46 1555 1555 2.09
LINK ZN ZN B 425 OE1 GLU B 42 1555 1555 2.12
LINK ZN ZN C 424 OD2 ASP C 65 1555 1555 2.23
LINK ZN ZN C 424 OD1 ASP C 65 1555 1555 2.73
LINK ZN ZN C 426 NE2 HIS C 46 1555 1555 2.41
LINK ZN ZN C 426 OE1 GLU C 42 1555 1555 2.25
LINK ZN ZN B 423 NE2 HIS C 23 1555 4557 2.19
LINK ZN ZN B 425 O HOH A 435 1555 3657 2.25
LINK ZN ZN B 425 OE2 GLU A 166 1555 3657 2.15
LINK ZN ZN C 424 O HOH A 517 1555 4457 2.26
LINK ZN ZN C 424 NE2 HIS A 23 1555 4457 2.27
CISPEP 1 SER A 14 PRO A 15 0 0.25
CISPEP 2 GLU A 166 PRO A 167 0 -0.28
CISPEP 3 LYS A 204 PRO A 205 0 0.23
CISPEP 4 SER B 14 PRO B 15 0 0.12
CISPEP 5 GLU B 166 PRO B 167 0 -0.41
CISPEP 6 LYS B 204 PRO B 205 0 0.57
CISPEP 7 SER C 14 PRO C 15 0 -0.03
CISPEP 8 GLU C 166 PRO C 167 0 -0.02
CISPEP 9 LYS C 204 PRO C 205 0 0.23
SITE 1 AC1 3 GLU A 42 HIS A 46 GLU B 166
SITE 1 AC2 4 HIS B 23 GLU B 30 HOH B 554 HIS C 23
SITE 1 AC3 3 HIS A 23 HOH A 517 ASP C 65
SITE 1 AC4 5 GLU A 166 HOH A 435 GLU B 42 HIS B 46
SITE 2 AC4 5 LEU B 241
SITE 1 AC5 2 GLU C 42 HIS C 46
SITE 1 AC6 15 TYR C 61 PRO C 89 LEU C 90 THR C 91
SITE 2 AC6 15 ARG C 96 GLY C 141 SER C 142 THR C 143
SITE 3 AC6 15 LEU C 192 GLU C 193 MET C 196 TYR C 220
SITE 4 AC6 15 HOH C 536 HOH C 537 HOH C 538
SITE 1 AC7 14 TYR A 61 PRO A 89 THR A 91 ARG A 96
SITE 2 AC7 14 GLY A 141 SER A 142 THR A 143 LEU A 192
SITE 3 AC7 14 GLU A 193 MET A 196 TYR A 220 HOH A 562
SITE 4 AC7 14 HOH A 563 HOH A 564
SITE 1 AC8 13 TYR B 61 PRO B 89 THR B 91 ARG B 96
SITE 2 AC8 13 GLY B 141 SER B 142 THR B 143 LEU B 192
SITE 3 AC8 13 GLU B 193 MET B 196 HOH B 528 HOH B 536
SITE 4 AC8 13 HOH B 591
CRYST1 113.800 163.170 47.180 90.00 90.00 90.00 P 21 21 2 12
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 0.008787 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006129 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021195 0.00000
ATOM 1 N LYS A 4 74.293 43.830 65.850 1.00 22.07 N
ATOM 2 CA LYS A 4 73.642 45.021 65.329 1.00 23.47 C
ATOM 3 C LYS A 4 73.617 44.954 63.814 1.00 22.30 C
ATOM 4 O LYS A 4 72.610 44.551 63.227 1.00 23.46 O
ATOM 5 N THR A 5 74.712 45.364 63.177 1.00 21.17 N
ATOM 6 CA THR A 5 74.810 45.308 61.717 1.00 20.08 C
ATOM 7 C THR A 5 74.985 43.850 61.263 1.00 17.92 C
ATOM 8 O THR A 5 75.897 43.149 61.712 1.00 17.62 O
ATOM 9 CB THR A 5 75.966 46.194 61.192 1.00 20.51 C
ATOM 10 OG1 THR A 5 75.620 47.567 61.388 1.00 21.90 O
ATOM 11 CG2 THR A 5 76.209 45.959 59.700 1.00 20.00 C
ATOM 12 N VAL A 6 74.077 43.400 60.401 1.00 15.32 N
ATOM 13 CA VAL A 6 74.086 42.037 59.871 1.00 13.03 C
ATOM 14 C VAL A 6 75.219 41.816 58.849 1.00 12.62 C
ATOM 15 O VAL A 6 75.313 42.526 57.845 1.00 13.73 O
ATOM 16 CB VAL A 6 72.704 41.719 59.231 1.00 12.57 C
ATOM 17 CG1 VAL A 6 72.708 40.339 58.582 1.00 14.28 C
ATOM 18 CG2 VAL A 6 71.591 41.820 60.287 1.00 13.08 C
ATOM 19 N VAL A 7 76.089 40.846 59.118 1.00 10.60 N
ATOM 20 CA VAL A 7 77.203 40.538 58.228 1.00 11.40 C
ATOM 21 C VAL A 7 76.685 39.579 57.156 1.00 9.47 C
ATOM 22 O VAL A 7 76.190 38.496 57.454 1.00 9.80 O
ATOM 23 CB VAL A 7 78.413 39.926 59.004 1.00 12.81 C
ATOM 24 CG1 VAL A 7 79.556 39.551 58.036 1.00 12.91 C
ATOM 25 CG2 VAL A 7 78.928 40.935 60.029 1.00 14.35 C
ATOM 26 N VAL A 8 76.718 40.043 55.917 1.00 9.72 N
ATOM 27 CA VAL A 8 76.231 39.264 54.793 1.00 9.72 C
ATOM 28 C VAL A 8 77.406 38.670 54.072 1.00 10.61 C
ATOM 29 O VAL A 8 78.342 39.397 53.736 1.00 11.88 O
ATOM 30 CB VAL A 8 75.466 40.164 53.775 1.00 9.89 C
ATOM 31 CG1 VAL A 8 75.034 39.343 52.550 1.00 11.25 C
ATOM 32 CG2 VAL A 8 74.257 40.805 54.424 1.00 9.27 C
ATOM 33 N THR A 9 77.416 37.350 53.910 1.00 10.59 N
ATOM 34 CA THR A 9 78.495 36.730 53.149 1.00 10.31 C
ATOM 35 C THR A 9 77.938 36.503 51.742 1.00 10.07 C
ATOM 36 O THR A 9 76.750 36.187 51.558 1.00 9.11 O
ATOM 37 CB THR A 9 79.026 35.400 53.772 1.00 10.26 C
ATOM 38 OG1 THR A 9 80.103 34.902 52.969 1.00 10.72 O
ATOM 39 CG2 THR A 9 77.930 34.328 53.878 1.00 9.92 C
ATOM 40 N THR A 10 78.778 36.790 50.754 1.00 10.38 N
ATOM 41 CA THR A 10 78.392 36.612 49.372 1.00 10.28 C
ATOM 42 C THR A 10 79.634 36.256 48.570 1.00 9.76 C
ATOM 43 O THR A 10 80.715 36.097 49.137 1.00 9.77 O
ATOM 44 CB THR A 10 77.618 37.858 48.834 1.00 10.19 C
ATOM 45 OG1 THR A 10 76.945 37.510 47.616 1.00 13.47 O
ATOM 46 CG2 THR A 10 78.550 39.065 48.630 1.00 9.31 C
ATOM 47 N ILE A 11 79.486 36.130 47.258 1.00 10.60 N
ATOM 48 CA ILE A 11 80.600 35.712 46.403 1.00 10.04 C
ATOM 49 C ILE A 11 80.701 36.571 45.132 1.00 9.98 C
ATOM 50 O ILE A 11 79.688 37.075 44.638 1.00 8.87 O
ATOM 51 CB ILE A 11 80.418 34.193 46.069 1.00 8.58 C
ATOM 52 CG1 ILE A 11 81.620 33.629 45.314 1.00 7.22 C
ATOM 53 CG2 ILE A 11 79.069 33.955 45.381 1.00 8.04 C
ATOM 54 CD1 ILE A 11 81.680 32.114 45.385 1.00 7.88 C
ATOM 55 N LEU A 12 81.928 36.834 44.686 1.00 10.07 N
ATOM 56 CA LEU A 12 82.132 37.624 43.473 1.00 11.09 C
ATOM 57 C LEU A 12 81.876 36.704 42.292 1.00 12.06 C
ATOM 58 O LEU A 12 82.759 35.966 41.849 1.00 12.69 O
ATOM 59 CB LEU A 12 83.549 38.193 43.414 1.00 11.78 C
ATOM 60 CG LEU A 12 83.727 39.468 44.215 1.00 12.78 C
ATOM 61 CD1 LEU A 12 85.157 39.974 44.031 1.00 16.01 C
ATOM 62 CD2 LEU A 12 82.712 40.512 43.778 1.00 12.94 C
ATOM 63 N GLU A 13 80.633 36.736 41.821 1.00 12.74 N
ATOM 64 CA GLU A 13 80.177 35.904 40.717 1.00 12.49 C
ATOM 65 C GLU A 13 79.275 36.782 39.882 1.00 12.72 C
ATOM 66 O GLU A 13 78.203 37.148 40.344 1.00 12.92 O
ATOM 67 CB GLU A 13 79.350 34.742 41.276 1.00 11.56 C
ATOM 68 CG GLU A 13 78.867 33.762 40.247 1.00 13.73 C
ATOM 69 CD GLU A 13 79.979 32.844 39.799 1.00 18.02 C
ATOM 70 OE1 GLU A 13 80.777 33.239 38.926 1.00 18.65 O
ATOM 71 OE2 GLU A 13 80.079 31.733 40.354 1.00 18.64 O
ATOM 72 N SER A 14 79.705 37.155 38.678 1.00 12.35 N
ATOM 73 CA SER A 14 78.871 38.007 37.816 1.00 12.53 C
ATOM 74 C SER A 14 77.662 37.192 37.349 1.00 11.42 C
ATOM 75 O SER A 14 77.812 36.022 37.041 1.00 12.12 O
ATOM 76 CB SER A 14 79.685 38.472 36.606 1.00 10.72 C
ATOM 77 OG SER A 14 80.818 39.203 37.024 1.00 12.27 O
ATOM 78 N PRO A 15 76.456 37.801 37.259 1.00 11.19 N
ATOM 79 CA PRO A 15 76.083 39.189 37.543 1.00 11.07 C
ATOM 80 C PRO A 15 75.506 39.387 38.951 1.00 11.14 C
ATOM 81 O PRO A 15 74.853 40.408 39.222 1.00 10.58 O
ATOM 82 CB PRO A 15 75.011 39.452 36.495 1.00 10.36 C
ATOM 83 CG PRO A 15 74.223 38.160 36.522 1.00 9.83 C
ATOM 84 CD PRO A 15 75.301 37.074 36.678 1.00 10.45 C
ATOM 85 N TYR A 16 75.753 38.423 39.836 1.00 8.81 N
ATOM 86 CA TYR A 16 75.228 38.496 41.197 1.00 9.33 C
ATOM 87 C TYR A 16 75.903 39.562 42.056 1.00 8.03 C
ATOM 88 O TYR A 16 75.224 40.423 42.645 1.00 7.56 O
ATOM 89 CB TYR A 16 75.281 37.118 41.841 1.00 9.34 C
ATOM 90 CG TYR A 16 74.369 36.140 41.135 1.00 10.83 C
ATOM 91 CD1 TYR A 16 72.981 36.146 41.377 1.00 11.45 C
ATOM 92 CD2 TYR A 16 74.881 35.216 40.222 1.00 10.93 C
ATOM 93 CE1 TYR A 16 72.126 35.241 40.726 1.00 11.72 C
ATOM 94 CE2 TYR A 16 74.040 34.318 39.566 1.00 12.60 C
ATOM 95 CZ TYR A 16 72.671 34.336 39.822 1.00 13.36 C
ATOM 96 OH TYR A 16 71.848 33.447 39.162 1.00 14.60 O
ATOM 97 N VAL A 17 77.229 39.517 42.103 1.00 8.43 N
ATOM 98 CA VAL A 17 78.008 40.496 42.842 1.00 8.58 C
ATOM 99 C VAL A 17 79.260 40.767 42.022 1.00 10.08 C
ATOM 100 O VAL A 17 79.974 39.845 41.619 1.00 9.66 O
ATOM 101 CB VAL A 17 78.390 40.013 44.267 1.00 8.36 C
ATOM 102 CG1 VAL A 17 79.201 41.084 44.977 1.00 9.61 C
ATOM 103 CG2 VAL A 17 77.125 39.712 45.083 1.00 8.79 C
ATOM 104 N MET A 18 79.495 42.044 41.750 1.00 10.78 N
ATOM 105 CA MET A 18 80.633 42.465 40.951 1.00 12.43 C
ATOM 106 C MET A 18 81.187 43.756 41.526 1.00 12.06 C
ATOM 107 O MET A 18 80.468 44.512 42.183 1.00 11.72 O
ATOM 108 CB MET A 18 80.175 42.726 39.510 1.00 14.84 C
ATOM 109 CG MET A 18 79.313 41.609 38.915 1.00 16.62 C
ATOM 110 SD MET A 18 78.847 41.903 37.200 1.00 21.40 S
ATOM 111 CE MET A 18 77.404 42.978 37.438 1.00 20.14 C
ATOM 112 N MET A 19 82.475 43.998 41.305 1.00 13.02 N
ATOM 113 CA MET A 19 83.087 45.239 41.760 1.00 14.63 C
ATOM 114 C MET A 19 82.675 46.368 40.797 1.00 14.66 C
ATOM 115 O MET A 19 82.735 46.200 39.580 1.00 13.91 O
ATOM 116 CB MET A 19 84.614 45.133 41.733 1.00 14.50 C
ATOM 117 CG MET A 19 85.208 44.007 42.538 1.00 18.07 C
ATOM 118 SD MET A 19 84.591 43.978 44.216 1.00 19.70 S
ATOM 119 CE MET A 19 85.165 45.575 44.835 1.00 21.21 C
ATOM 120 N LYS A 20 82.206 47.490 41.331 1.00 15.23 N
ATOM 121 CA LYS A 20 81.870 48.625 40.480 1.00 16.46 C
ATOM 122 C LYS A 20 83.195 49.125 39.876 1.00 18.00 C
ATOM 123 O LYS A 20 84.256 48.995 40.499 1.00 17.86 O
ATOM 124 CB LYS A 20 81.234 49.742 41.291 1.00 16.34 C
ATOM 125 CG LYS A 20 79.786 49.527 41.649 1.00 17.07 C
ATOM 126 CD LYS A 20 79.248 50.773 42.284 1.00 16.83 C
ATOM 127 CE LYS A 20 77.861 50.595 42.842 1.00 18.94 C
ATOM 128 NZ LYS A 20 77.549 51.798 43.675 1.00 20.03 N
ATOM 129 N LYS A 21 83.118 49.716 38.684 1.00 20.18 N
ATOM 130 CA LYS A 21 84.303 50.220 37.982 1.00 22.64 C
ATOM 131 C LYS A 21 85.121 51.121 38.879 1.00 23.94 C
ATOM 132 O LYS A 21 86.336 50.971 39.007 1.00 25.56 O
ATOM 133 CB LYS A 21 83.881 50.988 36.725 1.00 22.83 C
ATOM 134 N ASN A 22 84.423 52.043 39.520 1.00 24.56 N
ATOM 135 CA ASN A 22 84.983 53.063 40.424 1.00 26.79 C
ATOM 136 C ASN A 22 85.077 52.652 41.912 1.00 25.44 C
ATOM 137 O ASN A 22 85.221 53.520 42.781 1.00 24.45 O
ATOM 138 CB ASN A 22 84.034 54.258 40.353 1.00 30.61 C
ATOM 139 CG ASN A 22 82.554 53.813 40.407 1.00 34.87 C
ATOM 140 OD1 ASN A 22 82.283 52.623 40.600 1.00 37.86 O
ATOM 141 ND2 ASN A 22 81.608 54.736 40.211 1.00 37.22 N
ATOM 142 N HIS A 23 85.043 51.349 42.198 1.00 23.38 N
ATOM 143 CA HIS A 23 85.028 50.885 43.590 1.00 20.97 C
ATOM 144 C HIS A 23 86.099 51.403 44.544 1.00 19.98 C
ATOM 145 O HIS A 23 85.805 51.600 45.725 1.00 17.64 O
ATOM 146 CB HIS A 23 84.915 49.352 43.676 1.00 19.85 C
ATOM 147 CG HIS A 23 86.206 48.629 43.448 1.00 19.35 C
ATOM 148 ND1 HIS A 23 87.164 48.475 44.432 1.00 18.80 N
ATOM 149 CD2 HIS A 23 86.706 48.027 42.342 1.00 19.02 C
ATOM 150 CE1 HIS A 23 88.194 47.812 43.942 1.00 18.09 C
ATOM 151 NE2 HIS A 23 87.941 47.530 42.678 1.00 17.47 N
ATOM 152 N GLU A 24 87.324 51.637 44.057 1.00 20.14 N
ATOM 153 CA GLU A 24 88.404 52.134 44.930 1.00 20.55 C
ATOM 154 C GLU A 24 88.119 53.508 45.521 1.00 19.36 C
ATOM 155 O GLU A 24 88.709 53.885 46.531 1.00 20.78 O
ATOM 156 CB GLU A 24 89.735 52.139 44.211 1.00 20.85 C
ATOM 157 N MET A 25 87.196 54.235 44.903 1.00 19.77 N
ATOM 158 CA MET A 25 86.791 55.548 45.374 1.00 19.84 C
ATOM 159 C MET A 25 85.465 55.518 46.155 1.00 20.22 C
ATOM 160 O MET A 25 84.938 56.569 46.532 1.00 20.78 O
ATOM 161 CB MET A 25 86.689 56.517 44.190 1.00 22.53 C
ATOM 162 CG MET A 25 88.048 56.823 43.557 1.00 24.42 C
ATOM 163 SD MET A 25 89.351 57.022 44.843 1.00 27.72 S
ATOM 164 CE MET A 25 88.956 58.669 45.464 1.00 26.17 C
ATOM 165 N LEU A 26 84.937 54.318 46.401 1.00 19.67 N
ATOM 166 CA LEU A 26 83.662 54.150 47.122 1.00 19.64 C
ATOM 167 C LEU A 26 83.873 53.419 48.453 1.00 20.17 C
ATOM 168 O LEU A 26 84.937 52.842 48.669 1.00 19.76 O
ATOM 169 CB LEU A 26 82.664 53.394 46.246 1.00 18.56 C
ATOM 170 CG LEU A 26 82.420 54.065 44.887 1.00 19.26 C
ATOM 171 CD1 LEU A 26 81.563 53.172 43.994 1.00 18.08 C
ATOM 172 CD2 LEU A 26 81.774 55.429 45.090 1.00 18.32 C
ATOM 173 N GLU A 27 82.867 53.444 49.335 1.00 19.83 N
ATOM 174 CA GLU A 27 82.985 52.806 50.658 1.00 19.98 C
ATOM 175 C GLU A 27 81.933 51.748 50.892 1.00 17.38 C
ATOM 176 O GLU A 27 80.805 51.874 50.421 1.00 16.57 O
ATOM 177 CB GLU A 27 82.816 53.829 51.792 1.00 24.03 C
ATOM 178 CG GLU A 27 83.680 55.074 51.722 1.00 33.31 C
ATOM 179 CD GLU A 27 85.142 54.791 52.000 1.00 38.98 C
ATOM 180 OE1 GLU A 27 85.986 55.587 51.531 1.00 43.62 O
ATOM 181 OE2 GLU A 27 85.441 53.790 52.692 1.00 41.05 O
ATOM 182 N GLY A 28 82.302 50.745 51.684 1.00 15.16 N
ATOM 183 CA GLY A 28 81.390 49.678 52.058 1.00 14.30 C
ATOM 184 C GLY A 28 80.547 49.033 50.977 1.00 12.57 C
ATOM 185 O GLY A 28 81.051 48.606 49.941 1.00 12.10 O
ATOM 186 N ASN A 29 79.243 48.993 51.227 1.00 12.63 N
ATOM 187 CA ASN A 29 78.278 48.380 50.320 1.00 12.98 C
ATOM 188 C ASN A 29 78.243 48.976 48.921 1.00 13.20 C
ATOM 189 O ASN A 29 77.934 48.278 47.954 1.00 11.91 O
ATOM 190 CB ASN A 29 76.875 48.404 50.942 1.00 11.48 C
ATOM 191 CG ASN A 29 76.778 47.550 52.186 1.00 11.23 C
ATOM 192 OD1 ASN A 29 77.655 46.717 52.458 1.00 12.30 O
ATOM 193 ND2 ASN A 29 75.713 47.742 52.950 1.00 10.84 N
ATOM 194 N GLU A 30 78.597 50.253 48.834 1.00 13.86 N
ATOM 195 CA GLU A 30 78.608 51.003 47.582 1.00 16.82 C
ATOM 196 C GLU A 30 79.676 50.532 46.596 1.00 15.81 C
ATOM 197 O GLU A 30 79.621 50.879 45.427 1.00 15.84 O
ATOM 198 CB GLU A 30 78.770 52.508 47.858 1.00 18.73 C
ATOM 199 CG GLU A 30 77.920 53.049 49.021 1.00 23.87 C
ATOM 200 CD GLU A 30 76.444 52.720 48.895 1.00 28.99 C
ATOM 201 OE1 GLU A 30 75.870 52.981 47.810 1.00 30.78 O
ATOM 202 OE2 GLU A 30 75.859 52.195 49.880 1.00 31.17 O
ATOM 203 N ARG A 31 80.625 49.725 47.063 1.00 13.77 N
ATOM 204 CA ARG A 31 81.682 49.195 46.204 1.00 12.56 C
ATOM 205 C ARG A 31 81.175 48.113 45.238 1.00 11.56 C
ATOM 206 O ARG A 31 81.830 47.805 44.246 1.00 11.26 O
ATOM 207 CB ARG A 31 82.784 48.550 47.055 1.00 12.38 C
ATOM 208 CG ARG A 31 83.694 49.494 47.821 1.00 13.26 C
ATOM 209 CD ARG A 31 84.603 48.681 48.745 1.00 13.98 C
ATOM 210 NE ARG A 31 83.825 48.071 49.822 1.00 15.90 N
ATOM 211 CZ ARG A 31 84.286 47.165 50.681 1.00 17.05 C
ATOM 212 NH1 ARG A 31 85.545 46.745 50.617 1.00 18.03 N
ATOM 213 NH2 ARG A 31 83.464 46.635 51.578 1.00 14.79 N
ATOM 214 N TYR A 32 80.019 47.531 45.535 1.00 11.13 N
ATOM 215 CA TYR A 32 79.498 46.428 44.719 1.00 10.26 C
ATOM 216 C TYR A 32 78.201 46.701 43.989 1.00 9.47 C
ATOM 217 O TYR A 32 77.450 47.606 44.352 1.00 10.41 O
ATOM 218 CB TYR A 32 79.284 45.188 45.608 1.00 10.62 C
ATOM 219 CG TYR A 32 80.412 44.921 46.580 1.00 10.95 C
ATOM 220 CD1 TYR A 32 81.568 44.277 46.165 1.00 10.19 C
ATOM 221 CD2 TYR A 32 80.314 45.312 47.915 1.00 11.62 C
ATOM 222 CE1 TYR A 32 82.610 44.015 47.049 1.00 11.83 C
ATOM 223 CE2 TYR A 32 81.351 45.055 48.816 1.00 12.69 C
ATOM 224 CZ TYR A 32 82.497 44.399 48.374 1.00 13.11 C
ATOM 225 OH TYR A 32 83.509 44.089 49.260 1.00 14.56 O
ATOM 226 N GLU A 33 77.954 45.900 42.954 1.00 9.85 N
ATOM 227 CA GLU A 33 76.719 45.984 42.171 1.00 10.83 C
ATOM 228 C GLU A 33 76.352 44.586 41.658 1.00 10.42 C
ATOM 229 O GLU A 33 77.199 43.688 41.561 1.00 9.78 O
ATOM 230 CB GLU A 33 76.865 46.944 40.981 1.00 11.78 C
ATOM 231 CG GLU A 33 77.871 46.472 39.945 1.00 16.06 C
ATOM 232 CD GLU A 33 78.070 47.456 38.795 1.00 21.70 C
ATOM 233 OE1 GLU A 33 79.063 47.275 38.050 1.00 24.51 O
ATOM 234 OE2 GLU A 33 77.251 48.399 38.632 1.00 22.85 O
ATOM 235 N GLY A 34 75.083 44.400 41.328 1.00 9.36 N
ATOM 236 CA GLY A 34 74.669 43.118 40.821 1.00 7.85 C
ATOM 237 C GLY A 34 73.332 42.716 41.372 1.00 8.09 C
ATOM 238 O GLY A 34 72.759 43.399 42.226 1.00 8.95 O
ATOM 239 N TYR A 35 72.821 41.616 40.834 1.00 8.47 N
ATOM 240 CA TYR A 35 71.540 41.055 41.237 1.00 8.06 C
ATOM 241 C TYR A 35 71.431 40.877 42.769 1.00 9.06 C
ATOM 242 O TYR A 35 70.429 41.270 43.379 1.00 7.40 O
ATOM 243 CB TYR A 35 71.373 39.700 40.538 1.00 7.84 C
ATOM 244 CG TYR A 35 70.109 38.934 40.871 1.00 10.30 C
ATOM 245 CD1 TYR A 35 69.991 38.229 42.082 1.00 9.16 C
ATOM 246 CD2 TYR A 35 69.043 38.887 39.970 1.00 8.90 C
ATOM 247 CE1 TYR A 35 68.849 37.504 42.383 1.00 10.28 C
ATOM 248 CE2 TYR A 35 67.891 38.159 40.261 1.00 11.03 C
ATOM 249 CZ TYR A 35 67.802 37.472 41.472 1.00 11.88 C
ATOM 250 OH TYR A 35 66.660 36.774 41.798 1.00 14.41 O
ATOM 251 N CYS A 36 72.438 40.236 43.364 1.00 8.34 N
ATOM 252 CA CYS A 36 72.429 39.986 44.807 1.00 10.28 C
ATOM 253 C CYS A 36 72.640 41.226 45.651 1.00 10.50 C
ATOM 254 O CYS A 36 72.216 41.261 46.808 1.00 10.09 O
ATOM 255 CB CYS A 36 73.387 38.856 45.191 1.00 8.82 C
ATOM 256 SG CYS A 36 72.702 37.223 44.762 1.00 16.52 S
ATOM 257 N VAL A 37 73.289 42.238 45.071 1.00 9.12 N
ATOM 258 CA VAL A 37 73.484 43.506 45.762 1.00 9.00 C
ATOM 259 C VAL A 37 72.100 44.186 45.792 1.00 10.10 C
ATOM 260 O VAL A 37 71.667 44.702 46.827 1.00 9.15 O
ATOM 261 CB VAL A 37 74.522 44.388 45.054 1.00 8.56 C
ATOM 262 CG1 VAL A 37 74.603 45.758 45.729 1.00 10.22 C
ATOM 263 CG2 VAL A 37 75.891 43.707 45.059 1.00 10.09 C
ATOM 264 N ASP A 38 71.377 44.144 44.668 1.00 10.38 N
ATOM 265 CA ASP A 38 70.039 44.731 44.621 1.00 10.75 C
ATOM 266 C ASP A 38 69.112 43.971 45.581 1.00 10.85 C
ATOM 267 O ASP A 38 68.343 44.575 46.317 1.00 10.69 O
ATOM 268 CB ASP A 38 69.456 44.677 43.202 1.00 11.23 C
ATOM 269 CG ASP A 38 70.122 45.658 42.248 1.00 13.89 C
ATOM 270 OD1 ASP A 38 69.855 45.554 41.031 1.00 14.23 O
ATOM 271 OD2 ASP A 38 70.886 46.537 42.705 1.00 13.72 O
ATOM 272 N LEU A 39 69.213 42.643 45.584 1.00 9.88 N
ATOM 273 CA LEU A 39 68.382 41.821 46.458 1.00 9.77 C
ATOM 274 C LEU A 39 68.683 42.042 47.956 1.00 9.80 C
ATOM 275 O LEU A 39 67.761 42.117 48.758 1.00 10.21 O
ATOM 276 CB LEU A 39 68.546 40.343 46.092 1.00 10.37 C
ATOM 277 CG LEU A 39 67.725 39.324 46.893 1.00 9.13 C
ATOM 278 CD1 LEU A 39 66.236 39.669 46.836 1.00 7.99 C
ATOM 279 CD2 LEU A 39 67.994 37.934 46.345 1.00 7.09 C
ATOM 280 N ALA A 40 69.964 42.114 48.323 1.00 8.29 N
ATOM 281 CA ALA A 40 70.359 42.339 49.717 1.00 9.45 C
ATOM 282 C ALA A 40 69.775 43.644 50.256 1.00 9.19 C
ATOM 283 O ALA A 40 69.293 43.691 51.386 1.00 9.29 O
ATOM 284 CB ALA A 40 71.883 42.355 49.854 1.00 8.41 C
ATOM 285 N ALA A 41 69.799 44.691 49.434 1.00 8.43 N
ATOM 286 CA ALA A 41 69.265 45.987 49.833 1.00 9.95 C
ATOM 287 C ALA A 41 67.775 45.886 50.100 1.00 9.90 C
ATOM 288 O ALA A 41 67.258 46.486 51.047 1.00 10.20 O
ATOM 289 CB ALA A 41 69.536 47.018 48.771 1.00 8.83 C
ATOM 290 N GLU A 42 67.088 45.096 49.279 1.00 10.45 N
ATOM 291 CA GLU A 42 65.655 44.894 49.433 1.00 10.16 C
ATOM 292 C GLU A 42 65.310 44.013 50.632 1.00 10.61 C
ATOM 293 O GLU A 42 64.405 44.339 51.401 1.00 9.28 O
ATOM 294 CB GLU A 42 65.064 44.331 48.143 1.00 11.08 C
ATOM 295 CG GLU A 42 64.837 45.421 47.073 1.00 12.07 C
ATOM 296 CD GLU A 42 63.727 46.410 47.474 1.00 14.55 C
ATOM 297 OE1 GLU A 42 62.865 46.029 48.281 1.00 15.40 O
ATOM 298 OE2 GLU A 42 63.699 47.555 46.985 1.00 14.93 O
ATOM 299 N ILE A 43 66.028 42.902 50.798 1.00 9.15 N
ATOM 300 CA ILE A 43 65.770 42.015 51.924 1.00 9.74 C