HEADER OXIDOREDUCTASE 16-DEC-09 3ABM
TITLE BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE (200-S
TITLE 2 X-RAY EXPOSURE DATASET)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 1;
COMPND 3 CHAIN: A, N;
COMPND 4 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE I;
COMPND 5 EC: 1.9.3.1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND 8 CHAIN: B, O;
COMPND 9 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE II;
COMPND 10 EC: 1.9.3.1;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 3;
COMPND 13 CHAIN: C, P;
COMPND 14 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III;
COMPND 15 EC: 1.9.3.1;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1;
COMPND 18 CHAIN: D, Q;
COMPND 19 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT IV ISOFORM 1, COX IV-1,
COMPND 20 CYTOCHROME C OXIDASE POLYPEPTIDE IV;
COMPND 21 EC: 1.9.3.1;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 5A;
COMPND 24 CHAIN: E, R;
COMPND 25 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VA;
COMPND 26 EC: 1.9.3.1;
COMPND 27 MOL_ID: 6;
COMPND 28 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 5B;
COMPND 29 CHAIN: F, S;
COMPND 30 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VB, CYTOCHROME C OXIDASE
COMPND 31 POLYPEPTIDE VIA;
COMPND 32 EC: 1.9.3.1;
COMPND 33 MOL_ID: 7;
COMPND 34 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6A2;
COMPND 35 CHAIN: G, T;
COMPND 36 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIA-HEART, COXVIAH,
COMPND 37 CYTOCHROME C OXIDASE POLYPEPTIDE VIB;
COMPND 38 EC: 1.9.3.1;
COMPND 39 MOL_ID: 8;
COMPND 40 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6B1;
COMPND 41 CHAIN: H, U;
COMPND 42 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT VIB ISOFORM 1, COX VIB-1,
COMPND 43 CYTOCHROME C OXIDASE POLYPEPTIDE VII, CYTOCHROME C OXIDASE SUBUNIT
COMPND 44 AED;
COMPND 45 EC: 1.9.3.1;
COMPND 46 MOL_ID: 9;
COMPND 47 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6C;
COMPND 48 CHAIN: I, V;
COMPND 49 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIC, CYTOCHROME C OXIDASE
COMPND 50 SUBUNIT STA;
COMPND 51 EC: 1.9.3.1;
COMPND 52 MOL_ID: 10;
COMPND 53 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE 7A1;
COMPND 54 CHAIN: J, W;
COMPND 55 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA-HEART, CYTOCHROME C
COMPND 56 OXIDASE SUBUNIT VIIA-H, COX VIIA-M, VIIIC;
COMPND 57 EC: 1.9.3.1;
COMPND 58 MOL_ID: 11;
COMPND 59 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7B;
COMPND 60 CHAIN: K, X;
COMPND 61 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIB, IHQ;
COMPND 62 EC: 1.9.3.1;
COMPND 63 MOL_ID: 12;
COMPND 64 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7C;
COMPND 65 CHAIN: L, Y;
COMPND 66 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIC, CYTOCHROME C OXIDASE
COMPND 67 POLYPEPTIDE VIIIA;
COMPND 68 EC: 1.9.3.1;
COMPND 69 MOL_ID: 13;
COMPND 70 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 8B;
COMPND 71 CHAIN: M, Z;
COMPND 72 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT 8H, CYTOCHROME C OXIDASE
COMPND 73 POLYPEPTIDE VIII-HEART, CYTOCHROME C OXIDASE SUBUNIT 8-1, VIIIB, IX;
COMPND 74 EC: 1.9.3.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: BOVINE;
SOURCE 8 ORGANISM_TAXID: 9913;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 11 ORGANISM_COMMON: BOVINE;
SOURCE 12 ORGANISM_TAXID: 9913;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 15 ORGANISM_COMMON: BOVINE;
SOURCE 16 ORGANISM_TAXID: 9913;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 19 ORGANISM_COMMON: BOVINE;
SOURCE 20 ORGANISM_TAXID: 9913;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 23 ORGANISM_COMMON: BOVINE;
SOURCE 24 ORGANISM_TAXID: 9913;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 27 ORGANISM_COMMON: BOVINE;
SOURCE 28 ORGANISM_TAXID: 9913;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 31 ORGANISM_COMMON: BOVINE;
SOURCE 32 ORGANISM_TAXID: 9913;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 35 ORGANISM_COMMON: BOVINE;
SOURCE 36 ORGANISM_TAXID: 9913;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 39 ORGANISM_COMMON: BOVINE;
SOURCE 40 ORGANISM_TAXID: 9913;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 43 ORGANISM_COMMON: BOVINE;
SOURCE 44 ORGANISM_TAXID: 9913;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 47 ORGANISM_COMMON: BOVINE;
SOURCE 48 ORGANISM_TAXID: 9913;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 51 ORGANISM_COMMON: BOVINE;
SOURCE 52 ORGANISM_TAXID: 9913
KEYWDS OXIDOREDUCTASE, COPPER, ELECTRON TRANSPORT, FORMYLATION, HEME, IRON,
KEYWDS 2 MEMBRANE, MITOCHONDRION, MITOCHONDRION INNER MEMBRANE, RESPIRATORY
KEYWDS 3 CHAIN, TRANSMEMBRANE, TRANSPORT, ACETYLATION, TRANSIT PEPTIDE, ZINC,
KEYWDS 4 ISOPEPTIDE BOND, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.AOYAMA,K.MURAMOTO,K.SHINZAWA-ITOH,E.YAMASHITA,T.TSUKIHARA,T.OGURA,
AUTHOR 2 S.YOSHIKAWA
REVDAT 2 01-NOV-23 3ABM 1 REMARK HETSYN SSBOND LINK
REVDAT 1 19-JAN-10 3ABM 0
JRNL AUTH H.AOYAMA,K.MURAMOTO,K.SHINZAWA-ITOH,K.HIRATA,E.YAMASHITA,
JRNL AUTH 2 T.TSUKIHARA,T.OGURA,S.YOSHIKAWA
JRNL TITL A PEROXIDE BRIDGE BETWEEN FE AND CU IONS IN THE O2 REDUCTION
JRNL TITL 2 SITE OF FULLY OXIDIZED CYTOCHROME C OXIDASE COULD SUPPRESS
JRNL TITL 3 THE PROTON PUMP
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 2165 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19164527
JRNL DOI 10.1073/PNAS.0806391106
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 455485
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 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 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 28306
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2230
REMARK 3 SOLVENT ATOMS : 1577
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ABM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000029053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 5
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 473853
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 200.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2DYR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 91.84850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.12550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 103.49550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.12550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 91.84850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 103.49550
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
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: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M
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: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, O, P, Q, R, S, T, U, V, W,
REMARK 350 AND CHAINS: X, Y, Z
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 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 MET C 1
REMARK 465 THR C 2
REMARK 465 ALA D 1
REMARK 465 HIS D 2
REMARK 465 GLY D 3
REMARK 465 SER E 1
REMARK 465 HIS E 2
REMARK 465 GLY E 3
REMARK 465 SER E 4
REMARK 465 HIS E 5
REMARK 465 ALA F 1
REMARK 465 SER F 2
REMARK 465 GLY F 3
REMARK 465 ALA F 97
REMARK 465 HIS F 98
REMARK 465 PRO G 85
REMARK 465 ALA H 1
REMARK 465 GLU H 2
REMARK 465 ASP H 3
REMARK 465 ILE H 4
REMARK 465 GLN H 5
REMARK 465 ALA H 6
REMARK 465 LYS H 7
REMARK 465 ILE H 8
REMARK 465 LYS H 9
REMARK 465 ASN H 10
REMARK 465 SAC I 1
REMARK 465 THR I 2
REMARK 465 LYS J 58
REMARK 465 LYS J 59
REMARK 465 ILE K 1
REMARK 465 HIS K 2
REMARK 465 GLN K 3
REMARK 465 LYS K 4
REMARK 465 ARG K 5
REMARK 465 GLU K 55
REMARK 465 GLN K 56
REMARK 465 SER L 1
REMARK 465 SER M 44
REMARK 465 ALA M 45
REMARK 465 ALA M 46
REMARK 465 MET P 1
REMARK 465 THR P 2
REMARK 465 ALA Q 1
REMARK 465 HIS Q 2
REMARK 465 GLY Q 3
REMARK 465 SER R 1
REMARK 465 HIS R 2
REMARK 465 GLY R 3
REMARK 465 SER R 4
REMARK 465 HIS R 5
REMARK 465 ALA S 1
REMARK 465 SER S 2
REMARK 465 GLY S 3
REMARK 465 ALA S 97
REMARK 465 HIS S 98
REMARK 465 PRO T 85
REMARK 465 ALA U 1
REMARK 465 GLU U 2
REMARK 465 ASP U 3
REMARK 465 ILE U 4
REMARK 465 GLN U 5
REMARK 465 ALA U 6
REMARK 465 LYS U 7
REMARK 465 ILE U 8
REMARK 465 LYS U 9
REMARK 465 ASN U 10
REMARK 465 SAC V 1
REMARK 465 THR V 2
REMARK 465 LYS W 58
REMARK 465 LYS W 59
REMARK 465 ILE X 1
REMARK 465 HIS X 2
REMARK 465 GLN X 3
REMARK 465 LYS X 4
REMARK 465 ARG X 5
REMARK 465 GLU X 55
REMARK 465 GLN X 56
REMARK 465 SER Y 1
REMARK 465 SER Z 44
REMARK 465 ALA Z 45
REMARK 465 ALA Z 46
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 O HOH F 2113 O HOH F 2321 1.57
REMARK 500 UNK UNX P 1262 O HOH P 3027 2.02
REMARK 500 UNK UNX C 262 O HOH C 2027 2.06
REMARK 500 O ALA H 45 N GLY H 47 2.14
REMARK 500 OE1 GLU P 236 UNK UNX P 1262 2.15
REMARK 500 NE2 HIS C 148 UNK UNX C 262 2.16
REMARK 500 O GLU N 40 O HOH N 3060 2.16
REMARK 500 NE2 HIS P 232 UNK UNX P 1262 2.18
REMARK 500 OE2 GLU H 54 NH2 ARG H 57 2.18
REMARK 500 O HOH Q 3065 O HOH X 3011 2.18
REMARK 500 NH2 ARG L 20 CC3 TGL L 522 2.19
REMARK 500 C38 PEK G 265 C27 CDL G 269 2.19
REMARK 500 NE2 HIS P 148 UNK UNX P 1262 2.19
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 TYR A 260 CZ TYR A 260 CE2 0.083
REMARK 500 TYR A 261 CZ TYR A 261 OH 0.111
REMARK 500 TYR A 270 CD1 TYR A 270 CE1 0.146
REMARK 500 TYR A 371 CD1 TYR A 371 CE1 0.133
REMARK 500 TYR A 371 CE2 TYR A 371 CD2 0.122
REMARK 500 PHE A 393 CE1 PHE A 393 CZ 0.140
REMARK 500 TRP A 396 CE3 TRP A 396 CZ3 0.154
REMARK 500 TYR A 440 CE1 TYR A 440 CZ 0.098
REMARK 500 GLU A 474 CB GLU A 474 CG 0.118
REMARK 500 TRP A 494 CZ3 TRP A 494 CH2 0.116
REMARK 500 GLU B 19 CB GLU B 19 CG -0.124
REMARK 500 CYS B 200 CB CYS B 200 SG 0.130
REMARK 500 SER C 29 CB SER C 29 OG -0.096
REMARK 500 GLU C 236 CG GLU C 236 CD -0.098
REMARK 500 VAL D 17 CB VAL D 17 CG1 -0.197
REMARK 500 PHE E 61 CZ PHE E 61 CE2 0.115
REMARK 500 TYR F 31 CE1 TYR F 31 CZ 0.088
REMARK 500 LYS G 5 CB LYS G 5 CG 0.171
REMARK 500 TRP G 36 CB TRP G 36 CG 0.129
REMARK 500 GLU I 61 CG GLU I 61 CD -0.100
REMARK 500 SER K 20 CB SER K 20 OG -0.083
REMARK 500 ALA L 35 CA ALA L 35 CB 0.127
REMARK 500 LYS M 4 CB LYS M 4 CG -0.187
REMARK 500 ASP N 298 CB ASP N 298 CG 0.133
REMARK 500 GLU O 19 CB GLU O 19 CG -0.115
REMARK 500 TYR O 110 CD1 TYR O 110 CE1 0.096
REMARK 500 GLU O 198 C GLU O 198 O 0.120
REMARK 500 CYS O 200 CB CYS O 200 SG 0.118
REMARK 500 TYR P 8 CD1 TYR P 8 CE1 0.091
REMARK 500 SER P 29 CB SER P 29 OG -0.109
REMARK 500 SER P 89 CB SER P 89 OG 0.079
REMARK 500 TYR P 172 CD1 TYR P 172 CE1 0.109
REMARK 500 GLU P 180 CD GLU P 180 OE1 0.068
REMARK 500 PHE P 214 CD1 PHE P 214 CE1 0.155
REMARK 500 GLU P 236 CG GLU P 236 CD -0.105
REMARK 500 ALA P 238 CA ALA P 238 CB 0.141
REMARK 500 TYR P 253 CE2 TYR P 253 CD2 0.111
REMARK 500 LYS Q 121 CE LYS Q 121 NZ 0.153
REMARK 500 ASN S 54 CB ASN S 54 CG -0.252
REMARK 500 LYS T 5 CB LYS T 5 CG 0.185
REMARK 500 TRP T 36 CB TRP T 36 CG 0.153
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 LEU A 33 CB - CG - CD1 ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU A 35 CA - CB - CG ANGL. DEV. = -21.9 DEGREES
REMARK 500 ASP A 51 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 MET A 71 CG - SD - CE ANGL. DEV. = -11.8 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET A 117 CG - SD - CE ANGL. DEV. = -14.8 DEGREES
REMARK 500 MET A 208 CG - SD - CE ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP A 227 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 227 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 MET A 278 CA - CB - CG ANGL. DEV. = -10.3 DEGREES
REMARK 500 MET A 278 CG - SD - CE ANGL. DEV. = -12.2 DEGREES
REMARK 500 MET A 310 CG - SD - CE ANGL. DEV. = -18.8 DEGREES
REMARK 500 ARG A 438 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP A 442 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 442 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 480 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASN A 512 CB - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 TRP B 65 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG B 82 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 139 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 MET B 152 CG - SD - CE ANGL. DEV. = 9.9 DEGREES
REMARK 500 LYS B 171 CD - CE - NZ ANGL. DEV. = -15.3 DEGREES
REMARK 500 ASP B 173 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 188 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 SER C 29 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG C 80 CG - CD - NE ANGL. DEV. = -13.9 DEGREES
REMARK 500 ARG C 80 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG C 80 NE - CZ - NH2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG C 156 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG C 156 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 221 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU C 236 CA - CB - CG ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG D 19 NE - CZ - NH1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG D 19 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG D 20 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG D 20 NE - CZ - NH2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG E 90 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG E 90 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG H 27 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 LYS I 73 CD - CE - NZ ANGL. DEV. = -16.1 DEGREES
REMARK 500 ARG L 41 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP N 51 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 MET N 71 CG - SD - CE ANGL. DEV. = -15.0 DEGREES
REMARK 500 MET N 278 CA - CB - CG ANGL. DEV. = -10.6 DEGREES
REMARK 500 MET N 278 CG - SD - CE ANGL. DEV. = -13.2 DEGREES
REMARK 500 ILE N 286 CG1 - CB - CG2 ANGL. DEV. = -16.7 DEGREES
REMARK 500 ASP N 298 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 MET N 310 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 VAL N 366 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 66 ANGLE DEVIATIONS.
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 91 -167.79 -173.27
REMARK 500 GLU A 119 -130.95 49.73
REMARK 500 THR A 218 46.07 -142.28
REMARK 500 TRP A 334 58.95 -90.43
REMARK 500 TYR A 371 -6.85 -52.82
REMARK 500 ARG A 439 30.40 70.22
REMARK 500 ASN A 491 69.26 -151.62
REMARK 500 GLU B 60 -55.11 164.76
REMARK 500 MET B 87 -9.35 -58.00
REMARK 500 ASN B 91 -7.38 -141.80
REMARK 500 ASN B 92 80.44 65.21
REMARK 500 TYR B 113 -56.86 -131.78
REMARK 500 LEU B 135 -4.75 79.16
REMARK 500 ASP B 158 -94.03 -142.32
REMARK 500 CYS B 200 16.64 -147.98
REMARK 500 SER C 65 -69.54 -104.09
REMARK 500 GLU C 128 -111.97 -106.46
REMARK 500 HIS C 232 62.58 -160.82
REMARK 500 ALA D 129 75.00 44.62
REMARK 500 GLN D 132 -35.89 -143.26
REMARK 500 PHE D 134 -69.10 -142.79
REMARK 500 ASP F 65 -6.83 79.24
REMARK 500 HIS F 94 134.55 59.21
REMARK 500 GLN F 95 -99.94 142.13
REMARK 500 ALA G 3 -68.09 62.48
REMARK 500 ALA G 4 32.57 152.70
REMARK 500 LYS G 5 -141.20 -125.07
REMARK 500 ASP G 7 -82.61 26.75
REMARK 500 HIS G 8 4.95 21.86
REMARK 500 LEU G 23 -51.90 -127.16
REMARK 500 TRP G 36 58.33 -90.17
REMARK 500 LEU G 37 -69.40 -163.41
REMARK 500 HIS G 38 6.47 -68.42
REMARK 500 ALA H 45 -101.03 -48.00
REMARK 500 LYS H 46 30.79 -47.16
REMARK 500 LYS I 36 32.51 -80.35
REMARK 500 PHE I 37 -46.34 -148.29
REMARK 500 VAL I 39 -57.21 -129.30
REMARK 500 ASN L 10 39.85 -97.47
REMARK 500 TYR M 40 -72.96 -62.51
REMARK 500 LYS M 41 -47.80 -28.91
REMARK 500 THR N 10 33.65 -143.23
REMARK 500 LEU N 48 -63.20 -90.24
REMARK 500 ASP N 91 -159.36 -173.40
REMARK 500 GLU N 119 -135.07 46.96
REMARK 500 THR N 218 41.74 -140.94
REMARK 500 LEU N 483 -63.61 -107.01
REMARK 500 ASN N 491 70.13 -154.56
REMARK 500 HIS O 52 103.77 -162.11
REMARK 500 GLN O 59 29.59 -75.83
REMARK 500
REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO S 93 HIS S 94 103.57
REMARK 500 GLN S 95 LEU S 96 -133.12
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 NA A 519 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 40 OE1
REMARK 620 2 GLU A 40 O 70.0
REMARK 620 3 GLY A 45 O 88.8 129.3
REMARK 620 4 SER A 441 O 92.0 110.4 116.0
REMARK 620 5 HOH A2060 O 68.1 62.4 67.0 160.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA A 515 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 61 NE2
REMARK 620 2 HEA A 515 NA 91.8
REMARK 620 3 HEA A 515 NB 89.7 86.8
REMARK 620 4 HEA A 515 NC 92.0 176.2 93.6
REMARK 620 5 HEA A 515 ND 90.3 89.6 176.4 89.9
REMARK 620 6 HIS A 378 NE2 176.6 87.4 86.9 88.8 93.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 517 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 240 ND1
REMARK 620 2 HIS A 290 NE2 100.4
REMARK 620 3 HIS A 291 NE2 148.7 102.3
REMARK 620 4 PER A 520 O2 88.2 139.6 88.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 518 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 369 OD1
REMARK 620 2 HOH A2032 O 84.1
REMARK 620 3 GLU B 198 OE1 89.0 85.7
REMARK 620 4 HOH B2031 O 175.0 92.1 87.4
REMARK 620 5 HOH B2033 O 89.9 167.3 82.9 93.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA A 516 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 376 NE2
REMARK 620 2 HEA A 516 NA 91.5
REMARK 620 3 HEA A 516 NB 97.9 87.8
REMARK 620 4 HEA A 516 NC 98.2 170.3 91.1
REMARK 620 5 HEA A 516 ND 93.1 92.8 168.9 86.5
REMARK 620 6 PER A 520 O1 169.1 80.3 88.9 90.0 80.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA B 228 CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 161 ND1
REMARK 620 2 CUA B 228 CU2 132.8
REMARK 620 3 CYS B 196 SG 114.5 57.5
REMARK 620 4 CYS B 200 SG 105.8 54.3 111.5
REMARK 620 5 MET B 207 SD 99.2 127.1 115.5 109.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA B 228 CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 196 SG
REMARK 620 2 CUA B 228 CU1 56.5
REMARK 620 3 GLU B 198 O 94.8 113.8
REMARK 620 4 CYS B 200 SG 115.4 59.2 104.5
REMARK 620 5 HIS B 204 ND1 132.3 159.8 85.0 110.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 99 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 60 SG
REMARK 620 2 CYS F 62 SG 117.7
REMARK 620 3 CYS F 82 SG 109.3 108.6
REMARK 620 4 CYS F 85 SG 106.8 106.9 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA N1519 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU N 40 OE1
REMARK 620 2 GLU N 40 O 70.1
REMARK 620 3 GLY N 45 O 84.8 121.3
REMARK 620 4 SER N 441 O 97.0 116.7 118.4
REMARK 620 5 HOH N3026 O 168.6 101.5 93.6 93.7
REMARK 620 6 HOH N3060 O 70.6 57.0 64.8 167.2 98.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA N 515 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 61 NE2
REMARK 620 2 HEA N 515 NA 95.2
REMARK 620 3 HEA N 515 NB 86.7 88.7
REMARK 620 4 HEA N 515 NC 90.6 174.1 90.8
REMARK 620 5 HEA N 515 ND 95.0 88.1 176.5 92.2
REMARK 620 6 HIS N 378 NE2 173.0 84.4 86.3 89.7 92.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU N 517 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 240 ND1
REMARK 620 2 HIS N 290 NE2 104.5
REMARK 620 3 HIS N 291 NE2 153.9 90.6
REMARK 620 4 PER N 520 O2 91.3 145.6 87.5
REMARK 620 5 PER N 520 O1 84.9 109.4 110.3 40.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N1518 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP N 369 OD1
REMARK 620 2 HOH N3032 O 87.9
REMARK 620 3 GLU O 198 OE1 95.9 88.0
REMARK 620 4 HOH O3031 O 179.7 92.1 83.8
REMARK 620 5 HOH O3033 O 91.6 175.4 87.6 88.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA N 516 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 376 NE2
REMARK 620 2 HEA N 516 NA 90.5
REMARK 620 3 HEA N 516 NB 94.9 89.0
REMARK 620 4 HEA N 516 NC 97.2 172.3 90.9
REMARK 620 5 HEA N 516 ND 94.8 90.2 170.3 88.6
REMARK 620 6 PER N 520 O1 168.8 79.6 90.2 92.7 80.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA O 228 CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 161 ND1
REMARK 620 2 CUA O 228 CU2 126.0
REMARK 620 3 CYS O 196 SG 105.1 56.4
REMARK 620 4 CYS O 200 SG 107.6 54.4 110.3
REMARK 620 5 MET O 207 SD 109.2 124.7 115.3 109.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA O 228 CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 196 SG
REMARK 620 2 CUA O 228 CU1 56.9
REMARK 620 3 GLU O 198 O 96.4 113.7
REMARK 620 4 CYS O 200 SG 113.7 57.4 101.8
REMARK 620 5 HIS O 204 ND1 133.6 158.0 86.1 111.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN S 99 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 60 SG
REMARK 620 2 CYS S 62 SG 115.6
REMARK 620 3 CYS S 82 SG 110.2 108.2
REMARK 620 4 CYS S 85 SG 108.9 105.1 108.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PER A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV A 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA B 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 1086
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD C 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK C 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL C 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD C 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL D 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC E 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU G 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL G 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV H 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD J 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL L 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU M 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU N 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PER N 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 1518
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA N 1519
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1524
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1268
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA O 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD O 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL O 1521
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL O 1523
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU P 1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK P 1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL P 1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC R 1230
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK T 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK T 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL T 1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD W 1060
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL Y 1522
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU Z 1526
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OCC RELATED DB: PDB
REMARK 900 RELATED ID: 1OCZ RELATED DB: PDB
REMARK 900 RELATED ID: 1OCO RELATED DB: PDB
REMARK 900 RELATED ID: 1OCR RELATED DB: PDB
REMARK 900 RELATED ID: 2OCC RELATED DB: PDB
REMARK 900 RELATED ID: 1V54 RELATED DB: PDB
REMARK 900 RELATED ID: 1V55 RELATED DB: PDB
REMARK 900 RELATED ID: 2DYR RELATED DB: PDB
REMARK 900 RELATED ID: 2DYS RELATED DB: PDB
REMARK 900 RELATED ID: 2EIJ RELATED DB: PDB
REMARK 900 RELATED ID: 2EIK RELATED DB: PDB
REMARK 900 RELATED ID: 2EIL RELATED DB: PDB
REMARK 900 RELATED ID: 2EIM RELATED DB: PDB
REMARK 900 RELATED ID: 2EIN RELATED DB: PDB
REMARK 900 RELATED ID: 2ZXW RELATED DB: PDB
REMARK 900 RELATED ID: 3ABL RELATED DB: PDB
DBREF 3ABM A 1 514 UNP P00396 COX1_BOVIN 1 514
DBREF 3ABM B 1 227 UNP P68530 COX2_BOVIN 1 227
DBREF 3ABM C 1 261 UNP P00415 COX3_BOVIN 1 261
DBREF 3ABM D 1 147 UNP P00423 COX41_BOVIN 23 169
DBREF 3ABM E 1 109 UNP P00426 COX5A_BOVIN 44 152
DBREF 3ABM F 1 98 UNP P00428 COX5B_BOVIN 32 129
DBREF 3ABM G 1 85 UNP P07471 CX6A2_BOVIN 13 97
DBREF 3ABM H 1 85 UNP P00429 CX6B1_BOVIN 2 86
DBREF 3ABM I 1 73 UNP P04038 COX6C_BOVIN 2 74
DBREF 3ABM J 1 59 UNP P07470 CX7A1_BOVIN 22 80
DBREF 3ABM K 1 56 UNP P13183 COX7B_BOVIN 25 80
DBREF 3ABM L 1 47 UNP P00430 COX7C_BOVIN 17 63
DBREF 3ABM M 1 46 UNP P10175 COX8B_BOVIN 25 70
DBREF 3ABM N 1 514 UNP P00396 COX1_BOVIN 1 514
DBREF 3ABM O 1 227 UNP P68530 COX2_BOVIN 1 227
DBREF 3ABM P 1 261 UNP P00415 COX3_BOVIN 1 261
DBREF 3ABM Q 1 147 UNP P00423 COX41_BOVIN 23 169
DBREF 3ABM R 1 109 UNP P00426 COX5A_BOVIN 44 152
DBREF 3ABM S 1 98 UNP P00428 COX5B_BOVIN 32 129
DBREF 3ABM T 1 85 UNP P07471 CX6A2_BOVIN 13 97
DBREF 3ABM U 1 85 UNP P00429 CX6B1_BOVIN 2 86
DBREF 3ABM V 1 73 UNP P04038 COX6C_BOVIN 2 74
DBREF 3ABM W 1 59 UNP P07470 CX7A1_BOVIN 22 80
DBREF 3ABM X 1 56 UNP P13183 COX7B_BOVIN 25 80
DBREF 3ABM Y 1 47 UNP P00430 COX7C_BOVIN 17 63
DBREF 3ABM Z 1 46 UNP P10175 COX8B_BOVIN 25 70
SEQRES 1 A 514 FME PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS
SEQRES 2 A 514 ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA
SEQRES 3 A 514 GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA
SEQRES 4 A 514 GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN
SEQRES 5 A 514 ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET
SEQRES 6 A 514 ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE
SEQRES 7 A 514 GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP
SEQRES 8 A 514 MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU
SEQRES 9 A 514 LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET
SEQRES 10 A 514 VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO
SEQRES 11 A 514 PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL
SEQRES 12 A 514 ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER
SEQRES 13 A 514 SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE
SEQRES 14 A 514 ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO
SEQRES 15 A 514 LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU
SEQRES 16 A 514 LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET
SEQRES 17 A 514 LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP
SEQRES 18 A 514 PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU
SEQRES 19 A 514 PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE
SEQRES 20 A 514 LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR
SEQRES 21 A 514 TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET
SEQRES 22 A 514 VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE
SEQRES 23 A 514 VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL
SEQRES 24 A 514 ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE
SEQRES 25 A 514 ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA
SEQRES 26 A 514 THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET
SEQRES 27 A 514 MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY
SEQRES 28 A 514 GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP
SEQRES 29 A 514 ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE
SEQRES 30 A 514 HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET
SEQRES 31 A 514 GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR
SEQRES 32 A 514 THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE
SEQRES 33 A 514 MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS
SEQRES 34 A 514 PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP
SEQRES 35 A 514 TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER
SEQRES 36 A 514 MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET
SEQRES 37 A 514 VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU
SEQRES 38 A 514 VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP
SEQRES 39 A 514 LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU
SEQRES 40 A 514 PRO THR TYR VAL ASN LEU LYS
SEQRES 1 B 227 FME ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR
SEQRES 2 B 227 SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS
SEQRES 3 B 227 THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU
SEQRES 4 B 227 TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS
SEQRES 5 B 227 THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP
SEQRES 6 B 227 THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU
SEQRES 7 B 227 PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN
SEQRES 8 B 227 ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP
SEQRES 9 B 227 TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER
SEQRES 10 B 227 PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO
SEQRES 11 B 227 GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL
SEQRES 12 B 227 LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER
SEQRES 13 B 227 GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY
SEQRES 14 B 227 LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR
SEQRES 15 B 227 THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN
SEQRES 16 B 227 CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO
SEQRES 17 B 227 ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS
SEQRES 18 B 227 TRP SER ALA SER MET LEU
SEQRES 1 C 261 MET THR HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO
SEQRES 2 C 261 SER PRO TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU
SEQRES 3 C 261 MET THR SER GLY LEU THR MET TRP PHE HIS PHE ASN SER
SEQRES 4 C 261 MET THR LEU LEU MET ILE GLY LEU THR THR ASN MET LEU
SEQRES 5 C 261 THR MET TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER
SEQRES 6 C 261 THR PHE GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY
SEQRES 7 C 261 LEU ARG TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL
SEQRES 8 C 261 LEU PHE PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER
SEQRES 9 C 261 SER LEU ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO
SEQRES 10 C 261 PRO THR GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO
SEQRES 11 C 261 LEU LEU ASN THR SER VAL LEU LEU ALA SER GLY VAL SER
SEQRES 12 C 261 ILE THR TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG
SEQRES 13 C 261 LYS HIS MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU
SEQRES 14 C 261 GLY VAL TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR
SEQRES 15 C 261 GLU ALA PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER
SEQRES 16 C 261 THR PHE PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL
SEQRES 17 C 261 ILE ILE GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG
SEQRES 18 C 261 GLN LEU LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY
SEQRES 19 C 261 PHE GLU ALA ALA ALA TRP TYR TRP HIS PHE VAL ASP VAL
SEQRES 20 C 261 VAL TRP LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY
SEQRES 21 C 261 SER
SEQRES 1 D 147 ALA HIS GLY SER VAL VAL LYS SER GLU ASP TYR ALA LEU
SEQRES 2 D 147 PRO SER TYR VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP
SEQRES 3 D 147 VAL ALA HIS VAL LYS ASN LEU SER ALA SER GLN LYS ALA
SEQRES 4 D 147 LEU LYS GLU LYS GLU LYS ALA SER TRP SER SER LEU SER
SEQRES 5 D 147 ILE ASP GLU LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS
SEQRES 6 D 147 GLU SER PHE ALA GLU MET ASN ARG SER THR ASN GLU TRP
SEQRES 7 D 147 LYS THR VAL VAL GLY ALA ALA MET PHE PHE ILE GLY PHE
SEQRES 8 D 147 THR ALA LEU LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR
SEQRES 9 D 147 GLY PRO ILE PRO HIS THR PHE GLU GLU GLU TRP VAL ALA
SEQRES 10 D 147 LYS GLN THR LYS ARG MET LEU ASP MET LYS VAL ALA PRO
SEQRES 11 D 147 ILE GLN GLY PHE SER ALA LYS TRP ASP TYR ASP LYS ASN
SEQRES 12 D 147 GLU TRP LYS LYS
SEQRES 1 E 109 SER HIS GLY SER HIS GLU THR ASP GLU GLU PHE ASP ALA
SEQRES 2 E 109 ARG TRP VAL THR TYR PHE ASN LYS PRO ASP ILE ASP ALA
SEQRES 3 E 109 TRP GLU LEU ARG LYS GLY MET ASN THR LEU VAL GLY TYR
SEQRES 4 E 109 ASP LEU VAL PRO GLU PRO LYS ILE ILE ASP ALA ALA LEU
SEQRES 5 E 109 ARG ALA CYS ARG ARG LEU ASN ASP PHE ALA SER ALA VAL
SEQRES 6 E 109 ARG ILE LEU GLU VAL VAL LYS ASP LYS ALA GLY PRO HIS
SEQRES 7 E 109 LYS GLU ILE TYR PRO TYR VAL ILE GLN GLU LEU ARG PRO
SEQRES 8 E 109 THR LEU ASN GLU LEU GLY ILE SER THR PRO GLU GLU LEU
SEQRES 9 E 109 GLY LEU ASP LYS VAL
SEQRES 1 F 98 ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA
SEQRES 2 F 98 THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS
SEQRES 3 F 98 GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR
SEQRES 4 F 98 SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE
SEQRES 5 F 98 THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP
SEQRES 6 F 98 ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU
SEQRES 7 F 98 ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU
SEQRES 8 F 98 VAL PRO HIS GLN LEU ALA HIS
SEQRES 1 G 85 ALA SER ALA ALA LYS GLY ASP HIS GLY GLY TPO GLY ALA
SEQRES 2 G 85 ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO
SEQRES 3 G 85 SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER
SEQRES 4 G 85 GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS
SEQRES 5 G 85 LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY
SEQRES 6 G 85 ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU
SEQRES 7 G 85 PRO THR GLY TYR GLU LYS PRO
SEQRES 1 H 85 ALA GLU ASP ILE GLN ALA LYS ILE LYS ASN TYR GLN THR
SEQRES 2 H 85 ALA PRO PHE ASP SER ARG PHE PRO ASN GLN ASN GLN THR
SEQRES 3 H 85 ARG ASN CYS TRP GLN ASN TYR LEU ASP PHE HIS ARG CYS
SEQRES 4 H 85 GLU LYS ALA MET THR ALA LYS GLY GLY ASP VAL SER VAL
SEQRES 5 H 85 CYS GLU TRP TYR ARG ARG VAL TYR LYS SER LEU CYS PRO
SEQRES 6 H 85 ILE SER TRP VAL SER THR TRP ASP ASP ARG ARG ALA GLU
SEQRES 7 H 85 GLY THR PHE PRO GLY LYS ILE
SEQRES 1 I 73 SAC THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU
SEQRES 2 I 73 ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET
SEQRES 3 I 73 VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL
SEQRES 4 I 73 ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG
SEQRES 5 I 73 ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS
SEQRES 6 I 73 ALA GLY ILE PHE GLN SER ALA LYS
SEQRES 1 J 59 PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN
SEQRES 2 J 59 GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA
SEQRES 3 J 59 THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS
SEQRES 4 J 59 LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP
SEQRES 5 J 59 ALA SER PHE PRO HIS LYS LYS
SEQRES 1 K 56 ILE HIS GLN LYS ARG ALA PRO ASP PHE HIS ASP LYS TYR
SEQRES 2 K 56 GLY ASN ALA VAL LEU ALA SER GLY ALA THR PHE CYS VAL
SEQRES 3 K 56 ALA VAL TRP VAL TYR MET ALA THR GLN ILE GLY ILE GLU
SEQRES 4 K 56 TRP ASN PRO SER PRO VAL GLY ARG VAL THR PRO LYS GLU
SEQRES 5 K 56 TRP ARG GLU GLN
SEQRES 1 L 47 SER HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE
SEQRES 2 L 47 SER VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR
SEQRES 3 L 47 LEU PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE
SEQRES 4 L 47 VAL ARG HIS GLN LEU LEU LYS LYS
SEQRES 1 M 46 ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS
SEQRES 2 M 46 GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE
SEQRES 3 M 46 LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN
SEQRES 4 M 46 TYR LYS LYS SER SER ALA ALA
SEQRES 1 N 514 FME PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS
SEQRES 2 N 514 ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA
SEQRES 3 N 514 GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA
SEQRES 4 N 514 GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN
SEQRES 5 N 514 ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET
SEQRES 6 N 514 ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE
SEQRES 7 N 514 GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP
SEQRES 8 N 514 MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU
SEQRES 9 N 514 LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET
SEQRES 10 N 514 VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO
SEQRES 11 N 514 PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL
SEQRES 12 N 514 ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER
SEQRES 13 N 514 SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE
SEQRES 14 N 514 ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO
SEQRES 15 N 514 LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU
SEQRES 16 N 514 LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET
SEQRES 17 N 514 LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP
SEQRES 18 N 514 PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU
SEQRES 19 N 514 PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE
SEQRES 20 N 514 LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR
SEQRES 21 N 514 TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET
SEQRES 22 N 514 VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE
SEQRES 23 N 514 VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL
SEQRES 24 N 514 ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE
SEQRES 25 N 514 ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA
SEQRES 26 N 514 THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET
SEQRES 27 N 514 MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY
SEQRES 28 N 514 GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP
SEQRES 29 N 514 ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE
SEQRES 30 N 514 HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET
SEQRES 31 N 514 GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR
SEQRES 32 N 514 THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE
SEQRES 33 N 514 MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS
SEQRES 34 N 514 PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP
SEQRES 35 N 514 TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER
SEQRES 36 N 514 MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET
SEQRES 37 N 514 VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU
SEQRES 38 N 514 VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP
SEQRES 39 N 514 LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU
SEQRES 40 N 514 PRO THR TYR VAL ASN LEU LYS
SEQRES 1 O 227 FME ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR
SEQRES 2 O 227 SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS
SEQRES 3 O 227 THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU
SEQRES 4 O 227 TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS
SEQRES 5 O 227 THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP
SEQRES 6 O 227 THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU
SEQRES 7 O 227 PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN
SEQRES 8 O 227 ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP
SEQRES 9 O 227 TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER
SEQRES 10 O 227 PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO
SEQRES 11 O 227 GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL
SEQRES 12 O 227 LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER
SEQRES 13 O 227 GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY
SEQRES 14 O 227 LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR
SEQRES 15 O 227 THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN
SEQRES 16 O 227 CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO
SEQRES 17 O 227 ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS
SEQRES 18 O 227 TRP SER ALA SER MET LEU
SEQRES 1 P 261 MET THR HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO
SEQRES 2 P 261 SER PRO TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU
SEQRES 3 P 261 MET THR SER GLY LEU THR MET TRP PHE HIS PHE ASN SER
SEQRES 4 P 261 MET THR LEU LEU MET ILE GLY LEU THR THR ASN MET LEU
SEQRES 5 P 261 THR MET TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER
SEQRES 6 P 261 THR PHE GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY
SEQRES 7 P 261 LEU ARG TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL
SEQRES 8 P 261 LEU PHE PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER
SEQRES 9 P 261 SER LEU ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO
SEQRES 10 P 261 PRO THR GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO
SEQRES 11 P 261 LEU LEU ASN THR SER VAL LEU LEU ALA SER GLY VAL SER
SEQRES 12 P 261 ILE THR TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG
SEQRES 13 P 261 LYS HIS MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU
SEQRES 14 P 261 GLY VAL TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR
SEQRES 15 P 261 GLU ALA PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER
SEQRES 16 P 261 THR PHE PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL
SEQRES 17 P 261 ILE ILE GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG
SEQRES 18 P 261 GLN LEU LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY
SEQRES 19 P 261 PHE GLU ALA ALA ALA TRP TYR TRP HIS PHE VAL ASP VAL
SEQRES 20 P 261 VAL TRP LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY
SEQRES 21 P 261 SER
SEQRES 1 Q 147 ALA HIS GLY SER VAL VAL LYS SER GLU ASP TYR ALA LEU
SEQRES 2 Q 147 PRO SER TYR VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP
SEQRES 3 Q 147 VAL ALA HIS VAL LYS ASN LEU SER ALA SER GLN LYS ALA
SEQRES 4 Q 147 LEU LYS GLU LYS GLU LYS ALA SER TRP SER SER LEU SER
SEQRES 5 Q 147 ILE ASP GLU LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS
SEQRES 6 Q 147 GLU SER PHE ALA GLU MET ASN ARG SER THR ASN GLU TRP
SEQRES 7 Q 147 LYS THR VAL VAL GLY ALA ALA MET PHE PHE ILE GLY PHE
SEQRES 8 Q 147 THR ALA LEU LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR
SEQRES 9 Q 147 GLY PRO ILE PRO HIS THR PHE GLU GLU GLU TRP VAL ALA
SEQRES 10 Q 147 LYS GLN THR LYS ARG MET LEU ASP MET LYS VAL ALA PRO
SEQRES 11 Q 147 ILE GLN GLY PHE SER ALA LYS TRP ASP TYR ASP LYS ASN
SEQRES 12 Q 147 GLU TRP LYS LYS
SEQRES 1 R 109 SER HIS GLY SER HIS GLU THR ASP GLU GLU PHE ASP ALA
SEQRES 2 R 109 ARG TRP VAL THR TYR PHE ASN LYS PRO ASP ILE ASP ALA
SEQRES 3 R 109 TRP GLU LEU ARG LYS GLY MET ASN THR LEU VAL GLY TYR
SEQRES 4 R 109 ASP LEU VAL PRO GLU PRO LYS ILE ILE ASP ALA ALA LEU
SEQRES 5 R 109 ARG ALA CYS ARG ARG LEU ASN ASP PHE ALA SER ALA VAL
SEQRES 6 R 109 ARG ILE LEU GLU VAL VAL LYS ASP LYS ALA GLY PRO HIS
SEQRES 7 R 109 LYS GLU ILE TYR PRO TYR VAL ILE GLN GLU LEU ARG PRO
SEQRES 8 R 109 THR LEU ASN GLU LEU GLY ILE SER THR PRO GLU GLU LEU
SEQRES 9 R 109 GLY LEU ASP LYS VAL
SEQRES 1 S 98 ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA
SEQRES 2 S 98 THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS
SEQRES 3 S 98 GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR
SEQRES 4 S 98 SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE
SEQRES 5 S 98 THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP
SEQRES 6 S 98 ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU
SEQRES 7 S 98 ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU
SEQRES 8 S 98 VAL PRO HIS GLN LEU ALA HIS
SEQRES 1 T 85 ALA SER ALA ALA LYS GLY ASP HIS GLY GLY TPO GLY ALA
SEQRES 2 T 85 ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO
SEQRES 3 T 85 SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER
SEQRES 4 T 85 GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS
SEQRES 5 T 85 LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY
SEQRES 6 T 85 ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU
SEQRES 7 T 85 PRO THR GLY TYR GLU LYS PRO
SEQRES 1 U 85 ALA GLU ASP ILE GLN ALA LYS ILE LYS ASN TYR GLN THR
SEQRES 2 U 85 ALA PRO PHE ASP SER ARG PHE PRO ASN GLN ASN GLN THR
SEQRES 3 U 85 ARG ASN CYS TRP GLN ASN TYR LEU ASP PHE HIS ARG CYS
SEQRES 4 U 85 GLU LYS ALA MET THR ALA LYS GLY GLY ASP VAL SER VAL
SEQRES 5 U 85 CYS GLU TRP TYR ARG ARG VAL TYR LYS SER LEU CYS PRO
SEQRES 6 U 85 ILE SER TRP VAL SER THR TRP ASP ASP ARG ARG ALA GLU
SEQRES 7 U 85 GLY THR PHE PRO GLY LYS ILE
SEQRES 1 V 73 SAC THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU
SEQRES 2 V 73 ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET
SEQRES 3 V 73 VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL
SEQRES 4 V 73 ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG
SEQRES 5 V 73 ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS
SEQRES 6 V 73 ALA GLY ILE PHE GLN SER ALA LYS
SEQRES 1 W 59 PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN
SEQRES 2 W 59 GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA
SEQRES 3 W 59 THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS
SEQRES 4 W 59 LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP
SEQRES 5 W 59 ALA SER PHE PRO HIS LYS LYS
SEQRES 1 X 56 ILE HIS GLN LYS ARG ALA PRO ASP PHE HIS ASP LYS TYR
SEQRES 2 X 56 GLY ASN ALA VAL LEU ALA SER GLY ALA THR PHE CYS VAL
SEQRES 3 X 56 ALA VAL TRP VAL TYR MET ALA THR GLN ILE GLY ILE GLU
SEQRES 4 X 56 TRP ASN PRO SER PRO VAL GLY ARG VAL THR PRO LYS GLU
SEQRES 5 X 56 TRP ARG GLU GLN
SEQRES 1 Y 47 SER HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE
SEQRES 2 Y 47 SER VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR
SEQRES 3 Y 47 LEU PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE
SEQRES 4 Y 47 VAL ARG HIS GLN LEU LEU LYS LYS
SEQRES 1 Z 46 ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS
SEQRES 2 Z 46 GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE
SEQRES 3 Z 46 LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN
SEQRES 4 Z 46 TYR LYS LYS SER SER ALA ALA
MODRES 3ABM FME A 1 MET N-FORMYLMETHIONINE
MODRES 3ABM FME B 1 MET N-FORMYLMETHIONINE
MODRES 3ABM TPO G 11 THR PHOSPHOTHREONINE
MODRES 3ABM FME N 1 MET N-FORMYLMETHIONINE
MODRES 3ABM FME O 1 MET N-FORMYLMETHIONINE
MODRES 3ABM TPO T 11 THR PHOSPHOTHREONINE
HET FME A 1 10
HET FME B 1 10
HET TPO G 11 11
HET FME N 1 10
HET FME O 1 10
HET TPO T 11 11
HET CU A 517 1
HET PER A 520 2
HET MG A 518 1
HET NA A 519 1
HET HEA A 515 60
HET HEA A 516 60
HET TGL A 521 63
HET PGV A 524 51
HET PGV A 522 51
HET CUA B 228 2
HET CHD B1086 29
HET UNX C 262 1
HET CHD C 525 29
HET PEK C 264 53
HET PGV C 267 51
HET CDL C 270 100
HET CHD C 271 29
HET TGL D 523 63
HET PSC E 230 52
HET ZN F 99 1
HET DMU G 272 33
HET PEK G 265 53
HET CDL G 269 100
HET PEK G1263 53
HET PGV H 268 51
HET CHD J 60 29
HET TGL L 522 63
HET DMU M 526 33
HET CU N 517 1
HET PER N 520 2
HET MG N1518 1
HET NA N1519 1
HET HEA N 515 60
HET HEA N 516 60
HET PGV N1524 51
HET PGV N1266 51
HET PGV N1268 51
HET CUA O 228 2
HET CHD O 229 29
HET TGL O1521 63
HET TGL O1523 63
HET DMU P1272 33
HET UNX P1262 1
HET CHD P1525 29
HET PEK P1264 53
HET PGV P1267 51
HET CDL P1270 100
HET CHD P1271 29
HET PSC R1230 52
HET ZN S 99 1
HET PEK T 263 53
HET PEK T1265 53
HET CDL T1269 100
HET CHD W1060 29
HET TGL Y1522 63
HET DMU Z1526 33
HETNAM FME N-FORMYLMETHIONINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM CU COPPER (II) ION
HETNAM PER PEROXIDE ION
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM HEA HEME-A
HETNAM TGL TRISTEAROYLGLYCEROL
HETNAM PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)
HETNAM 2 PGV PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-
HETNAM 3 PGV OCTADEC-11-ENOATE
HETNAM CUA DINUCLEAR COPPER ION
HETNAM CHD CHOLIC ACID
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM PEK (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-
HETNAM 2 PEK [(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,
HETNAM 3 PEK 11,14-TETRAENOATE
HETNAM CDL CARDIOLIPIN
HETNAM PSC (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-
HETNAM 2 PSC [(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-
HETNAM 3 PSC 17,20-DIEN-1-AMINIUM 4-OXIDE
HETNAM ZN ZINC ION
HETNAM DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN TGL TRIACYLGLYCEROL
HETSYN PGV PHOSPHATIDYLGLYCEROL; 2-VACCENOYL-1-PALMITOYL-SN-
HETSYN 2 PGV GLYCEROL-3-PHOSPHOGLYCEROL
HETSYN PEK PHOSPHATIDYLETHANOLAMINE; 2-ARACHIDONOYL-1-STEAROYL-SN-
HETSYN 2 PEK GLYCEROL-3-PHOSPHOETHANOLAMINE
HETSYN CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-
HETSYN 2 CDL PHOSPHO)-1',3'-SN-GLYCEROL
HETSYN PSC PHOSPHATIDYLCHOLINE; 2-LINOLEOYL-1-PALMITOYL-SN-
HETSYN 2 PSC GYCEROL-3-PHOSPHOCHOLINE
HETSYN DMU DECYLMALTOSIDE
FORMUL 1 FME 4(C6 H11 N O3 S)
FORMUL 7 TPO 2(C4 H10 N O6 P)
FORMUL 27 CU 2(CU 2+)
FORMUL 28 PER 2(O2 2-)
FORMUL 29 MG 2(MG 2+)
FORMUL 30 NA 2(NA 1+)
FORMUL 31 HEA 4(C49 H56 FE N4 O6)
FORMUL 33 TGL 6(C57 H110 O6)
FORMUL 34 PGV 8(C40 H77 O10 P)
FORMUL 36 CUA 2(CU2)
FORMUL 37 CHD 8(C24 H40 O5)
FORMUL 38 UNX 2(X)
FORMUL 40 PEK 6(C43 H78 N O8 P)
FORMUL 42 CDL 4(C81 H156 O17 P2 2-)
FORMUL 45 PSC 2(C42 H81 N O8 P 1+)
FORMUL 46 ZN 2(ZN 2+)
FORMUL 47 DMU 4(C22 H42 O11)
FORMUL 83 HOH *1577(H2 O)
HELIX 1 1 FME A 1 LEU A 7 1 7
HELIX 2 2 ASN A 11 GLY A 42 1 32
HELIX 3 3 ASP A 50 PHE A 68 1 19
HELIX 4 4 MET A 69 ILE A 75 1 7
HELIX 5 5 GLY A 77 ILE A 87 1 11
HELIX 6 6 PHE A 94 LEU A 104 1 11
HELIX 7 7 LEU A 104 VAL A 118 1 15
HELIX 8 8 GLY A 140 MET A 171 1 32
HELIX 9 9 SER A 177 THR A 181 5 5
HELIX 10 10 PRO A 182 LEU A 215 1 34
HELIX 11 11 ASP A 221 GLY A 225 5 5
HELIX 12 12 ASP A 227 SER A 262 1 36
HELIX 13 13 GLY A 269 GLY A 284 1 16
HELIX 14 14 PHE A 285 ILE A 286 5 2
HELIX 15 15 VAL A 287 MET A 292 5 6
HELIX 16 16 ASP A 298 ILE A 312 1 15
HELIX 17 17 ILE A 312 HIS A 328 1 17
HELIX 18 18 SER A 335 ALA A 359 1 25
HELIX 19 19 ASN A 360 HIS A 368 1 9
HELIX 20 20 THR A 370 SER A 382 1 13
HELIX 21 21 MET A 383 GLY A 402 1 20
HELIX 22 22 ASN A 406 PHE A 426 1 21
HELIX 23 23 PRO A 427 SER A 434 1 8
HELIX 24 24 PRO A 444 ALA A 446 5 3
HELIX 25 25 TYR A 447 LYS A 479 1 33
HELIX 26 26 LEU A 487 LEU A 495 5 9
HELIX 27 27 SER B 14 LEU B 46 1 33
HELIX 28 28 GLU B 60 MET B 87 1 28
HELIX 29 29 PRO B 124 LEU B 128 5 5
HELIX 30 30 PRO B 166 GLY B 169 5 4
HELIX 31 31 ASN B 203 PHE B 206 5 4
HELIX 32 32 PRO B 215 MET B 226 1 12
HELIX 33 33 PRO C 15 PHE C 37 1 23
HELIX 34 34 MET C 40 THR C 66 1 27
HELIX 35 35 THR C 72 ALA C 107 1 36
HELIX 36 36 THR C 109 GLY C 113 5 5
HELIX 37 37 GLU C 128 GLU C 153 1 26
HELIX 38 38 ASP C 155 ALA C 184 1 30
HELIX 39 39 ASP C 190 LYS C 224 1 35
HELIX 40 40 HIS C 232 ILE C 256 1 25
HELIX 41 41 LYS D 7 TYR D 11 5 5
HELIX 42 42 SER D 34 GLU D 44 1 11
HELIX 43 43 LYS D 45 ALA D 46 5 2
HELIX 44 44 SER D 47 LEU D 51 5 5
HELIX 45 45 SER D 52 PHE D 64 1 13
HELIX 46 46 SER D 67 ASN D 72 1 6
HELIX 47 47 ASN D 76 VAL D 103 1 28
HELIX 48 48 PRO D 108 PHE D 111 5 4
HELIX 49 49 GLU D 112 MET D 126 1 15
HELIX 50 50 PHE D 134 ALA D 136 5 3
HELIX 51 51 THR E 7 LYS E 21 1 15
HELIX 52 52 ASP E 25 VAL E 37 1 13
HELIX 53 53 GLU E 44 LEU E 58 1 15
HELIX 54 54 ASP E 60 ALA E 75 1 16
HELIX 55 55 GLU E 80 GLY E 97 1 18
HELIX 56 56 THR F 8 ALA F 13 1 6
HELIX 57 57 THR F 14 LYS F 26 1 13
HELIX 58 58 GLY G 12 LEU G 23 1 12
HELIX 59 59 LEU G 23 TRP G 36 1 14
HELIX 60 60 GLN H 25 LYS H 46 1 22
HELIX 61 61 ASP H 49 VAL H 52 5 4
HELIX 62 62 CYS H 53 CYS H 64 1 12
HELIX 63 63 PRO H 65 GLY H 79 1 15
HELIX 64 64 GLY I 11 VAL I 39 1 29
HELIX 65 65 VAL I 39 ASN I 53 1 15
HELIX 66 66 ASP I 55 GLY I 67 1 13
HELIX 67 67 ARG J 4 GLN J 13 1 10
HELIX 68 68 PRO J 19 LYS J 23 5 5
HELIX 69 69 GLY J 25 SER J 54 1 30
HELIX 70 70 ASP K 8 ILE K 36 1 29
HELIX 71 71 ASN L 17 LEU L 45 1 29
HELIX 72 72 SER M 11 HIS M 36 1 26
HELIX 73 73 HIS M 36 LYS M 42 1 7
HELIX 74 74 FME N 1 LEU N 7 1 7
HELIX 75 75 ASN N 11 GLY N 42 1 32
HELIX 76 76 ASP N 50 PHE N 68 1 19
HELIX 77 77 MET N 69 ILE N 75 1 7
HELIX 78 78 GLY N 77 ILE N 87 1 11
HELIX 79 79 PHE N 94 LEU N 104 1 11
HELIX 80 80 LEU N 104 VAL N 118 1 15
HELIX 81 81 ALA N 141 MET N 171 1 31
HELIX 82 82 SER N 177 THR N 181 5 5
HELIX 83 83 PRO N 182 LEU N 215 1 34
HELIX 84 84 ASP N 221 GLY N 225 5 5
HELIX 85 85 ASP N 227 SER N 262 1 36
HELIX 86 86 GLY N 269 GLY N 284 1 16
HELIX 87 87 PHE N 285 ILE N 286 5 2
HELIX 88 88 VAL N 287 MET N 292 5 6
HELIX 89 89 ASP N 298 ILE N 312 1 15
HELIX 90 90 ILE N 312 HIS N 328 1 17
HELIX 91 91 SER N 335 ALA N 359 1 25
HELIX 92 92 ASN N 360 HIS N 368 1 9
HELIX 93 93 THR N 370 MET N 383 1 14
HELIX 94 94 MET N 383 GLY N 402 1 20
HELIX 95 95 ASN N 406 PHE N 426 1 21
HELIX 96 96 PRO N 427 SER N 434 1 8
HELIX 97 97 PRO N 444 ALA N 446 5 3
HELIX 98 98 TYR N 447 LYS N 479 1 33
HELIX 99 99 LEU N 487 LEU N 495 5 9
HELIX 100 100 SER O 14 THR O 47 1 34
HELIX 101 101 GLU O 60 GLU O 89 1 30
HELIX 102 102 PRO O 124 LEU O 128 5 5
HELIX 103 103 PRO O 166 GLY O 169 5 4
HELIX 104 104 PRO O 215 MET O 226 1 12
HELIX 105 105 PRO P 15 ASN P 38 1 24
HELIX 106 106 MET P 40 THR P 66 1 27
HELIX 107 107 THR P 72 ALA P 107 1 36
HELIX 108 108 THR P 109 GLY P 113 5 5
HELIX 109 109 GLU P 128 GLU P 153 1 26
HELIX 110 110 ASP P 155 ALA P 184 1 30
HELIX 111 111 ASP P 190 LYS P 224 1 35
HELIX 112 112 HIS P 232 ILE P 256 1 25
HELIX 113 113 SER Q 36 GLU Q 44 1 9
HELIX 114 114 LYS Q 45 ALA Q 46 5 2
HELIX 115 115 SER Q 47 LEU Q 51 5 5
HELIX 116 116 SER Q 52 PHE Q 64 1 13
HELIX 117 117 SER Q 67 ASN Q 72 1 6
HELIX 118 118 ASN Q 76 VAL Q 103 1 28
HELIX 119 119 PRO Q 108 PHE Q 111 5 4
HELIX 120 120 GLU Q 112 MET Q 126 1 15
HELIX 121 121 PHE Q 134 ALA Q 136 5 3
HELIX 122 122 THR R 7 LYS R 21 1 15
HELIX 123 123 ASP R 25 VAL R 37 1 13
HELIX 124 124 GLU R 44 LEU R 58 1 15
HELIX 125 125 ASP R 60 ALA R 75 1 16
HELIX 126 126 GLU R 80 GLY R 97 1 18
HELIX 127 127 THR S 8 ALA S 13 1 6
HELIX 128 128 THR S 14 LYS S 26 1 13
HELIX 129 129 GLY T 12 LEU T 23 1 12
HELIX 130 130 LEU T 23 TRP T 36 1 14
HELIX 131 131 GLN U 25 GLY U 47 1 23
HELIX 132 132 ASP U 49 VAL U 52 5 4
HELIX 133 133 CYS U 53 CYS U 64 1 12
HELIX 134 134 PRO U 65 GLY U 79 1 15
HELIX 135 135 GLY V 11 VAL V 39 1 29
HELIX 136 136 VAL V 39 ASN V 53 1 15
HELIX 137 137 ASP V 55 ALA V 66 1 12
HELIX 138 138 ARG W 4 GLN W 13 1 10
HELIX 139 139 PRO W 19 LYS W 23 5 5
HELIX 140 140 GLY W 25 SER W 54 1 30
HELIX 141 141 ASP X 8 ILE X 36 1 29
HELIX 142 142 ASN Y 17 LYS Y 47 1 31
HELIX 143 143 SER Z 11 HIS Z 36 1 26
HELIX 144 144 HIS Z 36 LYS Z 42 1 7
SHEET 1 A 2 VAL A 482 THR A 484 0
SHEET 2 A 2 THR M 2 ALA M 3 -1 O THR M 2 N LEU A 483
SHEET 1 B 5 LEU B 116 SER B 120 0
SHEET 2 B 5 TYR B 105 TYR B 110 -1 N TYR B 110 O LEU B 116
SHEET 3 B 5 LEU B 95 HIS B 102 -1 N MET B 100 O SER B 107
SHEET 4 B 5 ILE B 150 SER B 156 1 O LEU B 153 N THR B 99
SHEET 5 B 5 ASN B 180 LEU B 184 -1 O THR B 182 N MET B 152
SHEET 1 C 3 VAL B 142 PRO B 145 0
SHEET 2 C 3 PRO B 208 VAL B 214 1 O GLU B 212 N VAL B 142
SHEET 3 C 3 GLY B 190 GLN B 195 -1 N GLY B 190 O LEU B 213
SHEET 1 D 2 HIS B 161 VAL B 165 0
SHEET 2 D 2 LEU B 170 ALA B 174 -1 O THR B 172 N TRP B 163
SHEET 1 E 2 TRP D 138 ASP D 139 0
SHEET 2 E 2 GLU D 144 TRP D 145 -1 O GLU D 144 N ASP D 139
SHEET 1 F 3 ASN F 47 PRO F 50 0
SHEET 2 F 3 HIS F 88 VAL F 92 1 O LYS F 90 N ASN F 47
SHEET 3 F 3 GLN F 80 ARG F 81 -1 N GLN F 80 O TYR F 89
SHEET 1 G 2 LYS F 55 CYS F 60 0
SHEET 2 G 2 ILE F 70 HIS F 75 -1 O PHE F 72 N VAL F 58
SHEET 1 H 2 VAL N 482 THR N 484 0
SHEET 2 H 2 THR Z 2 ALA Z 3 -1 O THR Z 2 N LEU N 483
SHEET 1 I 5 LEU O 116 SER O 120 0
SHEET 2 I 5 TYR O 105 TYR O 110 -1 N TYR O 108 O PHE O 118
SHEET 3 I 5 LEU O 95 HIS O 102 -1 N MET O 100 O SER O 107
SHEET 4 I 5 ILE O 150 SER O 156 1 O ARG O 151 N LEU O 95
SHEET 5 I 5 ASN O 180 LEU O 184 -1 O ASN O 180 N VAL O 154
SHEET 1 J 3 VAL O 142 PRO O 145 0
SHEET 2 J 3 ILE O 209 VAL O 214 1 O GLU O 212 N VAL O 142
SHEET 3 J 3 GLY O 190 GLY O 194 -1 N GLY O 190 O LEU O 213
SHEET 1 K 2 HIS O 161 VAL O 165 0
SHEET 2 K 2 LEU O 170 ALA O 174 -1 O THR O 172 N TRP O 163
SHEET 1 L 2 TRP Q 138 ASP Q 139 0
SHEET 2 L 2 GLU Q 144 TRP Q 145 -1 O GLU Q 144 N ASP Q 139
SHEET 1 M 3 ASN S 47 SER S 51 0
SHEET 2 M 3 HIS S 88 PRO S 93 1 O LYS S 90 N ASN S 47
SHEET 3 M 3 GLN S 80 ARG S 81 -1 N GLN S 80 O TYR S 89
SHEET 1 N 2 LYS S 55 CYS S 60 0
SHEET 2 N 2 ILE S 70 HIS S 75 -1 O LEU S 74 N ARG S 56
SSBOND 1 CYS H 29 CYS H 64 1555 1555 2.07
SSBOND 2 CYS H 39 CYS H 53 1555 1555 2.05
SSBOND 3 CYS U 29 CYS U 64 1555 1555 2.05
SSBOND 4 CYS U 39 CYS U 53 1555 1555 2.05
LINK C FME A 1 N PHE A 2 1555 1555 1.34
LINK NE2 HIS A 240 CE2 TYR A 244 1555 1555 1.33
LINK C FME B 1 N ALA B 2 1555 1555 1.34
LINK C GLY G 10 N TPO G 11 1555 1555 1.34
LINK C TPO G 11 N GLY G 12 1555 1555 1.36
LINK C FME N 1 N PHE N 2 1555 1555 1.33
LINK NE2 HIS N 240 CE2 TYR N 244 1555 1555 1.35
LINK C FME O 1 N ALA O 2 1555 1555 1.30
LINK C GLY T 10 N TPO T 11 1555 1555 1.34
LINK C TPO T 11 N GLY T 12 1555 1555 1.38
LINK OE1 GLU A 40 NA NA A 519 1555 1555 2.28
LINK O GLU A 40 NA NA A 519 1555 1555 2.33
LINK O GLY A 45 NA NA A 519 1555 1555 2.35
LINK NE2 HIS A 61 FE HEA A 515 1555 1555 1.92
LINK ND1 HIS A 240 CU CU A 517 1555 1555 2.09
LINK NE2 HIS A 290 CU CU A 517 1555 1555 2.12
LINK NE2 HIS A 291 CU CU A 517 1555 1555 2.02
LINK OD1 ASP A 369 MG MG A 518 1555 1555 2.10
LINK NE2 HIS A 376 FE HEA A 516 1555 1555 2.01
LINK NE2 HIS A 378 FE HEA A 515 1555 1555 1.95
LINK O SER A 441 NA NA A 519 1555 1555 2.39
LINK FE HEA A 516 O1 PER A 520 1555 1555 2.19
LINK CU CU A 517 O2 PER A 520 1555 1555 2.16
LINK MG MG A 518 O HOH A2032 1555 1555 2.14
LINK MG MG A 518 OE1 GLU B 198 1555 1555 2.12
LINK MG MG A 518 O HOH B2031 1555 1555 2.10
LINK MG MG A 518 O HOH B2033 1555 1555 2.12
LINK NA NA A 519 O HOH A2060 1555 1555 2.08
LINK ND1 HIS B 161 CU1 CUA B 228 1555 1555 2.03
LINK SG CYS B 196 CU1 CUA B 228 1555 1555 2.30
LINK SG CYS B 196 CU2 CUA B 228 1555 1555 2.32
LINK O GLU B 198 CU2 CUA B 228 1555 1555 2.20
LINK SG CYS B 200 CU2 CUA B 228 1555 1555 2.23
LINK SG CYS B 200 CU1 CUA B 228 1555 1555 2.35
LINK ND1 HIS B 204 CU2 CUA B 228 1555 1555 2.02
LINK SD MET B 207 CU1 CUA B 228 1555 1555 2.38
LINK SG CYS F 60 ZN ZN F 99 1555 1555 2.30
LINK SG CYS F 62 ZN ZN F 99 1555 1555 2.33
LINK SG CYS F 82 ZN ZN F 99 1555 1555 2.28
LINK SG CYS F 85 ZN ZN F 99 1555 1555 2.37
LINK OE1 GLU N 40 NA NA N1519 1555 1555 2.26
LINK O GLU N 40 NA NA N1519 1555 1555 2.32
LINK O GLY N 45 NA NA N1519 1555 1555 2.28
LINK NE2 HIS N 61 FE HEA N 515 1555 1555 2.00
LINK ND1 HIS N 240 CU CU N 517 1555 1555 2.08
LINK NE2 HIS N 290 CU CU N 517 1555 1555 2.03
LINK NE2 HIS N 291 CU CU N 517 1555 1555 2.05
LINK OD1 ASP N 369 MG MG N1518 1555 1555 2.12
LINK NE2 HIS N 376 FE HEA N 516 1555 1555 2.03
LINK NE2 HIS N 378 FE HEA N 515 1555 1555 1.96
LINK O SER N 441 NA NA N1519 1555 1555 2.34
LINK FE HEA N 516 O1 PER N 520 1555 1555 2.37
LINK CU CU N 517 O2 PER N 520 1555 1555 2.10
LINK CU CU N 517 O1 PER N 520 1555 1555 2.59
LINK MG MG N1518 O HOH N3032 1555 1555 2.16
LINK MG MG N1518 OE1 GLU O 198 1555 1555 2.13
LINK MG MG N1518 O HOH O3031 1555 1555 1.97
LINK MG MG N1518 O HOH O3033 1555 1555 2.16
LINK NA NA N1519 O HOH N3026 1555 1555 1.96
LINK NA NA N1519 O HOH N3060 1555 1555 2.21
LINK ND1 HIS O 161 CU1 CUA O 228 1555 1555 1.97
LINK SG CYS O 196 CU2 CUA O 228 1555 1555 2.34
LINK SG CYS O 196 CU1 CUA O 228 1555 1555 2.35
LINK O GLU O 198 CU2 CUA O 228 1555 1555 2.15
LINK SG CYS O 200 CU2 CUA O 228 1555 1555 2.25
LINK SG CYS O 200 CU1 CUA O 228 1555 1555 2.34
LINK ND1 HIS O 204 CU2 CUA O 228 1555 1555 2.02
LINK SD MET O 207 CU1 CUA O 228 1555 1555 2.36
LINK SG CYS S 60 ZN ZN S 99 1555 1555 2.40
LINK SG CYS S 62 ZN ZN S 99 1555 1555 2.37
LINK SG CYS S 82 ZN ZN S 99 1555 1555 2.35
LINK SG CYS S 85 ZN ZN S 99 1555 1555 2.35
CISPEP 1 PRO A 130 PRO A 131 0 -0.23
CISPEP 2 CYS A 498 PRO A 499 0 -5.39
CISPEP 3 GLN B 103 TRP B 104 0 -13.38
CISPEP 4 TRP C 116 PRO C 117 0 -7.98
CISPEP 5 PRO N 130 PRO N 131 0 -6.19
CISPEP 6 CYS N 498 PRO N 499 0 -6.02
CISPEP 7 GLN O 103 TRP O 104 0 -3.87
CISPEP 8 TRP P 116 PRO P 117 0 -5.80
SITE 1 AC1 4 HIS A 240 HIS A 290 HIS A 291 PER A 520
SITE 1 AC2 5 HIS A 240 VAL A 243 HIS A 291 HEA A 516
SITE 2 AC2 5 CU A 517
SITE 1 AC3 6 HIS A 368 ASP A 369 HOH A2032 GLU B 198
SITE 2 AC3 6 HOH B2031 HOH B2033
SITE 1 AC4 6 GLU A 40 GLN A 43 GLY A 45 SER A 441
SITE 2 AC4 6 HOH A2026 HOH A2060
SITE 1 AC5 31 ALA A 24 MET A 28 THR A 31 SER A 34
SITE 2 AC5 31 ILE A 37 ARG A 38 TYR A 54 VAL A 58
SITE 3 AC5 31 HIS A 61 ALA A 62 MET A 65 ILE A 66
SITE 4 AC5 31 VAL A 70 GLY A 125 TRP A 126 TYR A 371
SITE 5 AC5 31 PHE A 377 HIS A 378 SER A 382 VAL A 386
SITE 6 AC5 31 PHE A 393 MET A 417 PHE A 425 GLN A 428
SITE 7 AC5 31 ARG A 438 ARG A 439 SER A 458 MET A 468
SITE 8 AC5 31 HOH A2005 HOH A2036 HOH A2045
SITE 1 AC6 27 TRP A 126 TRP A 236 VAL A 243 TYR A 244
SITE 2 AC6 27 HIS A 290 HIS A 291 THR A 309 THR A 316
SITE 3 AC6 27 GLY A 317 GLY A 352 GLY A 355 ILE A 356
SITE 4 AC6 27 LEU A 358 ALA A 359 ASP A 364 HIS A 368
SITE 5 AC6 27 VAL A 373 HIS A 376 PHE A 377 VAL A 380
SITE 6 AC6 27 LEU A 381 ARG A 438 PER A 520 HOH A2007
SITE 7 AC6 27 HOH A2016 HOH A2034 HOH A2044
SITE 1 AC7 15 TYR A 379 ASN A 422 PHE A 426 HIS A 429
SITE 2 AC7 15 PHE A 430 LEU A 433 HOH A4722 HOH A4765
SITE 3 AC7 15 LEU B 7 LEU B 28 VAL B 31 PHE B 32
SITE 4 AC7 15 SER B 35 LEU B 39 HOH D2376
SITE 1 AC8 9 ASN A 406 THR A 408 HOH A2153 HOH A2396
SITE 2 AC8 9 PHE D 87 PHE K 9 GLN M 15 LEU M 19
SITE 3 AC8 9 SER M 20
SITE 1 AC9 17 PHE A 94 PRO A 95 ARG A 96 MET A 97
SITE 2 AC9 17 HOH A2138 HOH A2226 HIS C 9 GLY C 20
SITE 3 AC9 17 ALA C 24 ASN C 50 TRP C 57 TRP C 58
SITE 4 AC9 17 GLU C 64 HIS C 71 GLY C 82 SER C 89
SITE 5 AC9 17 PEK C 264
SITE 1 BC1 6 HIS B 161 CYS B 196 GLU B 198 CYS B 200
SITE 2 BC1 6 HIS B 204 MET B 207
SITE 1 BC2 12 MET A 271 GLN B 59 GLU B 62 THR B 63
SITE 2 BC2 12 THR B 66 HOH B2375 ARG T 14 ARG T 17
SITE 3 BC2 12 PHE T 18 GLY T 22 PEK T1265 HOH T3302
SITE 1 BC3 7 HIS A 233 ASP A 300 THR A 301 TYR A 304
SITE 2 BC3 7 TRP C 99 HIS C 103 CDL T1269
SITE 1 BC4 18 HIS A 151 VAL A 155 PGV A 522 TRP C 34
SITE 2 BC4 18 TYR C 181 TYR C 182 ALA C 184 PHE C 186
SITE 3 BC4 18 THR C 187 ILE C 188 PHE C 198 TRP G 62
SITE 4 BC4 18 THR G 68 PHE G 69 PHE G 70 HIS G 71
SITE 5 BC4 18 ASN G 76 HOH G2254
SITE 1 BC5 17 TRP C 58 VAL C 61 SER C 65 THR C 66
SITE 2 BC5 17 ILE C 210 PHE C 214 ARG C 221 HIS C 226
SITE 3 BC5 17 PHE C 227 HIS C 231 PHE C 233 GLY C 234
SITE 4 BC5 17 CDL C 270 HOH C2214 HOH C2350 HOH F2130
SITE 5 BC5 17 HOH F4100
SITE 1 BC6 15 THR C 48 MET C 51 LEU C 52 TYR C 55
SITE 2 BC6 15 ARG C 59 ARG C 63 PHE C 67 THR C 213
SITE 3 BC6 15 VAL C 217 PHE C 220 LYS C 224 HIS C 226
SITE 4 BC6 15 PGV C 267 HOH C2164 LYS J 8
SITE 1 BC7 4 ARG C 156 PHE C 164 LEU C 223 PHE J 1
SITE 1 BC8 14 TRP A 334 GLY A 343 VAL A 419 ILE B 42
SITE 2 BC8 14 THR B 47 HOH B2353 HOH B4246 ARG D 73
SITE 3 BC8 14 SER D 74 THR D 75 GLU D 77 TRP D 78
SITE 4 BC8 14 HOH D4405 ARG I 16
SITE 1 BC9 15 HOH A4231 ILE B 41 HIS B 52 MET B 56
SITE 2 BC9 15 ASP B 57 VAL B 61 TRP B 65 HOH B4217
SITE 3 BC9 15 ASP E 8 PHE E 11 LEU E 41 HOH E2122
SITE 4 BC9 15 HOH E2394 HOH E4744 ARG I 10
SITE 1 CC1 4 CYS F 60 CYS F 62 CYS F 82 CYS F 85
SITE 1 CC2 5 TRP C 34 MET C 40 SER G 61 GLY G 63
SITE 2 CC2 5 PHE G 69
SITE 1 CC3 12 HIS C 158 GLN C 161 TYR C 172 ARG G 17
SITE 2 CC3 12 PHE G 21 GLY G 22 TRP G 36 CDL G 269
SITE 3 CC3 12 SER N 279 GLN O 59 THR O 66 CHD O 229
SITE 1 CC4 20 LEU C 127 LEU C 131 LEU C 138 VAL C 142
SITE 2 CC4 20 LEU G 23 SER G 27 LEU G 30 CYS G 31
SITE 3 CC4 20 ASN G 34 LEU G 37 HIS G 38 ARG G 42
SITE 4 CC4 20 PEK G 265 PHE N 282 ILE N 286 ASP N 300
SITE 5 CC4 20 SER N 307 ILE N 311 LEU O 78 TYR O 85
SITE 1 CC5 16 SER G 2 ALA G 3 LYS G 5 HIS G 8
SITE 2 CC5 16 HOH G4355 HOH G4660 PHE N 282 LYS P 77
SITE 3 CC5 16 ARG P 80 TYR P 81 ILE P 84 THR P 95
SITE 4 CC5 16 PHE P 98 TRP P 240 VAL P 247 PHE P 251
SITE 1 CC6 9 ASP A 298 TRP C 99 TYR C 102 HIS C 103
SITE 2 CC6 9 LEU C 106 HOH C4502 ASN H 22 ASN H 24
SITE 3 CC6 9 HOH H4417
SITE 1 CC7 5 TYR J 32 ARG J 33 MET J 36 THR J 37
SITE 2 CC7 5 LEU J 40
SITE 1 CC8 16 PHE A 2 THR A 17 LEU A 18 LEU A 20
SITE 2 CC8 16 TRP A 25 PRO A 106 LEU A 113 PHE A 400
SITE 3 CC8 16 ILE A 472 ILE L 11 PRO L 12 SER L 14
SITE 4 CC8 16 ARG L 20 MET L 24 PHE L 29 HOH L4545
SITE 1 CC9 7 TRP D 98 LEU M 27 LEU M 28 GLY M 31
SITE 2 CC9 7 TRP M 32 TYR M 35 HIS M 36
SITE 1 DC1 4 HIS N 240 HIS N 290 HIS N 291 PER N 520
SITE 1 DC2 5 HIS N 240 VAL N 243 HIS N 291 HEA N 516
SITE 2 DC2 5 CU N 517
SITE 1 DC3 6 HIS N 368 ASP N 369 HOH N3032 GLU O 198
SITE 2 DC3 6 HOH O3031 HOH O3033
SITE 1 DC4 6 GLU N 40 GLN N 43 GLY N 45 SER N 441
SITE 2 DC4 6 HOH N3026 HOH N3060
SITE 1 DC5 27 MET N 28 THR N 31 SER N 34 ILE N 37
SITE 2 DC5 27 ARG N 38 TYR N 54 VAL N 58 HIS N 61
SITE 3 DC5 27 ALA N 62 MET N 65 VAL N 70 GLY N 125
SITE 4 DC5 27 TRP N 126 TYR N 371 PHE N 377 HIS N 378
SITE 5 DC5 27 SER N 382 VAL N 386 PHE N 393 PHE N 425
SITE 6 DC5 27 GLN N 428 ARG N 438 ARG N 439 MET N 468
SITE 7 DC5 27 HOH N3005 HOH N3036 HOH N3045
SITE 1 DC6 30 TRP N 126 TRP N 236 VAL N 243 TYR N 244
SITE 2 DC6 30 HIS N 290 HIS N 291 THR N 309 ALA N 313
SITE 3 DC6 30 THR N 316 GLY N 317 GLY N 352 LEU N 353
SITE 4 DC6 30 GLY N 355 ILE N 356 LEU N 358 ALA N 359
SITE 5 DC6 30 ASP N 364 HIS N 368 VAL N 373 HIS N 376
SITE 6 DC6 30 PHE N 377 VAL N 380 LEU N 381 ARG N 438
SITE 7 DC6 30 PER N 520 HOH N3007 HOH N3016 HOH N3034
SITE 8 DC6 30 HOH N3044 ILE O 72
SITE 1 DC7 15 ASN N 406 THR N 408 TRP N 409 ILE N 412
SITE 2 DC7 15 HOH N3396 HOH N4418 HOH N4682 ALA Q 84
SITE 3 DC7 15 PHE Q 87 HIS X 10 PRO Z 12 ALA Z 16
SITE 4 DC7 15 LEU Z 19 SER Z 20 HOH Z3153
SITE 1 DC8 17 PHE N 94 PRO N 95 ARG N 96 MET N 97
SITE 2 DC8 17 MET N 100 HOH N3138 HOH N3226 HIS P 9
SITE 3 DC8 17 ASN P 50 MET P 54 TRP P 57 TRP P 58
SITE 4 DC8 17 GLU P 64 HIS P 71 LEU P 79 GLY P 82
SITE 5 DC8 17 PEK P1264
SITE 1 DC9 11 HOH C4575 ALA G 1 HOH G4754 ASP N 298
SITE 2 DC9 11 HOH N4084 HOH N4766 THR P 95 TRP P 99
SITE 3 DC9 11 HIS P 103 ALA P 107 CHD P1525
SITE 1 EC1 6 HIS O 161 CYS O 196 GLU O 198 CYS O 200
SITE 2 EC1 6 HIS O 204 MET O 207
SITE 1 EC2 9 ARG G 14 ARG G 17 PEK G 265 HOH G2302
SITE 2 EC2 9 MET N 271 GLU O 62 THR O 63 THR O 66
SITE 3 EC2 9 HOH O3375
SITE 1 EC3 9 ASN N 422 PHE N 430 LEU N 433 LEU O 7
SITE 2 EC3 9 LEU O 28 PHE O 32 SER O 35 LEU O 39
SITE 3 EC3 9 HOH Q4401
SITE 1 EC4 13 TRP N 334 LYS N 411 PHE N 414 HOH N4407
SITE 2 EC4 13 LEU O 39 ILE O 42 THR O 47 LYS O 49
SITE 3 EC4 13 ARG Q 73 SER Q 74 GLU Q 77 TRP Q 78
SITE 4 EC4 13 HOH Q4568
SITE 1 EC5 7 TRP P 34 MET P 40 HOH P4208 SER T 61
SITE 2 EC5 7 TRP T 62 GLY T 63 PHE T 69
SITE 1 EC6 8 HIS N 233 ASP N 300 THR N 301 TYR N 304
SITE 2 EC6 8 PGV N1268 TRP P 99 HIS P 103 HOH P4549
SITE 1 EC7 17 HIS N 151 LEU N 215 PGV N1266 TRP P 34
SITE 2 EC7 17 TYR P 181 TYR P 182 ALA P 184 PHE P 186
SITE 3 EC7 17 THR P 187 ILE P 188 PHE P 198 TRP T 62
SITE 4 EC7 17 THR T 68 PHE T 69 PHE T 70 HIS T 71
SITE 5 EC7 17 ASN T 76
SITE 1 EC8 19 MET P 54 TRP P 58 VAL P 61 SER P 65
SITE 2 EC8 19 THR P 66 HIS P 207 ILE P 210 THR P 213
SITE 3 EC8 19 PHE P 214 ARG P 221 HIS P 226 PHE P 227
SITE 4 EC8 19 HIS P 231 PHE P 233 GLY P 234 CDL P1270
SITE 5 EC8 19 HOH P3214 HOH P3350 HOH S3130
SITE 1 EC9 13 MET P 51 TYR P 55 ARG P 59 ARG P 63
SITE 2 EC9 13 PHE P 67 VAL P 217 PHE P 220 ARG P 221
SITE 3 EC9 13 LYS P 224 HIS P 226 PGV P1267 HOH P4189
SITE 4 EC9 13 THR W 27
SITE 1 FC1 4 ARG P 156 PHE P 164 LEU P 223 PHE W 1
SITE 1 FC2 18 PHE N 321 LEU N 324 HOH N4424 ILE O 41
SITE 2 FC2 18 HIS O 52 MET O 56 ASP O 57 VAL O 61
SITE 3 FC2 18 TRP O 65 GLU R 6 ASP R 8 PHE R 11
SITE 4 FC2 18 ASP R 40 LEU R 41 HOH R3122 HOH R3394
SITE 5 FC2 18 ARG V 10 ALA V 14
SITE 1 FC3 4 CYS S 60 CYS S 62 CYS S 82 CYS S 85
SITE 1 FC4 14 LYS C 77 ARG C 80 TYR C 81 ILE C 84
SITE 2 FC4 14 VAL C 91 THR C 95 PHE C 98 VAL C 247
SITE 3 FC4 14 HOH C4713 SER T 2 ALA T 3 LYS T 5
SITE 4 FC4 14 GLY T 6 HIS T 8
SITE 1 FC5 8 CHD B1086 HIS P 158 GLN P 161 THR P 168
SITE 2 FC5 8 HOH P4242 ARG T 17 TRP T 36 CDL T1269
SITE 1 FC6 22 PHE A 282 ASP A 300 SER A 307 ILE A 311
SITE 2 FC6 22 LEU B 73 LEU B 78 LEU B 81 ARG B 82
SITE 3 FC6 22 TYR B 85 CHD C 525 LEU P 131 TYR P 253
SITE 4 FC6 22 VAL P 254 TRP P 258 LEU T 23 SER T 27
SITE 5 FC6 22 LEU T 30 CYS T 31 ASN T 34 HIS T 38
SITE 6 FC6 22 PEK T1265 HOH T4409
SITE 1 FC7 5 LEU N 7 PHE N 8 TYR W 32 ARG W 33
SITE 2 FC7 5 THR W 37
SITE 1 FC8 18 THR N 17 LEU N 18 LEU N 21 PHE N 22
SITE 2 FC8 18 TRP N 81 PRO N 106 LEU N 113 PHE N 400
SITE 3 FC8 18 ILE Y 11 PRO Y 12 PHE Y 13 SER Y 14
SITE 4 FC8 18 ARG Y 20 MET Y 24 MET Y 25 PHE Y 28
SITE 5 FC8 18 PHE Y 29 HOH Y4350
SITE 1 FC9 9 LEU Q 95 TRP Q 98 TYR Q 102 LEU Z 27
SITE 2 FC9 9 LEU Z 28 GLY Z 31 TRP Z 32 TYR Z 35
SITE 3 FC9 9 HIS Z 36
CRYST1 183.697 206.991 178.251 90.00 90.00 90.00 P 21 21 21 8
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 0.005444 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004831 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005610 0.00000
HETATM 1 N FME A 1 53.798 335.156 224.481 1.00 50.38 N
HETATM 2 CN FME A 1 54.711 335.246 223.547 1.00 51.14 C
HETATM 3 O1 FME A 1 54.954 336.217 222.972 1.00 51.53 O
HETATM 4 CA FME A 1 53.800 333.755 224.840 1.00 51.42 C
HETATM 5 CB FME A 1 52.931 333.428 226.051 1.00 53.91 C
HETATM 6 CG FME A 1 53.650 332.617 227.133 1.00 62.46 C
HETATM 7 SD FME A 1 54.903 333.593 227.951 1.00 78.70 S
HETATM 8 CE FME A 1 56.462 333.686 227.095 1.00 72.17 C
HETATM 9 C FME A 1 53.538 332.907 223.583 1.00 49.09 C
HETATM 10 O FME A 1 54.357 332.048 223.269 1.00 48.05 O
(ATOM LINES ARE NOT SHOWN.)
END
