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PDBsum entry 3omi

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3omi
Jmol
Contents
Protein chains
535 a.a.
256 a.a.
Ligands
_OH ×2
DMU ×11
TRD ×9
HEA ×4
HTH
Metals
_CL ×2
_CD ×4
_CU ×4
_MG ×2
_CA ×2
CU1 ×2
_FE
Waters ×491
HEADER    OXIDOREDUCTASE                          27-AUG-10   3OMI
TITLE     CATALYTIC CORE SUBUNITS (I AND II) OF CYTOCHROME C OXIDASE FROM
TITLE    2 RHODOBACTER SPHAEROIDES WITH D132A MUTATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYTOCHROME C OXIDASE, AA3 TYPE, SUBUNIT I;
COMPND   3 CHAIN: A, C;
COMPND   4 FRAGMENT: UNP RESIDUES 17-551;
COMPND   5 EC: 1.9.3.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND  10 CHAIN: B, D;
COMPND  11 FRAGMENT: UNP RESIDUES 30-281;
COMPND  12 EC: 1.9.3.1;
COMPND  13 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES 2.4.1;
SOURCE   3 ORGANISM_TAXID: 272943;
SOURCE   4 STRAIN: ATCC 17023/2.4.1/NCIB 8253/DSM 158;
SOURCE   5 GENE: COXI, CTAD, RHOS4_04590, RSP_1877;
SOURCE   6 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRK415-1;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES 2.4.1;
SOURCE  12 ORGANISM_TAXID: 272943;
SOURCE  13 STRAIN: ATCC 17023/2.4.1/NCIB 8253/DSM 158;
SOURCE  14 GENE: COXII, CTAB, CTAC, RHOS4_04060, RSP_1826;
SOURCE  15 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PRK415-1
KEYWDS    TRANSMEMBRANE PROTEIN COMPLEX, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.LIU,L.QIN,S.FERGUSON-MILLER
REVDAT   3   02-MAY-12 3OMI    1       COMPND VERSN
REVDAT   2   16-MAR-11 3OMI    1       JRNL
REVDAT   1   02-FEB-11 3OMI    0
JRNL        AUTH   J.LIU,L.QIN,S.FERGUSON-MILLER
JRNL        TITL   CRYSTALLOGRAPHIC AND ONLINE SPECTRAL EVIDENCE FOR ROLE OF
JRNL        TITL 2 CONFORMATIONAL CHANGE AND CONSERVED WATER IN CYTOCHROME
JRNL        TITL 3 OXIDASE PROTON PUMP.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  1284 2011
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   21205904
JRNL        DOI    10.1073/PNAS.1012846108
REMARK   2
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.84
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5
REMARK   3   NUMBER OF REFLECTIONS             : 151679
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) : 0.193
REMARK   3   R VALUE            (WORKING SET) : 0.192
REMARK   3   FREE R VALUE                     : 0.215
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4574
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) : 2.15
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7705
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.36
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520
REMARK   3   BIN FREE R VALUE SET COUNT          : 231
REMARK   3   BIN FREE R VALUE                    : 0.2930
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 12279
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 646
REMARK   3   SOLVENT ATOMS            : 491
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.49
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.61000
REMARK   3    B22 (A**2) : -0.37000
REMARK   3    B33 (A**2) : 1.99000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
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): 0.095
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.594
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13333 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18197 ; 1.164 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1573 ; 5.540 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   502 ;36.208 ;22.769
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1804 ;13.436 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;18.227 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2011 ; 0.084 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10036 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7023 ; 0.200 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9302 ; 0.313 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   656 ; 0.139 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    21 ; 0.121 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    51 ; 0.182 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.073 ; 0.200
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):  8027 ; 0.657 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12608 ; 1.072 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6264 ; 1.484 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5587 ; 2.112 ; 4.500
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 : MASK
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:
REMARK   3  THERE IS RESIDUAL DENSITY IN (FO-FC) DIFFERENCE FOURIER MAP AT THE
REMARK   3  MAGNESIUM SITES IN BOTH MOLECULES AND THE B-FACTOR FOR EACH
REMARK   3  MAGNESIUM ION IS UNUSUALLY LOW. THESE OBSERVATIONS SUGGEST THAT
REMARK   3  THIS MAGNESIUM SITE MAY BE PARTIALLY OCCUPIED BY A HEAVIER META ION
REMARK   3  IN THE PROTEIN CRYSTAL.
REMARK   3  THERE ARE RESIDUAL DENSITIES IN (FO-FC) DIFFERENCE FOURIER MAP AT
REMARK   3  THE SITE OF CU AND HEMEA FE. THESE DENSITIES SUGGEST THAT THE
REMARK   3  METEAL CENTER OF THIS MUTATNT MIGHT BE IN A STATE DIFFERENT FROM
REMARK   3  WILD TYPE IN CRYSTAL.
REMARK   4
REMARK   4 3OMI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061302.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 21-ID-G
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872
REMARK 200  MONOCHROMATOR                  : DIAMOND
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 151816
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 6.900
REMARK 200  R MERGE                    (I) : 0.09200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.55600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WEAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 69.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-29% PEG 400, PH 6.3, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K, VAPOR DIFFUSION,
REMARK 280  SITTING DROP
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       62.53200
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.83700
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.75950
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       87.83700
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       62.53200
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.75950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -185.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -196.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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     PHE C    17
REMARK 465     THR C    18
REMARK 465     ARG C    19
REMARK 465     THR C   550
REMARK 465     PHE C   551
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     PHE A  17    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     THR A  18    OG1  CG2
REMARK 470     ARG A  19    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A  72    CG   CD1  CD2
REMARK 470     VAL A  73    CG1  CG2
REMARK 470     LYS A  74    CG   CD   CE   NZ
REMARK 470     HIS A 223    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS A 224    CE   NZ
REMARK 470     GLU A 533    CG   CD   OE1  OE2
REMARK 470     GLU A 548    CG   CD   OE1  OE2
REMARK 470     HIS A 549    ND1  CD2  CE1  NE2
REMARK 470     LYS B  86    CE   NZ
REMARK 470     LYS B  89    CE   NZ
REMARK 470     GLU B 131    CG   CD   OE1  OE2
REMARK 470     GLU B 273    CG   CD   OE1  OE2
REMARK 470     HIS B 284    CG   ND1  CD2  CE1  NE2
REMARK 470     TRP C  20    CG   CD1  CD2  NE1  CE2  CE3  CZ2
REMARK 470     TRP C  20    CZ3  CH2
REMARK 470     LEU C  72    CG   CD1  CD2
REMARK 470     LYS C  74    CG   CD   CE   NZ
REMARK 470     GLN C  78    CG   CD   OE1  NE2
REMARK 470     HIS C 223    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS C 224    CG   CD   CE   NZ
REMARK 470     TYR C 318    CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU C 488    CG   CD   OE1  OE2
REMARK 470     ARG C 521    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C 524    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C 548    CG   CD   OE1  OE2
REMARK 470     HIS C 549    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS D  86    CG   CD   CE   NZ
REMARK 470     LYS D  89    CG   CD   CE   NZ
REMARK 470     ARG D  93    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 131    CG   CD   OE1  OE2
REMARK 470     HIS D 284    CG   ND1  CD2  CE1  NE2
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     OH C   741     O    HOH C   743              1.93
REMARK 500   O     OH A   741     O    HOH A   742              1.94
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    GLU A  69   CD    GLU A  69   OE2     0.082
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    VAL A 110      -76.25   -126.23
REMARK 500    GLN A 165     -169.30   -115.86
REMARK 500    MET A 335       19.82   -140.09
REMARK 500    LEU A 377       48.64    -89.07
REMARK 500    ARG A 482       30.54     70.66
REMARK 500    ARG A 521       22.88   -147.40
REMARK 500    TRP A 531      -97.28    -97.22
REMARK 500    ASN B  97       73.20   -166.31
REMARK 500    ASP B 169       45.62   -140.70
REMARK 500    TYR B 185     -165.63   -119.26
REMARK 500    LEU B 191      -15.05     88.04
REMARK 500    ASP B 214      -61.09   -138.77
REMARK 500    VAL C 110      -74.23   -123.63
REMARK 500    MET C 220       88.94    -61.35
REMARK 500    LEU C 377       56.05    -95.85
REMARK 500    ARG C 482       30.52     73.63
REMARK 500    THR C 520      -63.98    -97.03
REMARK 500    ALA C 523      121.20    -35.95
REMARK 500    TRP C 531      -89.24   -105.10
REMARK 500    ASN D  97       86.00   -177.07
REMARK 500    ASP D 169       45.35   -142.67
REMARK 500    TYR D 185     -162.61   -105.56
REMARK 500    LEU D 191      -15.48     88.30
REMARK 500    ASP D 214      -62.67   -142.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    HIS A 284        24.4      L          L   OUTSIDE RANGE
REMARK 500    PHE A 420        25.0      L          L   OUTSIDE RANGE
REMARK 500    HIS C 284        24.5      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 LIGANDS LABELLED AS TRD ARE ALL ALKYL CHAINS WITH DIFFERENT LENGTHS
REMARK 600 OF EITHER DMU OR NATIVE MEMBRANE LIPIDS SUCH AS PHOSPHATIDYL
REMARK 600 ETHANOLAMINE OR CARDIOLIPIN. THE AUTHORS DO NOT KNOW FOR SURE THE
REMARK 600 IDENTITIES OF THE COMPLETE MOLECULES.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     DMU A    7
REMARK 610     DMU A 1005
REMARK 610     TRD A 1009
REMARK 610     TRD A 1013
REMARK 610     TRD A 1015
REMARK 610     DMU B    6
REMARK 610     TRD B    4
REMARK 610     DMU C    5
REMARK 610     DMU C    9
REMARK 610     HEA C  552
REMARK 610     TRD C  553
REMARK 610     DMU D    4
REMARK 610     DMU D    8
REMARK 610     TRD D   14
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                              FE C   1  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEA C 552   NB
REMARK 620 2 HEA C 552   ND  178.6
REMARK 620 3 HIS C 102   NE2  94.3  86.9
REMARK 620 4 HIS C 421   NE2  90.4  88.5 174.8
REMARK 620 5 HEA C 552   NC   94.1  86.7  85.6  91.8
REMARK 620 6 HEA C 552   NA   87.9  91.3  92.6  89.9 177.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CD B   9  CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 101   OE2
REMARK 620 2 GLU B 101   OE1  58.8
REMARK 620 3 HIS B  96   ND1 115.2 166.4
REMARK 620 4 HOH B 761   O   150.0  91.2  94.1
REMARK 620 5 HOH B 708   O    82.2  84.8  82.2  96.4
REMARK 620 6 HOH B 762   O    86.7 100.3  91.1  99.6 163.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C   6  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 254   OE1
REMARK 620 2 ASP C 412   OD2  97.0
REMARK 620 3 HOH C 568   O    92.3 167.9
REMARK 620 4 HOH D 316   O    89.2  93.4  94.4
REMARK 620 5 HOH D 314   O    87.4  85.3  87.5 176.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU A   5  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 333   NE2
REMARK 620 2 HIS A 334   NE2  97.8
REMARK 620 3 HIS A 284   ND1  98.0 143.7
REMARK 620 4  OH A 741   O   150.6  87.5  94.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CD B   8  CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 280   OE1
REMARK 620 2 HIS B 285   NE2  82.0
REMARK 620 3 HIS B 283   ND1 137.1  95.0
REMARK 620 4 GLU B 280   OE2  57.6 135.3 101.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA A   1  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 102   NE2
REMARK 620 2 HEA A   1   NA   92.7
REMARK 620 3 HEA A   1   NB   93.7  88.4
REMARK 620 4 HEA A   1   NC   86.2 178.7  90.9
REMARK 620 5 HEA A   1   ND   87.8  89.1 177.2  91.6
REMARK 620 6 HIS A 421   NE2 176.5  90.8  86.5  90.3  92.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A   6  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 254   OE1
REMARK 620 2 ASP A 412   OD2  94.9
REMARK 620 3 HOH B 503   O    82.5 173.4
REMARK 620 4 HOH B 797   O    91.5  91.0  95.0
REMARK 620 5 HOH B 793   O    87.5  89.0  84.9 179.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU D 286  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 260   ND1
REMARK 620 2 CYS D 252   SG  128.3
REMARK 620 3 CYS D 256   SG  113.5 115.9
REMARK 620 4 CU1 D 287  CU   157.7  57.9  58.5
REMARK 620 5 GLU D 254   O    89.0  97.6  98.7 112.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CD D 288  CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 280   OE1
REMARK 620 2 HIS D 283   ND1 136.7
REMARK 620 3 HIS D 285   NE2  88.0  88.5
REMARK 620 4 GLU D 280   OE2  58.3 106.1 143.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CU1 D 287  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 217   ND1
REMARK 620 2 CYS D 252   SG  119.9
REMARK 620 3 CYS D 256   SG   99.6 109.4
REMARK 620 4 MET D 263   SD   98.7 117.8 109.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU B 287  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 260   ND1
REMARK 620 2 CYS B 252   SG  129.8
REMARK 620 3 CYS B 256   SG  115.3 112.4
REMARK 620 4 GLU B 254   O    89.1  99.2  98.0
REMARK 620 5 CU1 B 288  CU   159.0  55.2  57.6 111.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CU1 B 288  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 217   ND1
REMARK 620 2 CYS B 252   SG  118.5
REMARK 620 3 CYS B 256   SG  101.5 109.9
REMARK 620 4 MET B 263   SD  100.7 114.3 111.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU C 554  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 333   NE2
REMARK 620 2 HIS C 334   NE2  97.3
REMARK 620 3 HIS C 284   ND1  96.2 146.2
REMARK 620 4  OH C 741   O   145.4  87.5  98.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA A   2  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 419   NE2
REMARK 620 2 HEA A   2   NA   90.6
REMARK 620 3 HEA A   2   NB   96.8  88.5
REMARK 620 4 HEA A   2   NC   98.4 170.9  90.0
REMARK 620 5 HEA A   2   ND   94.2  90.3 168.9  89.4
REMARK 620 6 HOH A 742   O   174.5  85.4  86.9  85.6  82.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA C   2  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 419   NE2
REMARK 620 2 HEA C   2   NA   90.7
REMARK 620 3 HEA C   2   NB   95.0  88.6
REMARK 620 4 HEA C   2   NC   96.8 172.5  91.1
REMARK 620 5 HEA C   2   ND   94.5  92.3 170.5  86.8
REMARK 620 6 HOH C 743   O   174.9  84.4  83.7  88.2  87.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CD D   9  CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 101   OE2
REMARK 620 2 GLU D 101   OE1  58.7
REMARK 620 3 HIS D  96   ND1 172.6 114.2
REMARK 620 4 HOH D 379   O    88.4 147.0  98.7
REMARK 620 5 HOH D 380   O    81.8  88.3  96.4  85.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA C   7  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C  54   O
REMARK 620 2 ALA C  57   O    93.8
REMARK 620 3 GLU C  54   OE1  82.7 175.6
REMARK 620 4 GLY C  59   O   152.7  83.8  98.3
REMARK 620 5 GLN C  61   OE1 135.0 103.8  80.5  71.3
REMARK 620 6 HOH C 569   O    75.5  86.6  90.1  77.2 145.3
REMARK 620 7 HOH C 582   O    70.9  83.0  98.2 135.2  70.7 143.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 553  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A  59   O
REMARK 620 2 GLU A  54   O   149.0
REMARK 620 3 ALA A  57   O    84.5  95.2
REMARK 620 4 GLU A  54   OE1  94.0  84.6 176.6
REMARK 620 5 GLN A  61   OE1  76.1 133.7 101.3  81.2
REMARK 620 6 HOH A 808   O    70.3  78.8  85.8  90.8 144.8
REMARK 620 7 HOH A 815   O   142.4  68.3  86.8  96.2  69.8 145.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH A 741
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRD A 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRD A 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRD A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 553
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRD B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTH B 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 287
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH C 741
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU C 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU C 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA C 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA C 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRD C 553
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 554
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU D 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU D 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRD D 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 D 287
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 9
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GSM   RELATED DB: PDB
REMARK 900 THE WILD TYPE FORM OF THIS MUTANT.
REMARK 900 RELATED ID: 3OM3   RELATED DB: PDB
REMARK 900 THE SAME KIND PROTEIN CRYSTAL REDUCED WITH SODIUM
REMARK 900 DITHIONITE.
REMARK 900 RELATED ID: 3OMA   RELATED DB: PDB
REMARK 900 RELATED ID: 3OMN   RELATED DB: PDB
DBREF  3OMI A   17   551  UNP    Q3J5A7   Q3J5A7_RHOS4    17    551
DBREF  3OMI B   30   281  UNP    Q3J5G0   Q3J5G0_RHOS4    30    281
DBREF  3OMI C   17   551  UNP    Q3J5A7   Q3J5A7_RHOS4    17    551
DBREF  3OMI D   30   281  UNP    Q3J5G0   Q3J5G0_RHOS4    30    281
SEQADV 3OMI ALA A  132  UNP  Q3J5A7    ASP   132 ENGINEERED MUTATION
SEQADV 3OMI HIS B  282  UNP  Q3J5G0              EXPRESSION TAG
SEQADV 3OMI HIS B  283  UNP  Q3J5G0              EXPRESSION TAG
SEQADV 3OMI HIS B  284  UNP  Q3J5G0              EXPRESSION TAG
SEQADV 3OMI HIS B  285  UNP  Q3J5G0              EXPRESSION TAG
SEQADV 3OMI ALA C  132  UNP  Q3J5A7    ASP   132 ENGINEERED MUTATION
SEQADV 3OMI HIS D  282  UNP  Q3J5G0              EXPRESSION TAG
SEQADV 3OMI HIS D  283  UNP  Q3J5G0              EXPRESSION TAG
SEQADV 3OMI HIS D  284  UNP  Q3J5G0              EXPRESSION TAG
SEQADV 3OMI HIS D  285  UNP  Q3J5G0              EXPRESSION TAG
SEQRES   1 A  535  PHE THR ARG TRP PHE MET SER THR ASN HIS LYS ASP ILE
SEQRES   2 A  535  GLY VAL LEU TYR LEU PHE THR GLY GLY LEU VAL GLY LEU
SEQRES   3 A  535  ILE SER VAL ALA PHE THR VAL TYR MET ARG MET GLU LEU
SEQRES   4 A  535  MET ALA PRO GLY VAL GLN PHE MET CYS ALA GLU HIS LEU
SEQRES   5 A  535  GLU SER GLY LEU VAL LYS GLY PHE PHE GLN SER LEU TRP
SEQRES   6 A  535  PRO SER ALA VAL GLU ASN CYS THR PRO ASN GLY HIS LEU
SEQRES   7 A  535  TRP ASN VAL MET ILE THR GLY HIS GLY ILE LEU MET MET
SEQRES   8 A  535  PHE PHE VAL VAL ILE PRO ALA LEU PHE GLY GLY PHE GLY
SEQRES   9 A  535  ASN TYR PHE MET PRO LEU HIS ILE GLY ALA PRO ALA MET
SEQRES  10 A  535  ALA PHE PRO ARG MET ASN ASN LEU SER TYR TRP LEU TYR
SEQRES  11 A  535  VAL ALA GLY THR SER LEU ALA VAL ALA SER LEU PHE ALA
SEQRES  12 A  535  PRO GLY GLY ASN GLY GLN LEU GLY SER GLY ILE GLY TRP
SEQRES  13 A  535  VAL LEU TYR PRO PRO LEU SER THR SER GLU SER GLY TYR
SEQRES  14 A  535  SER THR ASP LEU ALA ILE PHE ALA VAL HIS LEU SER GLY
SEQRES  15 A  535  ALA SER SER ILE LEU GLY ALA ILE ASN MET ILE THR THR
SEQRES  16 A  535  PHE LEU ASN MET ARG ALA PRO GLY MET THR MET HIS LYS
SEQRES  17 A  535  VAL PRO LEU PHE ALA TRP SER ILE PHE VAL THR ALA TRP
SEQRES  18 A  535  LEU ILE LEU LEU ALA LEU PRO VAL LEU ALA GLY ALA ILE
SEQRES  19 A  535  THR MET LEU LEU THR ASP ARG ASN PHE GLY THR THR PHE
SEQRES  20 A  535  PHE GLN PRO SER GLY GLY GLY ASP PRO VAL LEU TYR GLN
SEQRES  21 A  535  HIS ILE LEU TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE
SEQRES  22 A  535  ILE VAL LEU PRO ALA PHE GLY ILE VAL SER HIS VAL ILE
SEQRES  23 A  535  ALA THR PHE ALA LYS LYS PRO ILE PHE GLY TYR LEU PRO
SEQRES  24 A  535  MET VAL TYR ALA MET VAL ALA ILE GLY VAL LEU GLY PHE
SEQRES  25 A  535  VAL VAL TRP ALA HIS HIS MET TYR THR ALA GLY LEU SER
SEQRES  26 A  535  LEU THR GLN GLN SER TYR PHE MET MET ALA THR MET VAL
SEQRES  27 A  535  ILE ALA VAL PRO THR GLY ILE LYS ILE PHE SER TRP ILE
SEQRES  28 A  535  ALA THR MET TRP GLY GLY SER ILE GLU LEU LYS THR PRO
SEQRES  29 A  535  MET LEU TRP ALA LEU GLY PHE LEU PHE LEU PHE THR VAL
SEQRES  30 A  535  GLY GLY VAL THR GLY ILE VAL LEU SER GLN ALA SER VAL
SEQRES  31 A  535  ASP ARG TYR TYR HIS ASP THR TYR TYR VAL VAL ALA HIS
SEQRES  32 A  535  PHE HIS TYR VAL MET SER LEU GLY ALA VAL PHE GLY ILE
SEQRES  33 A  535  PHE ALA GLY ILE TYR PHE TRP ILE GLY LYS MET SER GLY
SEQRES  34 A  535  ARG GLN TYR PRO GLU TRP ALA GLY LYS LEU HIS PHE TRP
SEQRES  35 A  535  MET MET PHE VAL GLY ALA ASN LEU THR PHE PHE PRO GLN
SEQRES  36 A  535  HIS PHE LEU GLY ARG GLN GLY MET PRO ARG ARG TYR ILE
SEQRES  37 A  535  ASP TYR PRO GLU ALA PHE ALA THR TRP ASN PHE VAL SER
SEQRES  38 A  535  SER LEU GLY ALA PHE LEU SER PHE ALA SER PHE LEU PHE
SEQRES  39 A  535  PHE LEU GLY VAL ILE PHE TYR THR LEU THR ARG GLY ALA
SEQRES  40 A  535  ARG VAL THR ALA ASN ASN TYR TRP ASN GLU HIS ALA ASP
SEQRES  41 A  535  THR LEU GLU TRP THR LEU THR SER PRO PRO PRO GLU HIS
SEQRES  42 A  535  THR PHE
SEQRES   1 B  256  LEU GLU ILE ILE GLY ARG PRO GLN PRO GLY GLY THR GLY
SEQRES   2 B  256  PHE GLN PRO SER ALA SER PRO VAL ALA THR GLN ILE HIS
SEQRES   3 B  256  TRP LEU ASP GLY PHE ILE LEU VAL ILE ILE ALA ALA ILE
SEQRES   4 B  256  THR ILE PHE VAL THR LEU LEU ILE LEU TYR ALA VAL TRP
SEQRES   5 B  256  ARG PHE HIS GLU LYS ARG ASN LYS VAL PRO ALA ARG PHE
SEQRES   6 B  256  THR HIS ASN SER PRO LEU GLU ILE ALA TRP THR ILE VAL
SEQRES   7 B  256  PRO ILE VAL ILE LEU VAL ALA ILE GLY ALA PHE SER LEU
SEQRES   8 B  256  PRO VAL LEU PHE ASN GLN GLN GLU ILE PRO GLU ALA ASP
SEQRES   9 B  256  VAL THR VAL LYS VAL THR GLY TYR GLN TRP TYR TRP GLY
SEQRES  10 B  256  TYR GLU TYR PRO ASP GLU GLU ILE SER PHE GLU SER TYR
SEQRES  11 B  256  MET ILE GLY SER PRO ALA THR GLY GLY ASP ASN ARG MET
SEQRES  12 B  256  SER PRO GLU VAL GLU GLN GLN LEU ILE GLU ALA GLY TYR
SEQRES  13 B  256  SER ARG ASP GLU PHE LEU LEU ALA THR ASP THR ALA MET
SEQRES  14 B  256  VAL VAL PRO VAL ASN LYS THR VAL VAL VAL GLN VAL THR
SEQRES  15 B  256  GLY ALA ASP VAL ILE HIS SER TRP THR VAL PRO ALA PHE
SEQRES  16 B  256  GLY VAL LYS GLN ASP ALA VAL PRO GLY ARG LEU ALA GLN
SEQRES  17 B  256  LEU TRP PHE ARG ALA GLU ARG GLU GLY ILE PHE PHE GLY
SEQRES  18 B  256  GLN CYS SER GLU LEU CYS GLY ILE SER HIS ALA TYR MET
SEQRES  19 B  256  PRO ILE THR VAL LYS VAL VAL SER GLU GLU ALA TYR ALA
SEQRES  20 B  256  ALA TRP LEU GLU GLN HIS HIS HIS HIS
SEQRES   1 C  535  PHE THR ARG TRP PHE MET SER THR ASN HIS LYS ASP ILE
SEQRES   2 C  535  GLY VAL LEU TYR LEU PHE THR GLY GLY LEU VAL GLY LEU
SEQRES   3 C  535  ILE SER VAL ALA PHE THR VAL TYR MET ARG MET GLU LEU
SEQRES   4 C  535  MET ALA PRO GLY VAL GLN PHE MET CYS ALA GLU HIS LEU
SEQRES   5 C  535  GLU SER GLY LEU VAL LYS GLY PHE PHE GLN SER LEU TRP
SEQRES   6 C  535  PRO SER ALA VAL GLU ASN CYS THR PRO ASN GLY HIS LEU
SEQRES   7 C  535  TRP ASN VAL MET ILE THR GLY HIS GLY ILE LEU MET MET
SEQRES   8 C  535  PHE PHE VAL VAL ILE PRO ALA LEU PHE GLY GLY PHE GLY
SEQRES   9 C  535  ASN TYR PHE MET PRO LEU HIS ILE GLY ALA PRO ALA MET
SEQRES  10 C  535  ALA PHE PRO ARG MET ASN ASN LEU SER TYR TRP LEU TYR
SEQRES  11 C  535  VAL ALA GLY THR SER LEU ALA VAL ALA SER LEU PHE ALA
SEQRES  12 C  535  PRO GLY GLY ASN GLY GLN LEU GLY SER GLY ILE GLY TRP
SEQRES  13 C  535  VAL LEU TYR PRO PRO LEU SER THR SER GLU SER GLY TYR
SEQRES  14 C  535  SER THR ASP LEU ALA ILE PHE ALA VAL HIS LEU SER GLY
SEQRES  15 C  535  ALA SER SER ILE LEU GLY ALA ILE ASN MET ILE THR THR
SEQRES  16 C  535  PHE LEU ASN MET ARG ALA PRO GLY MET THR MET HIS LYS
SEQRES  17 C  535  VAL PRO LEU PHE ALA TRP SER ILE PHE VAL THR ALA TRP
SEQRES  18 C  535  LEU ILE LEU LEU ALA LEU PRO VAL LEU ALA GLY ALA ILE
SEQRES  19 C  535  THR MET LEU LEU THR ASP ARG ASN PHE GLY THR THR PHE
SEQRES  20 C  535  PHE GLN PRO SER GLY GLY GLY ASP PRO VAL LEU TYR GLN
SEQRES  21 C  535  HIS ILE LEU TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE
SEQRES  22 C  535  ILE VAL LEU PRO ALA PHE GLY ILE VAL SER HIS VAL ILE
SEQRES  23 C  535  ALA THR PHE ALA LYS LYS PRO ILE PHE GLY TYR LEU PRO
SEQRES  24 C  535  MET VAL TYR ALA MET VAL ALA ILE GLY VAL LEU GLY PHE
SEQRES  25 C  535  VAL VAL TRP ALA HIS HIS MET TYR THR ALA GLY LEU SER
SEQRES  26 C  535  LEU THR GLN GLN SER TYR PHE MET MET ALA THR MET VAL
SEQRES  27 C  535  ILE ALA VAL PRO THR GLY ILE LYS ILE PHE SER TRP ILE
SEQRES  28 C  535  ALA THR MET TRP GLY GLY SER ILE GLU LEU LYS THR PRO
SEQRES  29 C  535  MET LEU TRP ALA LEU GLY PHE LEU PHE LEU PHE THR VAL
SEQRES  30 C  535  GLY GLY VAL THR GLY ILE VAL LEU SER GLN ALA SER VAL
SEQRES  31 C  535  ASP ARG TYR TYR HIS ASP THR TYR TYR VAL VAL ALA HIS
SEQRES  32 C  535  PHE HIS TYR VAL MET SER LEU GLY ALA VAL PHE GLY ILE
SEQRES  33 C  535  PHE ALA GLY ILE TYR PHE TRP ILE GLY LYS MET SER GLY
SEQRES  34 C  535  ARG GLN TYR PRO GLU TRP ALA GLY LYS LEU HIS PHE TRP
SEQRES  35 C  535  MET MET PHE VAL GLY ALA ASN LEU THR PHE PHE PRO GLN
SEQRES  36 C  535  HIS PHE LEU GLY ARG GLN GLY MET PRO ARG ARG TYR ILE
SEQRES  37 C  535  ASP TYR PRO GLU ALA PHE ALA THR TRP ASN PHE VAL SER
SEQRES  38 C  535  SER LEU GLY ALA PHE LEU SER PHE ALA SER PHE LEU PHE
SEQRES  39 C  535  PHE LEU GLY VAL ILE PHE TYR THR LEU THR ARG GLY ALA
SEQRES  40 C  535  ARG VAL THR ALA ASN ASN TYR TRP ASN GLU HIS ALA ASP
SEQRES  41 C  535  THR LEU GLU TRP THR LEU THR SER PRO PRO PRO GLU HIS
SEQRES  42 C  535  THR PHE
SEQRES   1 D  256  LEU GLU ILE ILE GLY ARG PRO GLN PRO GLY GLY THR GLY
SEQRES   2 D  256  PHE GLN PRO SER ALA SER PRO VAL ALA THR GLN ILE HIS
SEQRES   3 D  256  TRP LEU ASP GLY PHE ILE LEU VAL ILE ILE ALA ALA ILE
SEQRES   4 D  256  THR ILE PHE VAL THR LEU LEU ILE LEU TYR ALA VAL TRP
SEQRES   5 D  256  ARG PHE HIS GLU LYS ARG ASN LYS VAL PRO ALA ARG PHE
SEQRES   6 D  256  THR HIS ASN SER PRO LEU GLU ILE ALA TRP THR ILE VAL
SEQRES   7 D  256  PRO ILE VAL ILE LEU VAL ALA ILE GLY ALA PHE SER LEU
SEQRES   8 D  256  PRO VAL LEU PHE ASN GLN GLN GLU ILE PRO GLU ALA ASP
SEQRES   9 D  256  VAL THR VAL LYS VAL THR GLY TYR GLN TRP TYR TRP GLY
SEQRES  10 D  256  TYR GLU TYR PRO ASP GLU GLU ILE SER PHE GLU SER TYR
SEQRES  11 D  256  MET ILE GLY SER PRO ALA THR GLY GLY ASP ASN ARG MET
SEQRES  12 D  256  SER PRO GLU VAL GLU GLN GLN LEU ILE GLU ALA GLY TYR
SEQRES  13 D  256  SER ARG ASP GLU PHE LEU LEU ALA THR ASP THR ALA MET
SEQRES  14 D  256  VAL VAL PRO VAL ASN LYS THR VAL VAL VAL GLN VAL THR
SEQRES  15 D  256  GLY ALA ASP VAL ILE HIS SER TRP THR VAL PRO ALA PHE
SEQRES  16 D  256  GLY VAL LYS GLN ASP ALA VAL PRO GLY ARG LEU ALA GLN
SEQRES  17 D  256  LEU TRP PHE ARG ALA GLU ARG GLU GLY ILE PHE PHE GLY
SEQRES  18 D  256  GLN CYS SER GLU LEU CYS GLY ILE SER HIS ALA TYR MET
SEQRES  19 D  256  PRO ILE THR VAL LYS VAL VAL SER GLU GLU ALA TYR ALA
SEQRES  20 D  256  ALA TRP LEU GLU GLN HIS HIS HIS HIS
HET     OH  A 741       1
HET    DMU  A   7      22
HET    DMU  A1005      22
HET    TRD  A1009       7
HET    TRD  A1013       7
HET    TRD  A1015       7
HET    HEA  A   1      60
HET    HEA  A   2      60
HET    TRD  A 552      13
HET    TRD  A   3      13
HET     CU  A   5       1
HET     MG  A   6       1
HET     CA  A 553       1
HET     CL  A  10       1
HET    DMU  B   1      33
HET    DMU  B   2      33
HET    DMU  B   3      33
HET    DMU  B   6      23
HET    TRD  B   4       9
HET    HTH  B 286      10
HET     CU  B 287       1
HET    CU1  B 288       1
HET     CD  B   8       1
HET     CD  B   9       1
HET     OH  C 741       1
HET    DMU  C  10      33
HET    DMU  C   5      23
HET    DMU  C   9      23
HET     FE  C   1       1
HET    HEA  C 552      59
HET    HEA  C   2      60
HET    TRD  C 553      11
HET     CU  C 554       1
HET     MG  C   6       1
HET     CA  C   7       1
HET     CL  C 555       1
HET    DMU  D   4      23
HET    DMU  D   8      23
HET    TRD  D   3      13
HET    TRD  D  14       7
HET     CU  D 286       1
HET    CU1  D 287       1
HET     CD  D 288       1
HET     CD  D   9       1
HETNAM      OH HYDROXIDE ION
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETNAM     TRD TRIDECANE
HETNAM     HEA HEME-A
HETNAM      CU COPPER (II) ION
HETNAM      MG MAGNESIUM ION
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     HTH (2S,3R)-HEPTANE-1,2,3-TRIOL
HETNAM     CU1 COPPER (I) ION
HETNAM      CD CADMIUM ION
HETNAM      FE FE (III) ION
HETSYN     DMU DECYLMALTOSIDE
HETSYN     TRD LIPID FRAGMENT
HETSYN     HTH HEPTANE-1,2,3-TRIOL
FORMUL   5   OH    2(H O 1-)
FORMUL   6  DMU    11(C22 H42 O11)
FORMUL   8  TRD    9(C13 H28)
FORMUL  11  HEA    4(C49 H56 FE N4 O6)
FORMUL  15   CU    4(CU 2+)
FORMUL  16   MG    2(MG 2+)
FORMUL  17   CA    2(CA 2+)
FORMUL  18   CL    2(CL 1-)
FORMUL  24  HTH    C7 H16 O3
FORMUL  26  CU1    2(CU 1+)
FORMUL  27   CD    4(CD 2+)
FORMUL  33   FE    FE 3+
FORMUL  49  HOH   *491(H2 O)
HELIX    1   1 ASN A   25  MET A   56  1                                  32
HELIX    2   2 CYS A   64  SER A   70  5                                   7
HELIX    3   3 GLY A   71  SER A   79  1                                   9
HELIX    4   4 ALA A   84  CYS A   88  5                                   5
HELIX    5   5 ASN A   91  VAL A  110  1                                  20
HELIX    6   6 VAL A  110  PHE A  116  1                                   7
HELIX    7   7 GLY A  118  ILE A  128  1                                  11
HELIX    8   8 PHE A  135  LEU A  157  1                                  23
HELIX    9   9 GLY A  161  GLN A  165  5                                   5
HELIX   10  10 PRO A  177  GLU A  182  1                                   6
HELIX   11  11 TYR A  185  MET A  215  1                                  31
HELIX   12  12 THR A  221  VAL A  225  5                                   5
HELIX   13  13 PRO A  226  PHE A  259  1                                  34
HELIX   14  14 GLN A  265  GLY A  269  5                                   5
HELIX   15  15 ASP A  271  LYS A  307  1                                  37
HELIX   16  16 GLY A  312  GLY A  327  1                                  16
HELIX   17  17 PHE A  328  VAL A  329  5                                   2
HELIX   18  18 VAL A  330  MET A  335  5                                   6
HELIX   19  19 SER A  341  ILE A  355  1                                  15
HELIX   20  20 ILE A  355  TRP A  371  1                                  17
HELIX   21  21 LYS A  378  GLN A  403  1                                  26
HELIX   22  22 GLN A  403  HIS A  411  1                                   9
HELIX   23  23 THR A  413  SER A  425  1                                  13
HELIX   24  24 GLY A  427  GLY A  445  1                                  19
HELIX   25  25 PRO A  449  GLN A  477  1                                  29
HELIX   26  26 PRO A  487  ALA A  489  5                                   3
HELIX   27  27 PHE A  490  GLY A  522  1                                  33
HELIX   28  28 THR A  537  LEU A  542  5                                   6
HELIX   29  29 SER B   48  PHE B   83  1                                  36
HELIX   30  30 ASN B   97  GLU B  128  1                                  32
HELIX   31  31 SER B  163  GLY B  167  5                                   5
HELIX   32  32 SER B  173  ALA B  183  1                                  11
HELIX   33  33 SER B  186  PHE B  190  5                                   5
HELIX   34  34 SER B  259  MET B  263  5                                   5
HELIX   35  35 SER B  271  HIS B  283  1                                  13
HELIX   36  36 ASN C   25  MET C   56  1                                  32
HELIX   37  37 CYS C   64  GLU C   69  5                                   6
HELIX   38  38 GLY C   71  SER C   79  1                                   9
HELIX   39  39 ALA C   84  CYS C   88  5                                   5
HELIX   40  40 ASN C   91  VAL C  110  1                                  20
HELIX   41  41 VAL C  110  PHE C  116  1                                   7
HELIX   42  42 GLY C  118  GLY C  129  1                                  12
HELIX   43  43 PHE C  135  LEU C  157  1                                  23
HELIX   44  44 GLY C  161  GLN C  165  5                                   5
HELIX   45  45 PRO C  177  GLU C  182  1                                   6
HELIX   46  46 TYR C  185  MET C  215  1                                  31
HELIX   47  47 THR C  221  VAL C  225  5                                   5
HELIX   48  48 PRO C  226  PHE C  259  1                                  34
HELIX   49  49 GLN C  265  GLY C  269  5                                   5
HELIX   50  50 ASP C  271  ALA C  306  1                                  36
HELIX   51  51 GLY C  312  GLY C  327  1                                  16
HELIX   52  52 PHE C  328  VAL C  329  5                                   2
HELIX   53  53 VAL C  330  MET C  335  5                                   6
HELIX   54  54 SER C  341  ILE C  355  1                                  15
HELIX   55  55 ILE C  355  TRP C  371  1                                  17
HELIX   56  56 LYS C  378  GLN C  403  1                                  26
HELIX   57  57 GLN C  403  HIS C  411  1                                   9
HELIX   58  58 THR C  413  SER C  425  1                                  13
HELIX   59  59 GLY C  427  GLY C  445  1                                  19
HELIX   60  60 PRO C  449  PHE C  469  1                                  21
HELIX   61  61 PHE C  469  GLN C  477  1                                   9
HELIX   62  62 PRO C  487  ALA C  489  5                                   3
HELIX   63  63 PHE C  490  GLY C  522  1                                  33
HELIX   64  64 THR C  537  THR C  541  5                                   5
HELIX   65  65 SER D   48  PHE D   83  1                                  36
HELIX   66  66 ASN D   97  GLU D  128  1                                  32
HELIX   67  67 SER D  163  GLY D  167  5                                   5
HELIX   68  68 SER D  173  ALA D  183  1                                  11
HELIX   69  69 SER D  186  PHE D  190  5                                   5
HELIX   70  70 PRO D  222  GLY D  225  5                                   4
HELIX   71  71 SER D  259  MET D  263  5                                   5
HELIX   72  72 SER D  271  HIS D  283  1                                  13
SHEET    1   A 2 ARG A 446  GLN A 447  0
SHEET    2   A 2 ALA A 523  ARG A 524 -1  O  ALA A 523   N  GLN A 447
SHEET    1   B 4 ILE B  32  GLY B  34  0
SHEET    2   B 4 GLY B 246  GLY B 250  1  O  PHE B 249   N  GLY B  34
SHEET    3   B 4 ILE B 265  VAL B 270 -1  O  ILE B 265   N  GLY B 250
SHEET    4   B 4 MET B 198  PRO B 201  1  N  MET B 198   O  THR B 266
SHEET    1   C 5 ILE B 154  SER B 158  0
SHEET    2   C 5 TYR B 144  TYR B 149 -1  N  TYR B 149   O  ILE B 154
SHEET    3   C 5 VAL B 134  TYR B 141 -1  N  LYS B 137   O  GLU B 148
SHEET    4   C 5 THR B 205  GLY B 212  1  O  GLN B 209   N  VAL B 138
SHEET    5   C 5 ALA B 236  ARG B 241 -1  O  ALA B 236   N  VAL B 210
SHEET    1   D 2 HIS B 217  VAL B 221  0
SHEET    2   D 2 VAL B 226  ALA B 230 -1  O  ALA B 230   N  HIS B 217
SHEET    1   E 4 ILE D  32  GLY D  34  0
SHEET    2   E 4 GLY D 246  GLY D 250  1  O  PHE D 249   N  GLY D  34
SHEET    3   E 4 ILE D 265  VAL D 270 -1  O  VAL D 269   N  GLY D 246
SHEET    4   E 4 MET D 198  PRO D 201  1  N  MET D 198   O  THR D 266
SHEET    1   F 5 ILE D 154  SER D 158  0
SHEET    2   F 5 TYR D 144  TYR D 149 -1  N  TYR D 149   O  ILE D 154
SHEET    3   F 5 VAL D 134  TYR D 141 -1  N  LYS D 137   O  GLU D 148
SHEET    4   F 5 THR D 205  GLY D 212  1  O  GLN D 209   N  VAL D 138
SHEET    5   F 5 ALA D 236  ARG D 241 -1  O  ALA D 236   N  VAL D 210
SHEET    1   G 2 HIS D 217  VAL D 221  0
SHEET    2   G 2 VAL D 226  ALA D 230 -1  O  ALA D 230   N  HIS D 217
SSBOND   1 CYS A   64    CYS A   88                          1555   1555  2.06
SSBOND   2 CYS C   64    CYS C   88                          1555   1555  2.05
LINK        FE    FE C   1                 NB  HEA C 552     1555   1555  1.95
LINK         OE2 GLU B 101                CD    CD B   9     1555   1555  1.96
LINK         OE1 GLU D 254                MG    MG C   6     1555   1555  2.01
LINK         NE2 HIS A 333                CU    CU A   5     1555   1555  2.01
LINK         OE1 GLU B 280                CD    CD B   8     1555   1555  2.02
LINK        FE    FE C   1                 ND  HEA C 552     1555   1555  2.02
LINK         NE2 HIS A 102                FE   HEA A   1     1555   1555  2.03
LINK         NE2 HIS A 421                FE   HEA A   1     1555   1555  2.05
LINK         OE1 GLU B 254                MG    MG A   6     1555   1555  2.05
LINK         ND1 HIS D 260                CU    CU D 286     1555   1555  2.05
LINK         NE2 HIS C 102                FE    FE C   1     1555   1555  2.06
LINK         OE1 GLU D 280                CD    CD D 288     1555   1555  2.06
LINK         ND1 HIS D 217                CU   CU1 D 287     1555   1555  2.06
LINK         ND1 HIS B 260                CU    CU B 287     1555   1555  2.08
LINK         NE2 HIS C 421                FE    FE C   1     1555   1555  2.08
LINK        FE    FE C   1                 NC  HEA C 552     1555   1555  2.09
LINK         OD2 ASP C 412                MG    MG C   6     1555   1555  2.09
LINK         ND1 HIS B 217                CU   CU1 B 288     1555   1555  2.10
LINK         NE2 HIS A 334                CU    CU A   5     1555   1555  2.11
LINK         NE2 HIS C 333                CU    CU C 554     1555   1555  2.11
LINK         NE2 HIS A 419                FE   HEA A   2     1555   1555  2.12
LINK         NE2 HIS C 334                CU    CU C 554     1555   1555  2.13
LINK        FE    FE C   1                 NA  HEA C 552     1555   1555  2.13
LINK         NE2 HIS C 419                FE   HEA C   2     1555   1555  2.15
LINK         ND1 HIS D 283                CD    CD D 288     1555   1555  2.16
LINK         OE2 GLU D 101                CD    CD D   9     1555   1555  2.18
LINK         NE2 HIS B 285                CD    CD B   8     1555   1555  2.18
LINK         ND1 HIS C 284                CU    CU C 554     1555   1555  2.22
LINK         ND1 HIS A 284                CU    CU A   5     1555   1555  2.24
LINK         SG  CYS D 252                CU    CU D 286     1555   1555  2.26
LINK         O   GLU C  54                CA    CA C   7     1555   1555  2.26
LINK         O   ALA C  57                CA    CA C   7     1555   1555  2.27
LINK         SG  CYS B 252                CU   CU1 B 288     1555   1555  2.27
LINK         OE1 GLU D 101                CD    CD D   9     1555   1555  2.28
LINK         SG  CYS B 252                CU    CU B 287     1555   1555  2.29
LINK         SG  CYS B 256                CU    CU B 287     1555   1555  2.29
LINK         OD2 ASP A 412                MG    MG A   6     1555   1555  2.29
LINK         SG  CYS D 256                CU    CU D 286     1555   1555  2.29
LINK         O   GLY A  59                CA    CA A 553     1555   1555  2.29
LINK         OE1 GLU C  54                CA    CA C   7     1555   1555  2.32
LINK         NE2 HIS D 285                CD    CD D 288     1555   1555  2.33
LINK         ND1 HIS B 283                CD    CD B   8     1555   1555  2.33
LINK         O   GLU A  54                CA    CA A 553     1555   1555  2.34
LINK         O   ALA A  57                CA    CA A 553     1555   1555  2.34
LINK         O    OH C 741                CU    CU C 554     1555   1555  2.34
LINK         SG  CYS D 252                CU   CU1 D 287     1555   1555  2.34
LINK         OE2 GLU D 280                CD    CD D 288     1555   1555  2.36
LINK         O    OH A 741                CU    CU A   5     1555   1555  2.36
LINK         O   GLY C  59                CA    CA C   7     1555   1555  2.36
LINK         SG  CYS B 256                CU   CU1 B 288     1555   1555  2.36
LINK         SG  CYS D 256                CU   CU1 D 287     1555   1555  2.38
LINK         OE1 GLU A  54                CA    CA A 553     1555   1555  2.38
LINK         SD  MET D 263                CU   CU1 D 287     1555   1555  2.39
LINK         SD  MET B 263                CU   CU1 B 288     1555   1555  2.39
LINK         OE1 GLU B 101                CD    CD B   9     1555   1555  2.41
LINK         OE2 GLU B 280                CD    CD B   8     1555   1555  2.44
LINK         OE1 GLN C  61                CA    CA C   7     1555   1555  2.45
LINK         OE1 GLN A  61                CA    CA A 553     1555   1555  2.51
LINK         ND1 HIS D  96                CD    CD D   9     1555   1555  2.54
LINK        CU    CU D 286                CU   CU1 D 287     1555   1555  2.56
LINK         ND1 HIS B  96                CD    CD B   9     1555   1555  2.56
LINK         O   GLU B 254                CU    CU B 287     1555   1555  2.58
LINK        CU    CU B 287                CU   CU1 B 288     1555   1555  2.59
LINK         O   GLU D 254                CU    CU D 286     1555   1555  2.60
LINK        MG    MG A   6                 O   HOH B 503     1555   1555  1.87
LINK        MG    MG C   6                 O   HOH C 568     1555   1555  1.89
LINK        CD    CD D   9                 O   HOH D 379     1555   1555  1.95
LINK        MG    MG C   6                 O   HOH D 316     1555   1555  2.00
LINK        MG    MG A   6                 O   HOH B 797     1555   1555  2.01
LINK        FE   HEA C   2                 O   HOH C 743     1555   1555  2.11
LINK        MG    MG A   6                 O   HOH B 793     1555   1555  2.14
LINK        FE   HEA A   2                 O   HOH A 742     1555   1555  2.15
LINK        CD    CD D   9                 O   HOH D 380     1555   1555  2.16
LINK        CD    CD B   9                 O   HOH B 761     1555   1555  2.18
LINK        MG    MG C   6                 O   HOH D 314     1555   1555  2.19
LINK        CD    CD B   9                 O   HOH B 708     1555   1555  2.25
LINK        CD    CD B   9                 O   HOH B 762     1555   1555  2.52
LINK        CA    CA C   7                 O   HOH C 569     1555   1555  2.59
LINK        CA    CA A 553                 O   HOH A 808     1555   1555  2.60
LINK        CA    CA A 553                 O   HOH A 815     1555   1555  2.64
LINK        CA    CA C   7                 O   HOH C 582     1555   1555  2.65
LINK         NE2 HIS A 284                 CE2 TYR A 288     1555   1555  1.38
LINK         NE2 HIS C 284                 CE2 TYR C 288     1555   1555  1.38
CISPEP   1 PRO A  176    PRO A  177          0        -4.84
CISPEP   2 SER A  544    PRO A  545          0        -3.07
CISPEP   3 GLN B  142    TRP B  143          0        -6.72
CISPEP   4 PRO C  176    PRO C  177          0        -6.36
CISPEP   5 SER C  544    PRO C  545          0         2.45
CISPEP   6 GLN D  142    TRP D  143          0        -4.54
SITE     1 AC1  6 HEA A   2   CU A   5  HIS A 284  VAL A 287
SITE     2 AC1  6 HIS A 334  HOH A 742
SITE     1 AC2  6 TRP A  20  VAL A  31  LEU A  34  MET A 443
SITE     2 AC2  6 SER A 444  HOH A 727
SITE     1 AC3  6 MET A  56  ALA A  57  GLN A  61  PHE A 502
SITE     2 AC3  6 TRD A 552  HOH A 815
SITE     1 AC4  2 PHE A  76  SER A  79
SITE     1 AC5 30 LEU A  34  GLY A  38  VAL A  45  THR A  48
SITE     2 AC5 30 MET A  51  ARG A  52  TRP A  95  ILE A  99
SITE     3 AC5 30 HIS A 102  MET A 106  MET A 107  VAL A 111
SITE     4 AC5 30 GLY A 171  TRP A 172  TYR A 414  PHE A 420
SITE     5 AC5 30 HIS A 421  MET A 424  SER A 425  VAL A 429
SITE     6 AC5 30 MET A 460  PHE A 468  GLN A 471  ARG A 481
SITE     7 AC5 30 ARG A 482  SER A 504  PHE A 508  HOH A 782
SITE     8 AC5 30 HOH A 784  HOH A 825
SITE     1 AC6 30 HOH A  15  TRP A 172  TRP A 280  VAL A 287
SITE     2 AC6 30 TYR A 288  HIS A 333  HIS A 334  THR A 352
SITE     3 AC6 30 ILE A 355  THR A 359  GLY A 360  GLY A 395
SITE     4 AC6 30 GLY A 398  ILE A 399  LEU A 401  SER A 402
SITE     5 AC6 30 ASP A 407  HIS A 411  VAL A 416  HIS A 419
SITE     6 AC6 30 PHE A 420  VAL A 423  MET A 424  ARG A 481
SITE     7 AC6 30 HOH A 715  HOH A 724   OH A 741  HOH A 742
SITE     8 AC6 30 HOH A 792  ILE B  68
SITE     1 AC7  3 LEU A  80  TRP A  81  DMU A1005
SITE     1 AC8  2 ARG A 476  THR B  41
SITE     1 AC9  5 HIS A 284  HIS A 333  HIS A 334   OH A 741
SITE     2 AC9  5 HOH A 742
SITE     1 BC1  6 HIS A 411  ASP A 412  GLU B 254  HOH B 503
SITE     2 BC1  6 HOH B 793  HOH B 797
SITE     1 BC2  6 GLU A  54  ALA A  57  GLY A  59  GLN A  61
SITE     2 BC2  6 HOH A 808  HOH A 815
SITE     1 BC3  4 HIS A  26  MET A 133  HOH A 826  HOH A 830
SITE     1 BC4 12 PRO A 449  TRP A 451  PHE A 510  GLY A 513
SITE     2 BC4 12 DMU B   2  HOH B  26  GLN B 142  TRP B 143
SITE     3 BC4 12 PRO B 164  HOH B 403  HOH B 713  HOH B 785
SITE     1 BC5  4 TRP A 451  ALA A 506  HOH A 778  DMU B   1
SITE     1 BC6 12 TRP A 371  PHE B  94  HIS B  96  ASN B  97
SITE     2 BC6 12 LEU B 100  TRP B 104  HOH B 434  GLU C  86
SITE     3 BC6 12 SER D 173  PRO D 174  GLU D 177  HOH D 361
SITE     1 BC7  3 PRO B 121  PHE B 124  GLU B 128
SITE     1 BC8  4 LEU B 112  VAL B 113  GLY B 116  ALA B 117
SITE     1 BC9  8 GLU B 152  ALA B 276  GLU B 280  HIS B 283
SITE     2 BC9  8 HOH B 709  ALA D 276  GLU D 280  HIS D 283
SITE     1 CC1  5 CYS B 252  GLU B 254  CYS B 256  HIS B 260
SITE     2 CC1  5 CU1 B 288
SITE     1 CC2  5 HIS B 217  CYS B 252  CYS B 256  MET B 263
SITE     2 CC2  5  CU B 287
SITE     1 CC3  4 GLU B 280  HIS B 283  HIS B 285  GLU D 152
SITE     1 CC4  5 HIS B  96  GLU B 101  HOH B 708  HOH B 761
SITE     2 CC4  5 HOH B 762
SITE     1 CC5  6 HEA C   2  HIS C 284  VAL C 287  HIS C 334
SITE     2 CC5  6  CU C 554  HOH C 743
SITE     1 CC6  8 MET C  53  MET C  56  GLN C  61  SER C  83
SITE     2 CC6  8 PHE C 502  PHE C 505  TRD C 553  HOH C 582
SITE     1 CC7  2 MET C 443  SER C 444
SITE     1 CC8  3 HIS C 102  HIS C 421  HEA C 552
SITE     1 CC9 29  FE C   1  HOH C   3  LEU C  34  GLY C  38
SITE     2 CC9 29 THR C  48  MET C  51  ARG C  52  TRP C  95
SITE     3 CC9 29 ILE C  99  HIS C 102  MET C 106  MET C 107
SITE     4 CC9 29 VAL C 111  GLY C 171  TRP C 172  TYR C 414
SITE     5 CC9 29 PHE C 420  HIS C 421  MET C 424  SER C 425
SITE     6 CC9 29 VAL C 429  MET C 460  PHE C 468  GLN C 471
SITE     7 CC9 29 ARG C 481  ARG C 482  SER C 504  HOH C 583
SITE     8 CC9 29 HOH C 613
SITE     1 DC1 28 HOH C  15  TRP C 172  TRP C 280  VAL C 287
SITE     2 DC1 28 TYR C 288  HIS C 333  HIS C 334  THR C 352
SITE     3 DC1 28 ILE C 355  THR C 359  GLY C 360  GLY C 395
SITE     4 DC1 28 GLY C 398  LEU C 401  SER C 402  ASP C 407
SITE     5 DC1 28 HIS C 411  VAL C 416  HIS C 419  PHE C 420
SITE     6 DC1 28 VAL C 423  MET C 424  ARG C 481  HOH C 586
SITE     7 DC1 28 HOH C 591  HOH C 604   OH C 741  HOH C 743
SITE     1 DC2  4 DMU C  10  LEU C  80  TRP C  81  PRO C  82
SITE     1 DC3  5 HIS C 284  HIS C 333  HIS C 334   OH C 741
SITE     2 DC3  5 HOH C 743
SITE     1 DC4  6 HIS C 411  ASP C 412  HOH C 568  GLU D 254
SITE     2 DC4  6 HOH D 314  HOH D 316
SITE     1 DC5  6 GLU C  54  ALA C  57  GLY C  59  GLN C  61
SITE     2 DC5  6 HOH C 569  HOH C 582
SITE     1 DC6  3 HIS C  26  ALA C 132  MET C 133
SITE     1 DC7  2 PRO D 121  GLU D 128
SITE     1 DC8  2 HIS D  96  ASN D  97
SITE     1 DC9  2 ARG C 476  THR D  41
SITE     1 EC1  5 CYS D 252  GLU D 254  CYS D 256  HIS D 260
SITE     2 EC1  5 CU1 D 287
SITE     1 EC2  5 HIS D 217  CYS D 252  CYS D 256  MET D 263
SITE     2 EC2  5  CU D 286
SITE     1 EC3  4 GLU B 152  GLU D 280  HIS D 283  HIS D 285
SITE     1 EC4  4 HIS D  96  GLU D 101  HOH D 379  HOH D 380
CRYST1  125.064  131.519  175.674  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      0.007996  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007603  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005692        0.00000
      
PROCHECK
Go to PROCHECK summary
 References