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PDBsum entry 1q0k

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Oxidoreductase PDB id
1q0k
Jmol
Contents
Protein chains
(+ 6 more) 117 a.a. *
Ligands
SO4 ×12
THJ ×12
Metals
_NI ×12
Waters ×504
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          16-JUL-03   1Q0K
TITLE     CRYSTAL STRUCTURE OF NI-CONTAINING SUPEROXIDE DISMUTASE WITH NI-
TITLE    2 LIGATION CORRESPONDING TO THE THIOSULFATE-REDUCED STATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [NI];
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND   4 SYNONYM: NICKEL-CONTAINING SUPEROXIDE DISMUTASE; NISOD; NI-CONTAINING
COMPND   5 SUPEROXIDE DISMUTASE;
COMPND   6 EC: 1.15.1.1;
COMPND   7 OTHER_DETAILS: THE ASYMMETRIC UNIT CONTAINS TWO HEXAMERS
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES SEOULENSIS;
SOURCE   3 ORGANISM_TAXID: 73044
KEYWDS    HOMOHEXAMER OF FOUR-HELIX BUNDLES, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.WUERGES,J.-W.LEE,Y.-I.YIM,H.-S.YIM,S.-O.KANG,K.DJINOVIC CARUGO
REVDAT   5   13-JUL-11 1Q0K    1       VERSN
REVDAT   4   07-APR-09 1Q0K    1       HETNAM
REVDAT   3   24-FEB-09 1Q0K    1       VERSN
REVDAT   2   15-JUN-04 1Q0K    1       JRNL
REVDAT   1   18-MAY-04 1Q0K    0
JRNL        AUTH   J.WUERGES,J.-W.LEE,Y.-I.YIM,H.-S.YIM,S.-O.KANG,
JRNL        AUTH 2 K.DJINOVIC CARUGO
JRNL        TITL   CRYSTAL STRUCTURE OF NICKEL-CONTAINING SUPEROXIDE DISMUTASE
JRNL        TITL 2 REVEALS ANOTHER TYPE OF ACTIVE SITE
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101  8569 2004
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   15173586
JRNL        DOI    10.1073/PNAS.0308514101
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 95957
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.204
REMARK   3   FREE R VALUE                     : 0.238
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4836
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 11172
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 132
REMARK   3   SOLVENT ATOMS            : 504
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 38.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.90
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.00
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.76
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.390 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.080 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.260 ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.250 ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1Q0K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-03.
REMARK 100 THE RCSB ID CODE IS RCSB019764.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.25
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ELETTRA
REMARK 200  BEAMLINE                       : 5.2R
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1271
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95957
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.200
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.05100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.40600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
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   (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, 2-PROPANOL, PH 5.25,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
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       55.81750
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.67800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.82550
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.67800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.81750
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.82550
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMOHEXAMER WHICH SHOWS A
REMARK 300 THREEFOLD SYMMETRY AXIS AND THREE TWOFOLD SYMMETRY AXES IN A PLANE
REMARK 300 PERPENDICULAR TO THE THREEFOLD AXIS
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -199.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
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 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  10      115.95   -166.61
REMARK 500    ASP B  10      112.52   -166.34
REMARK 500    ASP D  10      116.51   -168.89
REMARK 500    PRO D  72       -3.66    -57.18
REMARK 500    ASP E  10      117.87   -170.92
REMARK 500    ASP F  10      113.26   -167.14
REMARK 500    ASP G  10      114.73   -176.33
REMARK 500    ASP H  10      115.97   -163.52
REMARK 500    PRO H  11       -8.26    -57.53
REMARK 500    ASP I  10      110.11   -167.85
REMARK 500    ASP J  10      112.95   -171.95
REMARK 500    PRO J  11       -9.60    -57.33
REMARK 500    ASP K  10      116.48   -170.92
REMARK 500    ASP L  10      111.45   -163.34
REMARK 500    LYS L 116       23.93    -75.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH F9048        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH J9040        DISTANCE =  5.02 ANGSTROMS
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                              NI A 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A   1   N
REMARK 620 2 CYS A   2   N    80.2
REMARK 620 3 CYS A   2   SG  167.1  88.3
REMARK 620 4 CYS A   6   SG   97.4 171.6  94.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI B 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B   1   N
REMARK 620 2 CYS B   2   N    79.5
REMARK 620 3 CYS B   2   SG  170.1  90.8
REMARK 620 4 CYS B   6   SG   94.8 169.9  95.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI C 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C   1   N
REMARK 620 2 CYS C   6   SG   95.5
REMARK 620 3 CYS C   2   N    76.5 162.7
REMARK 620 4 CYS C   2   SG  168.8  94.8  92.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI D 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D   2   SG
REMARK 620 2 HIS D   1   N   167.6
REMARK 620 3 CYS D   2   N    89.4  79.0
REMARK 620 4 CYS D   6   SG   96.7  95.3 170.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI E 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E   2   SG
REMARK 620 2 CYS E   6   SG   96.8
REMARK 620 3 CYS E   2   N    88.0 169.2
REMARK 620 4 HIS E   1   N   166.4  96.8  78.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI F 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F   2   N
REMARK 620 2 CYS F   2   SG   87.5
REMARK 620 3 HIS F   1   N    81.2 168.6
REMARK 620 4 CYS F   6   SG  166.0  99.3  92.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI G 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G   2   SG
REMARK 620 2 CYS G   6   SG   93.9
REMARK 620 3 CYS G   2   N    89.1 174.9
REMARK 620 4 HIS G   1   N   166.4  98.8  78.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI H 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H   1   N
REMARK 620 2 CYS H   2   N    81.2
REMARK 620 3 CYS H   6   SG   93.6 165.7
REMARK 620 4 CYS H   2   SG  172.8  92.3  92.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI I 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I   2   SG
REMARK 620 2 CYS I   6   SG   96.2
REMARK 620 3 CYS I   2   N    87.5 163.8
REMARK 620 4 HIS I   1   N   164.3  98.5  76.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI J 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J   1   N
REMARK 620 2 CYS J   2   SG  168.4
REMARK 620 3 CYS J   6   SG   89.2 102.4
REMARK 620 4 CYS J   2   N    79.0  89.4 165.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI K 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K   1   N
REMARK 620 2 CYS K   2   N    80.7
REMARK 620 3 CYS K   2   SG  169.5  90.4
REMARK 620 4 CYS K   6   SG   95.7 170.0  94.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI L 118  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L   1   N
REMARK 620 2 CYS L   2   SG  170.3
REMARK 620 3 CYS L   6   SG   95.7  93.8
REMARK 620 4 CYS L   2   N    81.1  89.8 171.5
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 NI A 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI E 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI F 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI G 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI H 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI I 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI J 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI K 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI L 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 9005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 9006
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 9007
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 9008
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 9009
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 9010
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 9011
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 9012
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ C 7001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ B 7002
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ A 7003
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ D 7004
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ B 7005
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ D 7006
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ G 7007
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ H 7008
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ I 7009
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ L 7010
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ H 7011
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THJ L 7012
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q0D   RELATED DB: PDB
REMARK 900 CONTAINS THE RESTING ENZYME IN THE SAME CRYSTAL FORM
REMARK 900 RELATED ID: 1Q0F   RELATED DB: PDB
REMARK 900 CONTAINS THE PARTIALLY X-RAY REDUCED ENZYME IN THE SAME
REMARK 900 CRYSTAL FORM
REMARK 900 RELATED ID: 1Q0G   RELATED DB: PDB
REMARK 900 CONTAINS THE FULLY X-RAY REDUCED ENZYME IN THE SAME CRYSTAL
REMARK 900 FORM
REMARK 900 RELATED ID: 1Q0M   RELATED DB: PDB
REMARK 900 CONTAINS THE FULLY X-RAY REDUCED ENZYME IN ANOTHER CRYSTAL
REMARK 900 FORM
DBREF  1Q0K A    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K B    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K C    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K D    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K E    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K F    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K G    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K H    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K I    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K J    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K K    1   117  UNP    P80734   SODN_STRSO      15    131
DBREF  1Q0K L    1   117  UNP    P80734   SODN_STRSO      15    131
SEQRES   1 A  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 A  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 A  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 A  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 A  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 A  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 A  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 A  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 A  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 B  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 B  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 B  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 B  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 B  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 B  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 B  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 B  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 B  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 C  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 C  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 C  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 C  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 C  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 C  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 C  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 C  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 C  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 D  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 D  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 D  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 D  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 D  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 D  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 D  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 D  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 D  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 E  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 E  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 E  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 E  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 E  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 E  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 E  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 E  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 E  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 F  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 F  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 F  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 F  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 F  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 F  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 F  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 F  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 F  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 G  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 G  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 G  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 G  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 G  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 G  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 G  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 G  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 G  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 H  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 H  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 H  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 H  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 H  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 H  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 H  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 H  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 H  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 I  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 I  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 I  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 I  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 I  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 I  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 I  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 I  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 I  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 J  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 J  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 J  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 J  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 J  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 J  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 J  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 J  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 J  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 K  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 K  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 K  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 K  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 K  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 K  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 K  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 K  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 K  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
SEQRES   1 L  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN
SEQRES   2 L  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA ILE GLN GLU
SEQRES   3 L  117  LYS MET ALA ALA ASN ASP ASP LEU HIS PHE GLN ILE ARG
SEQRES   4 L  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS
SEQRES   5 L  117  HIS HIS LEU ASP VAL LEU TRP SER ASP TYR PHE LYS PRO
SEQRES   6 L  117  PRO HIS PHE GLU SER TYR PRO GLU LEU HIS THR LEU VAL
SEQRES   7 L  117  ASN GLU ALA VAL LYS ALA LEU SER ALA ALA LYS ALA SER
SEQRES   8 L  117  THR ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE
SEQRES   9 L  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA
HET     NI  A 118       1
HET     NI  B 118       1
HET     NI  C 118       1
HET     NI  D 118       1
HET     NI  E 118       1
HET     NI  F 118       1
HET     NI  G 118       1
HET     NI  H 118       1
HET     NI  I 118       1
HET     NI  J 118       1
HET     NI  K 118       1
HET     NI  L 118       1
HET    SO4  A9001       5
HET    SO4  B9002       5
HET    SO4  C9003       5
HET    SO4  D9004       5
HET    SO4  E9005       5
HET    SO4  F9006       5
HET    SO4  G9007       5
HET    SO4  H9008       5
HET    SO4  I9009       5
HET    SO4  J9010       5
HET    SO4  K9011       5
HET    SO4  L9012       5
HET    THJ  C7001       5
HET    THJ  B7002       5
HET    THJ  A7003       5
HET    THJ  D7004       5
HET    THJ  B7005       5
HET    THJ  D7006       5
HET    THJ  G7007       5
HET    THJ  H7008       5
HET    THJ  I7009       5
HET    THJ  L7010       5
HET    THJ  H7011       5
HET    THJ  L7012       5
HETNAM      NI NICKEL (II) ION
HETNAM     SO4 SULFATE ION
HETNAM     THJ THIOSULFATE
FORMUL  13   NI    12(NI 2+)
FORMUL  25  SO4    12(O4 S 2-)
FORMUL  37  THJ    12(O3 S2 2-)
FORMUL  49  HOH   *504(H2 O)
HELIX    1   1 PRO A   11  ASN A   31  1                                  21
HELIX    2   2 ASP A   33  ASP A   61  1                                  29
HELIX    3   3 LYS A   64  TYR A   71  1                                   8
HELIX    4   4 GLU A   73  ALA A   90  1                                  18
HELIX    5   5 ASP A   93  ALA A  117  1                                  25
HELIX    6   6 ASP B   10  ASN B   31  1                                  22
HELIX    7   7 ASP B   33  ASP B   61  1                                  29
HELIX    8   8 LYS B   64  TYR B   71  1                                   8
HELIX    9   9 GLU B   73  ALA B   90  1                                  18
HELIX   10  10 ASP B   93  ALA B  117  1                                  25
HELIX   11  11 PRO C   11  ALA C   30  1                                  20
HELIX   12  12 ASP C   33  TYR C   62  1                                  30
HELIX   13  13 LYS C   64  TYR C   71  1                                   8
HELIX   14  14 GLU C   73  ALA C   90  1                                  18
HELIX   15  15 ASP C   93  ALA C  117  1                                  25
HELIX   16  16 PRO D   11  ASN D   31  1                                  21
HELIX   17  17 ASP D   33  ASP D   61  1                                  29
HELIX   18  18 LYS D   64  TYR D   71  1                                   8
HELIX   19  19 GLU D   73  ALA D   90  1                                  18
HELIX   20  20 ASP D   93  ALA D  117  1                                  25
HELIX   21  21 PRO E   11  ASN E   31  1                                  21
HELIX   22  22 ASP E   33  TYR E   62  1                                  30
HELIX   23  23 LYS E   64  TYR E   71  1                                   8
HELIX   24  24 GLU E   73  ALA E   90  1                                  18
HELIX   25  25 ASP E   93  LYS E  116  1                                  24
HELIX   26  26 PRO F   11  ASN F   31  1                                  21
HELIX   27  27 ASP F   33  ASP F   61  1                                  29
HELIX   28  28 LYS F   64  TYR F   71  1                                   8
HELIX   29  29 GLU F   73  ALA F   90  1                                  18
HELIX   30  30 ASP F   93  ALA F  117  1                                  25
HELIX   31  31 PRO G   11  ALA G   30  1                                  20
HELIX   32  32 ASP G   33  TYR G   62  1                                  30
HELIX   33  33 LYS G   64  TYR G   71  1                                   8
HELIX   34  34 GLU G   73  ALA G   90  1                                  18
HELIX   35  35 ASP G   93  LYS G  116  1                                  24
HELIX   36  36 PRO H   11  ASN H   31  1                                  21
HELIX   37  37 ASP H   33  ASP H   61  1                                  29
HELIX   38  38 LYS H   64  TYR H   71  1                                   8
HELIX   39  39 GLU H   73  ALA H   90  1                                  18
HELIX   40  40 ASP H   93  ALA H  117  1                                  25
HELIX   41  41 PRO I   11  ALA I   29  1                                  19
HELIX   42  42 ASP I   33  ASP I   61  1                                  29
HELIX   43  43 LYS I   64  TYR I   71  1                                   8
HELIX   44  44 GLU I   73  ALA I   90  1                                  18
HELIX   45  45 ASP I   93  ALA I  117  1                                  25
HELIX   46  46 PRO J   11  ASN J   31  1                                  21
HELIX   47  47 ASP J   33  ASP J   61  1                                  29
HELIX   48  48 LYS J   64  TYR J   71  1                                   8
HELIX   49  49 GLU J   73  ALA J   90  1                                  18
HELIX   50  50 ASP J   93  ALA J  117  1                                  25
HELIX   51  51 PRO K   11  ASN K   31  1                                  21
HELIX   52  52 ASP K   33  ASP K   61  1                                  29
HELIX   53  53 LYS K   64  TYR K   71  1                                   8
HELIX   54  54 GLU K   73  ALA K   90  1                                  18
HELIX   55  55 ASP K   93  ALA K  117  1                                  25
HELIX   56  56 PRO L   11  ASN L   31  1                                  21
HELIX   57  57 ASP L   33  TYR L   62  1                                  30
HELIX   58  58 LYS L   64  TYR L   71  1                                   8
HELIX   59  59 GLU L   73  ALA L   90  1                                  18
HELIX   60  60 ASP L   93  LYS L  116  1                                  24
LINK        NI    NI A 118                 N   HIS A   1     1555   1555  2.17
LINK        NI    NI A 118                 N   CYS A   2     1555   1555  1.97
LINK        NI    NI A 118                 SG  CYS A   2     1555   1555  2.31
LINK        NI    NI A 118                 SG  CYS A   6     1555   1555  2.26
LINK        NI    NI B 118                 N   HIS B   1     1555   1555  2.21
LINK        NI    NI B 118                 N   CYS B   2     1555   1555  1.96
LINK        NI    NI B 118                 SG  CYS B   2     1555   1555  2.33
LINK        NI    NI B 118                 SG  CYS B   6     1555   1555  2.30
LINK        NI    NI C 118                 N   HIS C   1     1555   1555  2.27
LINK        NI    NI C 118                 SG  CYS C   6     1555   1555  2.30
LINK        NI    NI C 118                 N   CYS C   2     1555   1555  1.98
LINK        NI    NI C 118                 SG  CYS C   2     1555   1555  2.23
LINK        NI    NI D 118                 SG  CYS D   2     1555   1555  2.21
LINK        NI    NI D 118                 N   HIS D   1     1555   1555  2.09
LINK        NI    NI D 118                 N   CYS D   2     1555   1555  2.05
LINK        NI    NI D 118                 SG  CYS D   6     1555   1555  2.31
LINK        NI    NI E 118                 SG  CYS E   2     1555   1555  2.37
LINK        NI    NI E 118                 SG  CYS E   6     1555   1555  2.33
LINK        NI    NI E 118                 N   CYS E   2     1555   1555  2.03
LINK        NI    NI E 118                 N   HIS E   1     1555   1555  2.11
LINK        NI    NI F 118                 N   CYS F   2     1555   1555  2.00
LINK        NI    NI F 118                 SG  CYS F   2     1555   1555  2.36
LINK        NI    NI F 118                 N   HIS F   1     1555   1555  2.10
LINK        NI    NI F 118                 SG  CYS F   6     1555   1555  2.18
LINK        NI    NI G 118                 SG  CYS G   2     1555   1555  2.34
LINK        NI    NI G 118                 SG  CYS G   6     1555   1555  2.33
LINK        NI    NI G 118                 N   CYS G   2     1555   1555  2.01
LINK        NI    NI G 118                 N   HIS G   1     1555   1555  2.23
LINK        NI    NI H 118                 N   HIS H   1     1555   1555  2.13
LINK        NI    NI H 118                 N   CYS H   2     1555   1555  1.90
LINK        NI    NI H 118                 SG  CYS H   6     1555   1555  2.32
LINK        NI    NI H 118                 SG  CYS H   2     1555   1555  2.23
LINK        NI    NI I 118                 SG  CYS I   2     1555   1555  2.37
LINK        NI    NI I 118                 SG  CYS I   6     1555   1555  2.28
LINK        NI    NI I 118                 N   CYS I   2     1555   1555  2.06
LINK        NI    NI I 118                 N   HIS I   1     1555   1555  2.24
LINK        NI    NI J 118                 N   HIS J   1     1555   1555  2.24
LINK        NI    NI J 118                 SG  CYS J   2     1555   1555  2.28
LINK        NI    NI J 118                 SG  CYS J   6     1555   1555  2.28
LINK        NI    NI J 118                 N   CYS J   2     1555   1555  2.01
LINK        NI    NI K 118                 N   HIS K   1     1555   1555  2.06
LINK        NI    NI K 118                 N   CYS K   2     1555   1555  1.96
LINK        NI    NI K 118                 SG  CYS K   2     1555   1555  2.30
LINK        NI    NI K 118                 SG  CYS K   6     1555   1555  2.34
LINK        NI    NI L 118                 N   HIS L   1     1555   1555  2.15
LINK        NI    NI L 118                 SG  CYS L   2     1555   1555  2.32
LINK        NI    NI L 118                 SG  CYS L   6     1555   1555  2.29
LINK        NI    NI L 118                 N   CYS L   2     1555   1555  1.95
CISPEP   1 LEU A    4    PRO A    5          0         0.03
CISPEP   2 LEU B    4    PRO B    5          0        -0.02
CISPEP   3 LEU C    4    PRO C    5          0         0.01
CISPEP   4 LEU D    4    PRO D    5          0        -0.16
CISPEP   5 LEU E    4    PRO E    5          0        -0.02
CISPEP   6 LEU F    4    PRO F    5          0        -0.20
CISPEP   7 LEU G    4    PRO G    5          0         0.04
CISPEP   8 LEU H    4    PRO H    5          0         0.16
CISPEP   9 LEU I    4    PRO I    5          0         0.14
CISPEP  10 LEU J    4    PRO J    5          0        -0.08
CISPEP  11 LEU K    4    PRO K    5          0         0.01
CISPEP  12 LEU L    4    PRO L    5          0         0.02
SITE     1 AC1  4 HIS A   1  CYS A   2  ASP A   3  CYS A   6
SITE     1 AC2  4 HIS B   1  CYS B   2  ASP B   3  CYS B   6
SITE     1 AC3  4 HIS C   1  CYS C   2  ASP C   3  CYS C   6
SITE     1 AC4  4 HIS D   1  CYS D   2  ASP D   3  CYS D   6
SITE     1 AC5  4 HIS E   1  CYS E   2  ASP E   3  CYS E   6
SITE     1 AC6  4 HIS F   1  CYS F   2  ASP F   3  CYS F   6
SITE     1 AC7  3 HIS G   1  CYS G   2  CYS G   6
SITE     1 AC8  4 HIS H   1  CYS H   2  ASP H   3  CYS H   6
SITE     1 AC9  4 HIS I   1  CYS I   2  ASP I   3  CYS I   6
SITE     1 BC1  4 HIS J   1  CYS J   2  ASP J   3  CYS J   6
SITE     1 BC2  4 HIS K   1  CYS K   2  ASP K   3  CYS K   6
SITE     1 BC3  4 HIS L   1  CYS L   2  ASP L   3  CYS L   6
SITE     1 BC4  4 PRO A   5  GLY A   7  TYR A   9  LYS A  64
SITE     1 BC5  4 PRO B   5  GLY B   7  TYR B   9  LYS B  64
SITE     1 BC6  4 PRO C   5  GLY C   7  TYR C   9  LYS C  64
SITE     1 BC7  4 PRO D   5  GLY D   7  TYR D   9  LYS D  64
SITE     1 BC8  4 PRO E   5  GLY E   7  TYR E   9  LYS E  64
SITE     1 BC9  5 PRO F   5  GLY F   7  TYR F   9  LYS F  64
SITE     2 BC9  5 HOH F9053
SITE     1 CC1  3 PRO G   5  GLY G   7  TYR G   9
SITE     1 CC2  6 PRO H   5  GLY H   7  TYR H   9  ASP H  61
SITE     2 CC2  6 LYS H  64  HOH H9040
SITE     1 CC3  4 PRO I   5  GLY I   7  TYR I   9  LYS I  64
SITE     1 CC4  5 PRO J   5  GLY J   7  TYR J   9  LYS J  64
SITE     2 CC4  5 HOH J9031
SITE     1 CC5  4 PRO K   5  GLY K   7  TYR K   9  LYS K  64
SITE     1 CC6  4 PRO L   5  GLY L   7  TYR L   9  LYS L  64
SITE     1 CC7  5 HIS A   1  HIS A  53  HOH A9035  ARG C  47
SITE     2 CC7  5 LEU C  50
SITE     1 CC8  5 HIS B  53  HIS B  54  HOH B9015  ARG E  47
SITE     2 CC8  5 LEU E  50
SITE     1 CC9  5 GLU A  17  ARG A  47  LEU A  50  HOH A9019
SITE     2 CC9  5 HIS C  53
SITE     1 DC1  3 HIS D  53  HOH D9019  ARG F  47
SITE     1 DC2  7 GLU B  17  ARG B  47  LEU B  50  HOH B9023
SITE     2 DC2  7 HIS E  53  HIS E  54  HOH E9032
SITE     1 DC3  4 ARG D  47  LEU D  50  HIS F  53  HOH F9014
SITE     1 DC4  6 HIS G  53  HOH G9021  HOH G9049  GLU I  17
SITE     2 DC4  6 ARG I  47  LEU I  50
SITE     1 DC5  4 HIS H  53  HOH H9018  ARG K  47  LEU K  50
SITE     1 DC6  4 ARG G  47  LEU G  50  HIS I  53  HIS I  54
SITE     1 DC7  6 HIS J  53  HIS J  54  HOH J9052  ARG L  47
SITE     2 DC7  6 LEU L  50  HOH L9029
SITE     1 DC8  5 ARG H  47  LEU H  50  HIS K   1  HIS K  53
SITE     2 DC8  5 HOH K9024
SITE     1 DC9  5 ARG J  47  LEU J  50  HIS L  53  HIS L  54
SITE     2 DC9  5 HOH L9037
CRYST1  111.635  113.651  129.356  90.00  90.00  90.00 P 21 21 21   48
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      0.008958  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008799  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007731        0.00000
      
PROCHECK
Go to PROCHECK summary
 References