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PDBsum entry 3a38

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Electron transport PDB id
3a38
Jmol
Contents
Protein chain
83 a.a.
Ligands
SF4
SO4 ×3
GOL
Waters ×227
HEADER    ELECTRON TRANSPORT                      10-JUN-09   3A38
TITLE     CRYSTAL STRUCTURE OF HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM
TITLE    2 THERMOCHROMATIUM TEPIDUM AT 0.7 ANGSTROM RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HIGH-POTENTIAL IRON-SULFUR PROTEIN;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: HIPIP
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOCHROMATIUM TEPIDUM;
SOURCE   3 ORGANISM_COMMON: CHROMATIUM TEPIDUM;
SOURCE   4 ORGANISM_TAXID: 1050
KEYWDS    IRON-SULFUR CLUSTER, ELECTRON TRANSPORT, IRON, IRON-SULFUR, METAL-
KEYWDS   2 BINDING, TRANSPORT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.TAKEDA,K.KUSUMOTO,Y.HIRANO,K.MIKI
REVDAT   2   05-MAR-14 3A38    1       JRNL   VERSN
REVDAT   1   26-JAN-10 3A38    0
JRNL        AUTH   K.TAKEDA,K.KUSUMOTO,Y.HIRANO,K.MIKI
JRNL        TITL   DETAILED ASSESSMENT OF X-RAY INDUCED STRUCTURAL PERTURBATION
JRNL        TITL 2 IN A CRYSTALLINE STATE PROTEIN.
JRNL        REF    J.STRUCT.BIOL.                V. 169   135 2010
JRNL        REFN                   ISSN 1047-8477
JRNL        PMID   19782139
JRNL        DOI    10.1016/J.JSB.2009.09.012
REMARK   2
REMARK   2 RESOLUTION.    0.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM FROM 0.8 TO 0.7
REMARK   3                                       ANGSTROM RESOLUTION
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.067
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.066
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.075
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 8561
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 96693
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.065
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.064
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.074
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 8266
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 166097
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 616
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 29
REMARK   3   SOLVENT ATOMS      : 162
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 744.38
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 544.02
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 38
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 8703
REMARK   3   NUMBER OF RESTRAINTS                     : 413
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.028
REMARK   3   ANGLE DISTANCES                      (A) : 2.800
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.000
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.000
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.000
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.000
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.000
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3A38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB028755.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 93
REMARK 200  PH                             : 4.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL41XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.71
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96778
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.700
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     (%) : 94.7
REMARK 200  DATA REDUNDANCY                : 6.200
REMARK 200  R MERGE                    (I) : 0.05500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 57.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.73
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.15600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 8.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1IUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 32.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9M AMMONIUM SULFATE, 10MM
REMARK 280  DITHIOTHREITOL, 100MM SODIUM CITRATE, PH 4.0, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
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       23.25450
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       11.70750
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.47950
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       11.70750
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.25450
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.47950
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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   C    ASP A    10     H    ASP A    11              1.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A  11   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    LYS A  59         11.98
REMARK 500    SER A  77        -14.67
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    GLN A  62        23.9      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             SF4 A  84  FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  43   SG
REMARK 620 2 SF4 A  84   S1  116.0
REMARK 620 3 SF4 A  84   S2  112.0 104.8
REMARK 620 4 SF4 A  84   S3  113.4 105.2 104.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             SF4 A  84  FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  46   SG
REMARK 620 2 SF4 A  84   S1  115.5
REMARK 620 3 SF4 A  84   S2  111.1 104.7
REMARK 620 4 SF4 A  84   S4  114.7 104.5 105.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             SF4 A  84  FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  61   SG
REMARK 620 2 SF4 A  84   S2  117.8
REMARK 620 3 SF4 A  84   S3  119.3 103.5
REMARK 620 4 SF4 A  84   S4  105.0 104.5 105.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             SF4 A  84  FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  75   SG
REMARK 620 2 SF4 A  84   S1  126.5
REMARK 620 3 SF4 A  84   S3  109.6 104.5
REMARK 620 4 SF4 A  84   S4  104.9 103.4 106.4
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 SF4 A 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A39   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN AT 0.72 ANGSTROM
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1IUA   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN AT 0.8 ANGSTROM
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1EYT   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN AT 1.5 ANGSTROME
REMARK 900 RESOLUTION
DBREF  3A38 A    1    83  UNP    P80176   HIP_THETI        1     83
SEQRES   1 A   83  ALA ALA PRO ALA ASN ALA VAL THR ALA ASP ASP PRO THR
SEQRES   2 A   83  ALA ILE ALA LEU LYS TYR ASN GLN ASP ALA THR LYS SER
SEQRES   3 A   83  GLU ARG VAL ALA ALA ALA ARG PRO GLY LEU PRO PRO GLU
SEQRES   4 A   83  GLU GLN HIS CYS ALA ASN CYS GLN PHE MET GLN ALA ASN
SEQRES   5 A   83  VAL GLY GLU GLY ASP TRP LYS GLY CYS GLN LEU PHE PRO
SEQRES   6 A   83  GLY LYS LEU ILE ASN VAL ASN GLY TRP CYS ALA SER TRP
SEQRES   7 A   83  THR LEU LYS ALA GLY
HET    SF4  A  84       8
HET    SO4  A 101       5
HET    SO4  A 102       5
HET    SO4  A 103       5
HET    GOL  A 201       6
HETNAM     SF4 IRON/SULFUR CLUSTER
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  SF4    FE4 S4
FORMUL   3  SO4    3(O4 S 2-)
FORMUL   6  GOL    C3 H8 O3
FORMUL   7  HOH   *162(H2 O)
HELIX    1   1 ASP A   11  LYS A   18  1                                   8
HELIX    2   2 ASP A   22  SER A   26  5                                   5
HELIX    3   3 GLU A   27  ALA A   32  1                                   6
HELIX    4   4 PRO A   37  GLN A   41  5                                   5
HELIX    5   5 HIS A   42  CYS A   46  5                                   5
SHEET    1   A 3 MET A  49  GLU A  55  0
SHEET    2   A 3 TRP A  58  CYS A  61 -1  O  GLY A  60   N  GLN A  50
SHEET    3   A 3 ILE A  69  ASN A  70 -1  O  ILE A  69   N  LYS A  59
LINK         SG  CYS A  43                FE4  SF4 A  84     1555   1555  2.25
LINK         SG  CYS A  46                FE3  SF4 A  84     1555   1555  2.27
LINK         SG  CYS A  61                FE1  SF4 A  84     1555   1555  2.26
LINK         SG  CYS A  75                FE2  SF4 A  84     1555   1555  2.27
SITE     1 AC1  6 TYR A  19  CYS A  43  CYS A  46  CYS A  61
SITE     2 AC1  6 LEU A  63  CYS A  75
SITE     1 AC2  8 LYS A  18  GLU A  55  GLY A  56  LYS A  59
SITE     2 AC2  8 HOH A 411  HOH A 425  HOH A 428  HOH A 458
SITE     1 AC3 12 ALA A   6  VAL A   7  THR A   8  ASP A  11
SITE     2 AC3 12 LYS A  25  LYS A  67  HOH A 312  HOH A 323
SITE     3 AC3 12 HOH A 393  HOH A 424  HOH A 426  HOH A 438
SITE     1 AC4  7 HIS A  42  GLN A  50  GLN A  62  GOL A 201
SITE     2 AC4  7 HOH A 333  HOH A 398  HOH A 434
SITE     1 AC5  9 LYS A  18  GLU A  27  GLU A  40  ASN A  45
SITE     2 AC5  9 GLN A  62  SO4 A 103  HOH A 337  HOH A 372
SITE     3 AC5  9 HOH A 457
CRYST1   46.509   58.959   23.415  90.00  90.00  90.00 P 21 21 21    4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.021501  0.000000  0.000000        0.00000
SCALE2      0.000000  0.016961  0.000000        0.00000
SCALE3      0.000000  0.000000  0.042708        0.00000
      
PROCHECK
Go to PROCHECK summary
 References