spacer
spacer

PDBsum entry 2c9u

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2c9u
Jmol
Contents
Protein chain
153 a.a.
Ligands
SO4 ×3
ACT ×2
Metals
_ZN ×4
_CU ×2
Waters ×389
HEADER    OXIDOREDUCTASE                          14-DEC-05   2C9U
TITLE     1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU-ZN
TITLE    2 HUMAN SUPEROXIDE DISMUTASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND   3 CHAIN: A, F;
COMPND   4 EC: 1.15.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 TISSUE: BLOOD;
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS    ACETYLATION, AMYOTROPHIC LATERAL SCLEROSIS, ZINC,
KEYWDS   2 ANTIOXIDANT, COPPER, DISEASE MUTATION, HUMAN CU, METAL-
KEYWDS   3 BINDING, OXIDOREDUCTASE, ZN SUPEROXIDE DISMUTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.W.STRANGE,S.V.ANTONYUK,M.A.HOUGH,P.A.DOUCETTE,
AUTHOR   2 J.S.VALENTINE S,S.HASNAIN
REVDAT   3   24-FEB-09 2C9U    1       VERSN
REVDAT   2   15-FEB-06 2C9U    1       AUTHOR JRNL
REVDAT   1   16-DEC-05 2C9U    0
JRNL        AUTH   R.W.STRANGE,S.V.ANTONYUK,M.A.HOUGH,P.A.DOUCETTE,
JRNL        AUTH 2 J.S.VALENTINE,S.S.HASNAIN
JRNL        TITL   VARIABLE METALLATION OF HUMAN SUPEROXIDE
JRNL        TITL 2 DISMUTASE: ATOMIC RESOLUTION CRYSTAL STRUCTURES OF
JRNL        TITL 3 CU-ZN, ZN-ZN AND AS-ISOLATED WILD-TYPE ENZYMES.
JRNL        REF    J.MOL.BIOL.                   V. 356  1152 2006
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16406071
JRNL        DOI    10.1016/J.JMB.2005.11.081
REMARK   2
REMARK   2 RESOLUTION.    1.24 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 1.24
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.19
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8
REMARK   3   NUMBER OF REFLECTIONS             : 66500
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 + TEST SET) : 0.141
REMARK   3   R VALUE            (WORKING SET) : 0.139
REMARK   3   FREE R VALUE                     : 0.176
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3501
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.24
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.27
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3900
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980
REMARK   3   BIN FREE R VALUE SET COUNT          : 203
REMARK   3   BIN FREE R VALUE                    : 0.3370
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2273
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 29
REMARK   3   SOLVENT ATOMS            : 389
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.39
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.43000
REMARK   3    B22 (A**2) : -0.36000
REMARK   3    B33 (A**2) : 0.06000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.24000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.045
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.045
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.025
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.271
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2328 ; 0.020 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  2055 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3138 ; 1.841 ; 1.951
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4845 ; 2.495 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   306 ; 6.798 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   101 ;39.028 ;25.644
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   397 ;11.843 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;13.630 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   346 ; 0.119 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2641 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   414 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   474 ; 0.253 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2074 ; 0.203 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1121 ; 0.169 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1335 ; 0.095 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   301 ; 0.302 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    24 ; 0.193 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    50 ; 0.182 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    47 ; 0.297 ; 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):  1916 ; 2.417 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2408 ; 3.041 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   898 ; 3.718 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   730 ; 4.618 ; 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   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2C9U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-05.
REMARK 100 THE PDBE ID CODE IS EBI-26849.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-03
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 8.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX10.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.074
REMARK 200  MONOCHROMATOR                  : SILICON
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70045
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.240
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.200
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: PDB ENTRY 1HL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0 M AMMONIUM SULPHATE, 100 MM
REMARK 280  SODIUM CHLORITE, 50MM SODIUM ACETATE BUFFER
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.77650
REMARK 290   SMTRY3   2  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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400
REMARK 400 COMPOUND
REMARK 400  ELIMINATES RADICALS WHICH ARE PRODUCED BY CELLS
REMARK 400  AND WHICH ARE TOXIC TO BIOLOGICAL SYSTEMS.
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     ASP A  11    OD1  OD2
REMARK 470     SER A  25    OG
REMARK 470     GLN F 153    O
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    GLY F    10  -  O    HOH F  2011              1.85
REMARK 500   O    GLY F    10  -  O    HOH F  2012              1.96
REMARK 500   C    ASP F    11  -  O    HOH F  2011              2.18
REMARK 500   N    GLY F    12  -  O    HOH F  2011              1.95
REMARK 500   O    GLU F    77  -  O    HOH F  2109              1.80
REMARK 500   O    HOH A  2005  -  O    HOH A  2013              1.91
REMARK 500   O    HOH A  2066  -  O    HOH F  2184              2.19
REMARK 500   O    HOH A  2084  -  O    HOH F  2184              2.12
REMARK 500   O    HOH A  2100  -  O    HOH A  2114              2.17
REMARK 500   O    HOH A  2130  -  O    HOH A  2134              2.19
REMARK 500   O    HOH F  2010  -  O    HOH A  2064              2.02
REMARK 500   O    HOH F  2089  -  O    HOH F  2177              2.17
REMARK 500   O    HOH F  2120  -  O    HOH F  2129              2.10
REMARK 500   O    HOH F  2122  -  O    HOH F  2129              2.16
REMARK 500   O    HOH F  2173  -  O    HOH F  2187              2.19
REMARK 500   O    HOH F  2186  -  O    HOH F  2188              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500
REMARK 500   O    HOH A  2058     O    HOH F  2124     1645      2.08
REMARK 500   O    HOH F  2067     O    HOH A  2110     1756      1.96
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    SER A  59   CA    SER A  59   CB      0.099
REMARK 500    GLU F  49   CG    GLU F  49   CD     -0.106
REMARK 500    SER F  59   CA    SER F  59   CB      0.105
REMARK 500    GLU F  78   CD    GLU F  78   OE1     0.075
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    ARG A 115   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
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 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                              CU A1157  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  48   NE2
REMARK 620 2 HIS A 120   NE2 112.5
REMARK 620 3 HIS A  46   ND1 136.1  98.3
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU F1156  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F  48   NE2
REMARK 620 2 HIS F  46   ND1 133.6
REMARK 620 3 HIS F 120   NE2 123.9 101.6
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1158  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  71   ND1
REMARK 620 2 HIS A  63   ND1 104.5
REMARK 620 3 HIS A  80   ND1 119.8 109.3
REMARK 620 4 ASP A  83   OD1  99.5 106.3 116.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1159  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  48   NE2
REMARK 620 2 HIS A 120   NE2 124.0
REMARK 620 3 SO4 A1154   O1  112.2 104.5
REMARK 620 4 HOH A2193   O   102.8 109.8   9.5
REMARK 620 5 HIS A  46   ND1 113.2  94.8 105.8 112.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN F1155  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F  48   NE2
REMARK 620 2 HIS F  46   ND1 111.2
REMARK 620 3 HIS F 120   NE2 123.3  95.5
REMARK 620 4 SO4 F1154   O1  112.6 111.0 101.7
REMARK 620 5 HOH F2190   O   111.1 109.0 105.2   3.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN F1157  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F  63   ND1
REMARK 620 2 HIS F  71   ND1 105.2
REMARK 620 3 ASP F  83   OD1 105.5  99.1
REMARK 620 4 HIS F  80   ND1 108.3 121.9 115.3
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 SO4 A1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU A1157
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F1156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1157
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F1159
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB
REMARK 900  FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED MONOMERIC
REMARK 900  SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB
REMARK 900  THE SOLUTION STRUCTURE OF A MONOMERIC,
REMARK 900  REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE
REMARK 900  DISMUTASE BEARING THE SAMECHARGE AS THE
REMARK 900  NATIVE PROTEIN
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH LYS 136
REMARK 900  REPLACED BY GLU, CYS 6 REPLACED BY ALA
REMARK 900  AND CYS 111 REPLACED BY SER (K136E, C6A,
REMARK 900  C111S)
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF APO TYPE HUMAN CU, ZN
REMARK 900  SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN
REMARK 900  SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-
REMARK 900  FREE SUPEROXIDEDISMUTASE
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED DIMERIC
REMARK 900  COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF
REMARK 900  DIMERIZATION
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB
REMARK 900  MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q
REMARK 900  AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB
REMARK 900  THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE
REMARK 900  DISMUTASE, C6A,C111S
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE HSOD A4V MUTANT
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB
REMARK 900  ZN HIS46ARG MUTANT OF HUMAN CU, ZN
REMARK 900  SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS
REMARK 900  MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (
REMARK 900  CUZNSOD) TO 2.5A RESOLUTION
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT
REMARK 900  S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (
REMARK 900  CUZNSOD) TO 1.3A RESOLUTION
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN
REMARK 900  COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT
REMARK 900   D125H TO 1.4A
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CU, ZN
REMARK 900  SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC
REMARK 900  LATERAL SCLEROSIS (FALS) MUTANT H43R
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN CU,ZN SUPEROXIDE
REMARK 900  DISMUTASE
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE
REMARK 900  DISMUTASE: ROLEOF METAL IONS IN PROTEIN
REMARK 900  FOLDING
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH CYS 6
REMARK 900  REPLACED BY ALA AND CYS 111 REPLACED BY
REMARK 900  SER (C6A, C111S)
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB
REMARK 900  SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB
REMARK 900  I113T MUTANT OF HUMAN SOD1
REMARK 900 RELATED ID: 1UXM   RELATED DB: PDB
REMARK 900  A4V MUTANT OF HUMAN SOD1
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF DISULFIDE REDUCED AND
REMARK 900  COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB
REMARK 900  CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS
REMARK 900  6 REPLACED BY ALA AND CYS 111 REPLACED
REMARK 900  BY SER (C6A,C111S) WITH AN 18-RESIDUE
REMARK 900  HEPARIN-BINDING PEPTIDE FUSED TO THE C-
REMARK 900  TERMINUS (THEORETICAL MODEL)
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-
REMARK 900  ZN HUMAN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB
REMARK 900  ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN
REMARK 900  SUPEROXIDE DISMUTASE
DBREF  2C9U A    1   153  UNP    P00441   SODC_HUMAN       1    153
DBREF  2C9U F    1   153  UNP    P00441   SODC_HUMAN       1    153
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES   1 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET    SO4  A1154       5
HET    SO4  A1155       5
HET     CU  A1157       1
HET     ZN  A1158       1
HET     ZN  A1159       1
HET    SO4  F1154       5
HET     ZN  F1155       1
HET     CU  F1156       1
HET     ZN  F1157       1
HET    ACT  F1158       4
HET    ACT  F1159       4
HETNAM     SO4 SULFATE ION
HETNAM      CU COPPER (II) ION
HETNAM      ZN ZINC ION
HETNAM     ACT ACETATE ION
FORMUL   3  SO4    3(O4 S 2-)
FORMUL   5   CU    2(CU 2+)
FORMUL   6   ZN    4(ZN 2+)
FORMUL  12  ACT    2(C2 H3 O2 1-)
FORMUL  14  HOH   *389(H2 O1)
HELIX    1   1 ALA A   55  GLY A   61  5                                   7
HELIX    2   2 SER A  107  HIS A  110  5                                   4
HELIX    3   3 ASN A  131  LYS A  136  5                                   6
HELIX    4   4 ALA F   55  GLY F   61  5                                   7
HELIX    5   5 ASN F  131  LYS F  136  5                                   6
SHEET    1  AA 5 ALA A  95  ASP A 101  0
SHEET    2  AA 5 VAL A  29  LYS A  36 -1  O  VAL A  29   N  ASP A 101
SHEET    3  AA 5 GLN A  15  GLU A  21 -1  O  GLN A  15   N  LYS A  36
SHEET    4  AA 5 LYS A   3  LYS A   9 -1  O  ALA A   4   N  PHE A  20
SHEET    5  AA 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5
SHEET    1  AB 4 ASP A  83  ALA A  89  0
SHEET    2  AB 4 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89
SHEET    3  AB 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48
SHEET    4  AB 4 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119
SHEET    1  FA 5 ALA F  95  ASP F 101  0
SHEET    2  FA 5 VAL F  29  LYS F  36 -1  O  VAL F  29   N  ASP F 101
SHEET    3  FA 5 VAL F  14  GLN F  22 -1  O  GLN F  15   N  LYS F  36
SHEET    4  FA 5 THR F   2  GLY F  10 -1  O  THR F   2   N  GLN F  22
SHEET    5  FA 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5
SHEET    1  FB 4 ASP F  83  ALA F  89  0
SHEET    2  FB 4 GLY F  41  HIS F  48 -1  O  GLY F  41   N  ALA F  89
SHEET    3  FB 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48
SHEET    4  FB 4 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119
SSBOND   1 CYS F   57    CYS F  146                          1555   1555  2.58
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.00
LINK         O1  SO4 A1154                ZN    ZN A1159     1555   1555  1.98
LINK        CU    CU A1157                 NE2 HIS A  48     1555   1555  2.04
LINK        CU    CU A1157                 NE2 HIS A 120     1555   1555  2.23
LINK        CU    CU A1157                 ND1 HIS A  46     1555   1555  1.82
LINK        ZN    ZN A1158                 ND1 HIS A  71     1555   1555  2.08
LINK        ZN    ZN A1158                 ND1 HIS A  63     1555   1555  2.03
LINK        ZN    ZN A1158                 ND1 HIS A  80     1555   1555  2.02
LINK        ZN    ZN A1158                 OD1 ASP A  83     1555   1555  1.97
LINK        ZN    ZN A1159                 NE2 HIS A  48     1555   1555  2.07
LINK        ZN    ZN A1159                 NE2 HIS A 120     1555   1555  1.95
LINK        ZN    ZN A1159                 O   HOH A2193     1555   1555  2.31
LINK        ZN    ZN A1159                 ND1 HIS A  46     1555   1555  2.22
LINK         OD1 ASP F  11                 OXT ACT F1159     1555   1555  1.65
LINK         CG  ASP F  11                 OXT ACT F1159     1555   1555  1.93
LINK        ZN    ZN F1155                 NE2 HIS F  48     1555   1555  2.16
LINK        ZN    ZN F1155                 ND1 HIS F  46     1555   1555  2.28
LINK        ZN    ZN F1155                 NE2 HIS F 120     1555   1555  1.85
LINK        ZN    ZN F1155                 O1  SO4 F1154     1555   1555  2.06
LINK        ZN    ZN F1155                 O   HOH F2190     1555   1555  2.08
LINK        CU    CU F1156                 NE2 HIS F 120     1555   1555  2.00
LINK        CU    CU F1156                 ND1 HIS F  46     1555   1555  1.98
LINK        CU    CU F1156                 NE2 HIS F  48     1555   1555  2.01
LINK        ZN    ZN F1157                 ND1 HIS F  80     1555   1555  1.99
LINK        ZN    ZN F1157                 OD1 ASP F  83     1555   1555  1.96
LINK        ZN    ZN F1157                 ND1 HIS F  71     1555   1555  2.07
LINK        ZN    ZN F1157                 ND1 HIS F  63     1555   1555  2.06
CISPEP   1 GLY F   12    PRO F   13          0         1.50
SITE     1 AC1 15 HIS A  46  HIS A  48  HIS A  63  HIS A 120
SITE     2 AC1 15 THR A 137  ARG A 143   CU A1157   ZN A1159
SITE     3 AC1 15 HOH A2177  HOH A2178  HOH A2191  HOH A2192
SITE     4 AC1 15 HOH A2193  HOH A2194  HOH A2196
SITE     1 AC2  6 THR A  58  ARG A 143  HOH A2080  HOH A2195
SITE     2 AC2  6 HOH A2196  HOH A2197
SITE     1 AC3  5 HIS A  46  HIS A  48  HIS A 120  SO4 A1154
SITE     2 AC3  5  ZN A1159
SITE     1 AC4  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83
SITE     1 AC5  8 HIS A  46  HIS A  48  HIS A  63  HIS A 120
SITE     2 AC5  8 SO4 A1154   CU A1157  HOH A2191  HOH A2193
SITE     1 AC6 16 HIS F  46  HIS F  48  HIS F  63  HIS F 120
SITE     2 AC6 16 THR F 137  ARG F 143   ZN F1155   CU F1156
SITE     3 AC6 16 HOH F2172  HOH F2173  HOH F2185  HOH F2186
SITE     4 AC6 16 HOH F2187  HOH F2188  HOH F2189  HOH F2190
SITE     1 AC7  8 HIS F  46  HIS F  48  HIS F  63  HIS F 120
SITE     2 AC7  8 SO4 F1154   CU F1156  HOH F2189  HOH F2190
SITE     1 AC8  7 HIS F  46  HIS F  48  HIS F  63  HIS F 120
SITE     2 AC8  7 SO4 F1154   ZN F1155  HOH F2190
SITE     1 AC9  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83
SITE     1 BC1  6 GLY F  85  ASN F  86  LEU F 126  HOH F2041
SITE     2 BC1  6 HOH F2191  HOH F2192
SITE     1 BC2  3 GLY F  10  ASP F  11  HOH F2175
CRYST1   38.638   67.553   52.320  90.00 106.48  90.00 P 1 21 1      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      0.025881  0.000000  0.007657        0.00000
SCALE2      0.000000  0.014803  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019932        0.00000
      
PROCHECK
Go to PROCHECK summary
 References