HEADER OXIDOREDUCTASE 14-APR-09 3H2P
TITLE HUMAN SOD1 D124V VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SOD1;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: EGY118;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: YEP351-HSOD
KEYWDS OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,
KEYWDS 2 METAL-BINDING, COPPER, ZINC, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE
KEYWDS 3 MUTATION, ACETYLATION, CYTOPLASM, DISULFIDE BOND, PHOSPHOPROTEIN,
KEYWDS 4 UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.V.SEETHARAMAN,D.D.WINKLER,A.B.TAYLOR,X.CAO,L.J.WHITSON,
AUTHOR 2 P.A.DOUCETTE,J.S.VALENTINE,M.C.CARROLL,V.C.CULOTTA,P.J.HART
REVDAT 1 05-MAY-10 3H2P 0
JRNL AUTH S.V.SEETHARAMAN,D.D.WINKLER,A.B.TAYLOR,X.CAO,L.J.WHITSON,
JRNL AUTH 2 P.A.DOUCETTE,J.S.VALENTINE,M.C.CARROLL,V.C.CULOTTA,P.J.HART
JRNL TITL STRUCTURES OF PATHOGENIC SOD1 MUTANTS H80R AND D124V:
JRNL TITL 2 DISRUPTED ZINC-BINDING AND COMPROMISED POST-TRANSLATIONAL
JRNL TITL 3 MODIFICATION BY THE COPPER CHAPERONE CCS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 35621
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1776
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.9307 - 3.6496 1.00 2804 161 0.1567 0.1638
REMARK 3 2 3.6496 - 2.8971 0.99 2650 149 0.1503 0.1859
REMARK 3 3 2.8971 - 2.5310 0.99 2623 136 0.1665 0.2178
REMARK 3 4 2.5310 - 2.2996 0.99 2634 125 0.1458 0.2336
REMARK 3 5 2.2996 - 2.1348 0.99 2612 135 0.1303 0.2021
REMARK 3 6 2.1348 - 2.0089 1.00 2596 135 0.1158 0.1728
REMARK 3 7 2.0089 - 1.9083 1.00 2587 150 0.1172 0.1776
REMARK 3 8 1.9083 - 1.8252 1.00 2612 134 0.1248 0.2229
REMARK 3 9 1.8252 - 1.7550 1.00 2577 137 0.1310 0.2033
REMARK 3 10 1.7550 - 1.6944 1.00 2626 137 0.1462 0.2390
REMARK 3 11 1.6944 - 1.6414 0.99 2557 137 0.1573 0.2485
REMARK 3 12 1.6414 - 1.5945 0.98 2543 115 0.1581 0.2296
REMARK 3 13 1.5945 - 1.5500 0.93 2424 125 0.1610 0.2337
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.41
REMARK 3 B_SOL : 56.40
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.14
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.56360
REMARK 3 B22 (A**2) : 7.25450
REMARK 3 B33 (A**2) : -1.69090
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 NULL
REMARK 3 ANGLE : 0.903 NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3H2P COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052616.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35692
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.56600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: 1AZV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 19.95950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.51050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.98600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.51050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.95950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.98600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LEU A 67
REMARK 465 SER A 68
REMARK 465 ARG A 69
REMARK 465 LYS A 70
REMARK 465 HIS A 71
REMARK 465 GLY A 72
REMARK 465 GLY A 73
REMARK 465 PRO A 74
REMARK 465 LYS A 75
REMARK 465 ASP A 76
REMARK 465 GLU A 77
REMARK 465 GLU A 78
REMARK 465 ASP A 125
REMARK 465 LEU A 126
REMARK 465 GLY A 127
REMARK 465 LYS A 128
REMARK 465 GLY A 129
REMARK 465 GLY A 130
REMARK 465 ASN A 131
REMARK 465 GLU A 132
REMARK 465 GLU A 133
REMARK 465 SER A 134
REMARK 465 THR A 135
REMARK 465 LYS A 136
REMARK 465 THR A 137
REMARK 465 GLY A 138
REMARK 465 ASN A 139
REMARK 465 ARG B 69
REMARK 465 LYS B 70
REMARK 465 HIS B 71
REMARK 465 GLY B 72
REMARK 465 GLY B 73
REMARK 465 PRO B 74
REMARK 465 LYS B 75
REMARK 465 ASP B 76
REMARK 465 GLU B 77
REMARK 465 GLU B 78
REMARK 465 ASP B 125
REMARK 465 LEU B 126
REMARK 465 GLY B 127
REMARK 465 LYS B 128
REMARK 465 GLY B 129
REMARK 465 GLY B 130
REMARK 465 ASN B 131
REMARK 465 GLU B 132
REMARK 465 GLU B 133
REMARK 465 SER B 134
REMARK 465 THR B 135
REMARK 465 LYS B 136
REMARK 465 THR B 137
REMARK 465 GLY B 138
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 HIS A 63 CD2 CE1 NE2
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 ASN A 65 84.64 -160.25
REMARK 500 ASN B 65 74.74 -160.43
REMARK 500 LEU B 67 36.88 -78.34
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 ZN A 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 132.2
REMARK 620 3 HIS A 120 NE2 94.9 105.5
REMARK 620 4 MLI A 156 O8 116.8 101.2 101.2
REMARK 620 5 HIS A 63 NE2 70.1 112.9 138.8 57.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 HIS A 80 ND1 112.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 154 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 48 NE2 129.9
REMARK 620 3 HIS B 120 NE2 101.2 109.7
REMARK 620 4 MLI B 155 O6 100.9 100.4 115.0
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 ZN A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE B 0
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI B 155
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3H2Q RELATED DB: PDB
REMARK 900 HUMAN SOD1 H80R VARIANT, P21 CRYSTAL FORM
REMARK 900 RELATED ID: 3H2R RELATED DB: PDB
REMARK 900 HUMAN SOD1 H80R VARIANT, P212121 CRYSTAL FORM
DBREF 3H2P A 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3H2P B 1 153 UNP P00441 SODC_HUMAN 2 154
SEQADV 3H2P VAL A 124 UNP P00441 ASP 125 ENGINEERED
SEQADV 3H2P VAL B 124 UNP P00441 ASP 125 ENGINEERED
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 VAL 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 B 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 B 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 B 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 B 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 B 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 B 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 B 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 B 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 B 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 B 153 VAL VAL HIS GLU LYS ALA VAL ASP LEU GLY LYS GLY GLY
SEQRES 11 B 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 B 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET ZN A 154 1
HET ZN A 155 1
HET MLI A 156 7
HET ACE B 0 3
HET ZN B 154 1
HET MLI B 155 7
HETNAM ZN ZINC ION
HETNAM MLI MALONATE ION
HETNAM ACE ACETYL GROUP
FORMUL 3 ZN 3(ZN 2+)
FORMUL 5 MLI 2(C3 H2 O4 2-)
FORMUL 6 ACE C2 H4 O
FORMUL 9 HOH *259(H2 O)
HELIX 1 1 ALA A 55 ALA A 60 5 6
HELIX 2 2 SER A 107 CYS A 111 5 5
HELIX 3 3 ALA B 55 ALA B 60 5 6
HELIX 4 4 SER B 107 CYS B 111 5 5
SHEET 1 A 5 ALA A 95 ASP A 101 0
SHEET 2 A 5 VAL A 29 LYS A 36 -1 N ILE A 35 O ALA A 95
SHEET 3 A 5 GLN A 15 GLN A 22 -1 N ASN A 19 O TRP A 32
SHEET 4 A 5 THR A 2 LYS A 9 -1 N ALA A 4 O PHE A 20
SHEET 5 A 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 B 4 ASP A 83 ALA A 89 0
SHEET 2 B 4 GLY A 41 HIS A 48 -1 N HIS A 43 O VAL A 87
SHEET 3 B 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 4 B 4 ARG A 143 VAL A 148 -1 O GLY A 147 N LEU A 117
SHEET 1 C 5 ALA B 95 ASP B 101 0
SHEET 2 C 5 VAL B 29 LYS B 36 -1 N ILE B 35 O ALA B 95
SHEET 3 C 5 GLN B 15 GLU B 21 -1 N ASN B 19 O TRP B 32
SHEET 4 C 5 LYS B 3 LEU B 8 -1 N LEU B 8 O GLY B 16
SHEET 5 C 5 GLY B 150 GLN B 153 -1 O GLY B 150 N VAL B 5
SHEET 1 D 4 ASP B 83 ALA B 89 0
SHEET 2 D 4 GLY B 41 HIS B 48 -1 N GLY B 41 O ALA B 89
SHEET 3 D 4 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 4 D 4 ARG B 143 VAL B 148 -1 O GLY B 147 N LEU B 117
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.07
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.07
LINK ND1 HIS A 46 ZN ZN A 154 1555 1555 2.38
LINK NE2 HIS A 48 ZN ZN A 154 1555 1555 2.11
LINK ND1 HIS A 63 ZN ZN A 155 1555 1555 1.80
LINK ND1 HIS A 80 ZN ZN A 155 1555 1555 2.36
LINK NE2 HIS A 120 ZN ZN A 154 1555 1555 2.15
LINK ND1 HIS B 46 ZN ZN B 154 1555 1555 2.17
LINK NE2 HIS B 48 ZN ZN B 154 1555 1555 2.12
LINK NE2 HIS B 120 ZN ZN B 154 1555 1555 2.13
LINK ZN ZN A 154 O8 MLI A 156 1555 1555 2.28
LINK ZN ZN B 154 O6 MLI B 155 1555 1555 1.88
LINK N ALA B 1 C ACE B 0 1555 1555 1.33
LINK NE2 HIS A 63 ZN ZN A 154 1555 1555 2.55
SITE 1 AC1 4 HIS A 46 HIS A 48 HIS A 120 MLI A 156
SITE 1 AC2 2 HIS A 63 HIS A 80
SITE 1 AC3 6 HIS A 46 HIS A 48 HIS A 120 ALA A 140
SITE 2 AC3 6 ARG A 143 ZN A 154
SITE 1 AC4 3 ALA B 1 THR B 2 HOH B 218
SITE 1 AC5 4 HIS B 46 HIS B 48 HIS B 120 MLI B 155
SITE 1 AC6 11 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 2 AC6 11 ALA B 140 ZN B 154 HOH B 192 HOH B 216
SITE 3 AC6 11 HOH B 229 HOH B 287 HOH B 288
CRYST1 39.919 57.972 105.021 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.025051 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017250 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009522 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
