HEADER OXIDOREDUCTASE 13-MAR-03 1HL4
TITLE THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B, C, D;
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 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: EG118;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: YEP351
KEYWDS OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,P.J.HART,
AUTHOR 2 L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN
REVDAT 3 13-JUL-11 1HL4 1 VERSN
REVDAT 2 24-FEB-09 1HL4 1 VERSN
REVDAT 1 08-MAY-03 1HL4 0
JRNL AUTH R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,
JRNL AUTH 2 P.J.HART,L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN
JRNL TITL THE STRUCTURE OF HOLO AND METAL-DEFICIENT WILD-TYPE HUMAN
JRNL TITL 2 CU, ZN SUPEROXIDE DISMUTASE AND ITS RELEVANCE TO FAMILIAL
JRNL TITL 3 AMYOTROPHIC LATERAL SCLEROSIS
JRNL REF J.MOL.BIOL. V. 328 877 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12729761
JRNL DOI 10.1016/S0022-2836(03)00355-3
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 47806
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2545
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2938
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3690
REMARK 3 BIN FREE R VALUE SET COUNT : 167
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.96000
REMARK 3 B22 (A**2) : 8.87000
REMARK 3 B33 (A**2) : -5.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.69000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.695
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4062 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5492 ; 1.819 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 549 ; 4.762 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 656 ;21.915 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 623 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3090 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1873 ; 0.222 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 479 ; 0.193 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.190 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 39 ; 0.185 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.334 ; 0.500
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): 2714 ; 1.198 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4304 ; 1.608 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1348 ; 2.910 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1188 ; 3.758 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3230 -2.5300 20.7480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1922 T22: 0.1108
REMARK 3 T33: 0.1997 T12: -0.0052
REMARK 3 T13: 0.0202 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.2765 L22: 0.7852
REMARK 3 L33: 1.9569 L12: 0.1158
REMARK 3 L13: 0.5674 L23: 0.1294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0469 S12: 0.1603 S13: -0.0890
REMARK 3 S21: -0.0800 S22: -0.0491 S23: -0.0227
REMARK 3 S31: 0.0730 S32: 0.0248 S33: 0.0021
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 0 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8120 2.5550 46.5030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1585 T22: 0.1559
REMARK 3 T33: 0.2102 T12: -0.0249
REMARK 3 T13: 0.0079 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.1759 L22: 0.6777
REMARK 3 L33: 1.9011 L12: -0.0593
REMARK 3 L13: 0.2634 L23: -0.0656
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: -0.2088 S13: 0.0367
REMARK 3 S21: 0.0104 S22: 0.0213 S23: -0.0295
REMARK 3 S31: 0.0043 S32: 0.0004 S33: -0.0169
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 153
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9140 11.7480 30.4600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1839 T22: 0.0101
REMARK 3 T33: 0.2097 T12: -0.0400
REMARK 3 T13: 0.0079 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 2.0460 L22: 0.9230
REMARK 3 L33: 2.9785 L12: 0.3265
REMARK 3 L13: -0.1157 L23: 0.0417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: -0.2785 S13: 0.0774
REMARK 3 S21: -0.0237 S22: -0.0181 S23: -0.0128
REMARK 3 S31: -0.0973 S32: 0.2112 S33: -0.0183
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 153
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7840 5.2450 8.5970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2253 T22: 0.0122
REMARK 3 T33: 0.2179 T12: -0.0273
REMARK 3 T13: -0.0071 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.6552 L22: 1.4424
REMARK 3 L33: 3.2502 L12: 0.0299
REMARK 3 L13: 0.2515 L23: 0.0485
REMARK 3 S TENSOR
REMARK 3 S11: 0.0116 S12: 0.2408 S13: -0.0718
REMARK 3 S21: -0.0622 S22: -0.0191 S23: 0.0385
REMARK 3 S31: 0.0728 S32: -0.0322 S33: 0.0075
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED REGIONS IN MONOMERS B AND
REMARK 3 D WERE REMOVED FROM THE STRUCTURE
REMARK 4
REMARK 4 1HL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-03.
REMARK 100 THE PDBE ID CODE IS EBI-12324.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-02
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 : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 265996
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 1SOS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NH4CL, 20%PEG2000,
REMARK 280 10% ETHYLENE GLYCOL, 0.1 M MES PH 5.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 78.20200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.48900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.20200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 17.48900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ACE A 0
REMARK 465 ACE C 0
REMARK 465 ARG C 69
REMARK 465 LYS C 70
REMARK 465 HIS C 71
REMARK 465 GLY C 72
REMARK 465 GLY C 73
REMARK 465 PRO C 74
REMARK 465 LYS C 75
REMARK 465 ASP C 76
REMARK 465 GLU C 77
REMARK 465 GLU C 78
REMARK 465 ASP C 125
REMARK 465 LEU C 126
REMARK 465 GLY C 127
REMARK 465 LYS C 128
REMARK 465 GLY C 129
REMARK 465 GLY C 130
REMARK 465 ASN C 131
REMARK 465 GLU C 132
REMARK 465 GLU C 133
REMARK 465 SER C 134
REMARK 465 THR C 135
REMARK 465 LYS C 136
REMARK 465 THR C 137
REMARK 465 GLY C 138
REMARK 465 ASN C 139
REMARK 465 ALA C 140
REMARK 465 ACE D 0
REMARK 465 SER D 68
REMARK 465 ARG D 69
REMARK 465 LYS D 70
REMARK 465 HIS D 71
REMARK 465 GLY D 72
REMARK 465 GLY D 73
REMARK 465 PRO D 74
REMARK 465 LYS D 75
REMARK 465 ASP D 76
REMARK 465 GLU D 77
REMARK 465 GLU D 78
REMARK 465 ASP D 125
REMARK 465 LEU D 126
REMARK 465 GLY D 127
REMARK 465 LYS D 128
REMARK 465 GLY D 129
REMARK 465 GLY D 130
REMARK 465 ASN D 131
REMARK 465 GLU D 132
REMARK 465 GLU D 133
REMARK 465 SER D 134
REMARK 465 THR D 135
REMARK 465 LYS D 136
REMARK 465 THR D 137
REMARK 465 GLY D 138
REMARK 465 ASN D 139
REMARK 465 ALA D 140
REMARK 465 GLY D 141
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 LYS A 23 CG CD CE NZ
REMARK 470 GLU A 24 CD OE1 OE2
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 LYS A 70 CE NZ
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 136 NZ
REMARK 470 LYS B 9 CD CE NZ
REMARK 470 LYS B 75 CE NZ
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 LYS B 91 NZ
REMARK 470 LYS B 122 CE NZ
REMARK 470 SER C 68 C O OG
REMARK 470 HIS C 80 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 91 CE NZ
REMARK 470 LYS C 122 CD CE NZ
REMARK 470 HIS D 80 C O CB CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 83 CG OD1 OD2
REMARK 470 LYS D 91 CG CD CE NZ
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 OD2 ASP B 124 O HOH B 2078 2.17
REMARK 500 NH2 ARG C 79 OD1 ASP C 101 2.01
REMARK 500 O HOH C 2049 O HOH B 2069 1.98
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 O HOH B 2013 O HOH B 2026 2556 2.19
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 76 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 101 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 109 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 115 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 143 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP C 11 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU C 38 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 ASP C 52 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 124 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 124 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS B 136 -53.66 -125.50
REMARK 500 ASN C 65 87.13 -159.78
REMARK 500 ASP C 90 -168.92 -76.29
REMARK 500 ASN D 65 72.96 -152.05
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 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 71 ND1
REMARK 620 2 ASP A 83 OD1 75.2
REMARK 620 3 HIS A 63 ND1 119.9 131.8
REMARK 620 4 HIS A 80 ND1 122.1 113.8 96.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 ND1
REMARK 620 2 HIS B 80 ND1 97.7
REMARK 620 3 ASP B 83 OD1 110.9 109.1
REMARK 620 4 HIS B 71 ND1 125.8 121.4 91.2
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
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 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WZ6 RELATED DB: PDB
REMARK 900 G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.
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: 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: 1AZV RELATED DB: PDB
REMARK 900 FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)
REMARK 900 RELATED ID: 2WYZ RELATED DB: PDB
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH UMP
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: 2VR6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF
REMARK 900 HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)
REMARK 900 AT 1.3 A RESOLUTION
REMARK 900 RELATED ID: 2C9V RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2WZ5 RELATED DB: PDB
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE
REMARK 900 .
REMARK 900 RELATED ID: 2XJL RELATED DB: PDB
REMARK 900 MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE
REMARK 900 WITHOUT CU LIGANDS
REMARK 900 RELATED ID: 1PU0 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE
REMARK 900 DISMUTASE
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: 2XJK RELATED DB: PDB
REMARK 900 MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE
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: 1N19 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT
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: 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: 2WKO RELATED DB: PDB
REMARK 900 STRUCTURE OF METAL LOADED PATHOGENIC SOD1
REMARK 900 MUTANT G93A.
REMARK 900 RELATED ID: 2WZ0 RELATED DB: PDB
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH ANILINE.
REMARK 900 RELATED ID: 1UXL RELATED DB: PDB
REMARK 900 I113T 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: 2VR8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF
REMARK 900 HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)
REMARK 900 AT 1.36 A RESOLUTION
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: 2VR7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF
REMARK 900 HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)
REMARK 900 AT 1.58 A RESOLUTION
REMARK 900 RELATED ID: 2V0A RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN
REMARK 900 SUPEROXIDE DISMUTASE
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: 2C9S RELATED DB: PDB
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-
REMARK 900 ZN HUMAN 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: 2WYT RELATED DB: PDB
REMARK 900 1.0 A RESOLUTION STRUCTURE OF L38V SOD1
REMARK 900 MUTANT
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: 1KMG RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER-
REMARK 900 FREE SUPEROXIDEDISMUTASE
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: 1N18 RELATED DB: PDB
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE
REMARK 900 DISMUTASE, C6A,C111S
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: 1HL5 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 2C9U RELATED DB: PDB
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-
REMARK 900 ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1UXM RELATED DB: PDB
REMARK 900 A4V MUTANT OF HUMAN SOD1
REMARK 900 RELATED ID: 1SPD RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE
DBREF 1HL4 A 0 0 PDB 1HL4 1HL4 0 0
DBREF 1HL4 A 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL4 B 0 0 PDB 1HL4 1HL4 0 0
DBREF 1HL4 B 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL4 C 0 0 PDB 1HL4 1HL4 0 0
DBREF 1HL4 C 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL4 D 0 0 PDB 1HL4 1HL4 0 0
DBREF 1HL4 D 1 153 UNP P00441 SODC_HUMAN 2 154
SEQRES 1 A 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 A 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 A 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 A 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 A 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 A 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 A 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 A 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 A 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 A 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 A 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 A 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 B 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 B 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 B 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 B 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 B 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 B 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 B 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 B 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 B 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 B 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 B 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 B 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 C 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 C 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 C 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 C 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 C 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 C 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 C 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 C 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 C 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 C 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 C 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 C 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 D 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 D 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 D 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 D 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 D 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 D 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 D 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 D 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 D 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 D 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 D 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 D 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET ZN A 155 1
HET ZN B 155 1
HET ACE B 0 3
HETNAM ZN ZINC ION
HETNAM ACE ACETYL GROUP
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 ACE C2 H4 O
FORMUL 7 HOH *311(H2 O)
HELIX 1 1 ALA A 55 GLY A 61 5 7
HELIX 2 2 GLU A 132 LYS A 136 5 5
HELIX 3 3 GLY B 56 GLY B 61 5 6
HELIX 4 4 GLU B 133 GLY B 138 1 6
HELIX 5 5 ALA C 55 GLY C 61 5 7
HELIX 6 6 SER C 107 HIS C 110 5 4
HELIX 7 7 ALA D 55 GLY D 61 5 7
SHEET 1 AA11 THR A 2 GLY A 10 0
SHEET 2 AA11 GLN A 15 GLN A 22 -1 O GLY A 16 N LEU A 8
SHEET 3 AA11 VAL A 29 LYS A 36 -1 O LYS A 30 N GLU A 21
SHEET 4 AA11 ALA A 95 ASP A 101 -1 O ALA A 95 N ILE A 35
SHEET 5 AA11 ASP A 83 ALA A 89 -1 O THR A 88 N ASP A 96
SHEET 6 AA11 GLY A 41 HIS A 48 -1 O GLY A 41 N ALA A 89
SHEET 7 AA11 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 8 AA11 ARG A 143 VAL A 148 -1 N LEU A 144 O VAL A 119
SHEET 9 AA11 THR A 2 GLY A 10 -1 O LYS A 9 N CYS A 146
SHEET 10 AA11 GLN A 15 GLN A 22 -1 O GLY A 16 N LEU A 8
SHEET 11 AA11 THR A 2 GLY A 10 -1 O THR A 2 N GLN A 22
SHEET 1 BA 5 ALA B 95 ASP B 101 0
SHEET 2 BA 5 VAL B 29 LYS B 36 -1 O VAL B 29 N ASP B 101
SHEET 3 BA 5 GLN B 15 GLU B 21 -1 O GLN B 15 N LYS B 36
SHEET 4 BA 5 LYS B 3 LYS B 9 -1 O ALA B 4 N PHE B 20
SHEET 5 BA 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 BB 4 ASP B 83 ALA B 89 0
SHEET 2 BB 4 GLY B 41 HIS B 48 -1 O GLY B 41 N ALA B 89
SHEET 3 BB 4 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 4 BB 4 ARG B 143 VAL B 148 -1 N LEU B 144 O VAL B 119
SHEET 1 CA 5 ALA C 95 ASP C 101 0
SHEET 2 CA 5 VAL C 29 LYS C 36 -1 O VAL C 29 N ASP C 101
SHEET 3 CA 5 GLN C 15 GLN C 22 -1 O GLN C 15 N LYS C 36
SHEET 4 CA 5 LYS C 3 LEU C 8 -1 O ALA C 4 N PHE C 20
SHEET 5 CA 5 GLY C 150 ILE C 151 -1 O GLY C 150 N VAL C 5
SHEET 1 CB 4 ASP C 83 ALA C 89 0
SHEET 2 CB 4 GLY C 41 HIS C 48 -1 O GLY C 41 N ALA C 89
SHEET 3 CB 4 THR C 116 HIS C 120 -1 O THR C 116 N HIS C 48
SHEET 4 CB 4 ARG C 143 VAL C 148 -1 N LEU C 144 O VAL C 119
SHEET 1 DA 5 ALA D 95 ASP D 101 0
SHEET 2 DA 5 VAL D 29 LYS D 36 -1 O VAL D 29 N ASP D 101
SHEET 3 DA 5 GLN D 15 GLN D 22 -1 O GLN D 15 N LYS D 36
SHEET 4 DA 5 LYS D 3 LYS D 9 -1 O ALA D 4 N PHE D 20
SHEET 5 DA 5 GLY D 150 ILE D 151 -1 O GLY D 150 N VAL D 5
SHEET 1 DB 4 ASP D 83 ALA D 89 0
SHEET 2 DB 4 GLY D 41 HIS D 48 -1 O GLY D 41 N ALA D 89
SHEET 3 DB 4 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48
SHEET 4 DB 4 ARG D 143 VAL D 148 -1 N LEU D 144 O VAL D 119
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.03
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.07
SSBOND 3 CYS C 57 CYS C 146 1555 1555 2.08
SSBOND 4 CYS D 57 CYS D 146 1555 1555 2.05
LINK ZN ZN A 155 ND1 HIS A 71 1555 1555 2.45
LINK ZN ZN A 155 OD1 ASP A 83 1555 1555 2.08
LINK ZN ZN A 155 ND1 HIS A 63 1555 1555 2.03
LINK ZN ZN A 155 ND1 HIS A 80 1555 1555 1.91
LINK C ACE B 0 N ALA B 1 1555 1555 1.33
LINK ZN ZN B 155 OD1 ASP B 83 1555 1555 1.90
LINK ZN ZN B 155 ND1 HIS B 71 1555 1555 2.17
LINK ZN ZN B 155 ND1 HIS B 80 1555 1555 1.98
LINK ZN ZN B 155 ND1 HIS B 63 1555 1555 1.97
SITE 1 AC1 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC2 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
CRYST1 156.404 34.978 114.809 90.00 112.26 90.00 C 1 2 1 16
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 0.006394 0.000000 0.002617 0.00000
SCALE2 0.000000 0.028589 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009411 0.00000
MTRIX1 1 0.763240 -0.016790 -0.645900 19.85701 1
MTRIX2 1 -0.025800 -0.999660 -0.004490 0.08071 1
MTRIX3 1 -0.645610 0.020090 -0.763410 53.73026 1
MTRIX1 2 -0.969750 -0.244100 0.001570 17.90989 1
MTRIX2 2 -0.205170 0.811570 -0.547040 9.16435 1
MTRIX3 2 0.132260 -0.530820 -0.837100 51.25463 1
MTRIX1 3 -0.834840 0.141310 0.532040 0.75498 1
MTRIX2 3 0.207630 -0.814280 0.542070 -9.10994 1
MTRIX3 3 0.509830 0.563010 0.650450 3.23855 1
(ATOM LINES ARE NOT SHOWN.)
END
