HEADER OXIDOREDUCTASE 22-NOV-17 5YUL
TITLE NATIVE STRUCTURE OF HSOD1 IN P6322 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, H, B, C, D, E, F, G, I, J;
COMPND 4 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: 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: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETM11
KEYWDS DIMER, NATIVE, OXIDOREDUCTASE, DISMUTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MANJULA,B.PADMANABHAN
REVDAT 2 22-NOV-23 5YUL 1 LINK
REVDAT 1 21-NOV-18 5YUL 0
JRNL AUTH R.MANJULA,G.S.A.WRIGHT,R.W.STRANGE,B.PADMANABHAN
JRNL TITL ASSESSMENT OF LIGAND BINDING AT A SITE RELEVANT TO SOD1
JRNL TITL 2 OXIDATION AND AGGREGATION
JRNL REF FEBS LETT. V. 592 1725 2018
JRNL REFN ISSN 1873-3468
JRNL PMID 29679384
JRNL DOI 10.1002/1873-3468.13055
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 183647
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9635
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13213
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 723
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10957
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 1377
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : 0.50000
REMARK 3 B33 (A**2) : -1.62000
REMARK 3 B12 (A**2) : 0.50000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.683
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11292 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15261 ; 1.839 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1535 ; 6.605 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 474 ;41.845 ;25.591
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1846 ;14.292 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;19.526 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1685 ; 0.138 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8638 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 5YUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1300005911.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 193714
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 1HL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 72.05650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 72.05650
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.05650
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 72.05650
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 72.05650
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 72.05650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
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: 14090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
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: 1460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
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: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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 MET F 0
REMARK 465 MET J 0
REMARK 465 LEU J 67
REMARK 465 SER J 68
REMARK 465 ARG J 69
REMARK 465 LYS J 70
REMARK 465 HIS J 71
REMARK 465 GLY J 72
REMARK 465 GLY J 73
REMARK 465 PRO J 74
REMARK 465 LYS J 75
REMARK 465 ASP J 76
REMARK 465 GLU J 77
REMARK 465 GLU J 78
REMARK 465 LEU J 126
REMARK 465 GLY J 127
REMARK 465 LYS J 128
REMARK 465 GLY J 129
REMARK 465 GLY J 130
REMARK 465 ASN J 131
REMARK 465 GLU J 132
REMARK 465 GLU J 133
REMARK 465 SER J 134
REMARK 465 THR J 135
REMARK 465 LYS J 136
REMARK 465 THR J 137
REMARK 465 GLY J 138
REMARK 465 ASN J 139
REMARK 465 ALA J 140
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 MET C 0 CG SD CE
REMARK 470 MET D 0 CG SD CE
REMARK 470 MET E 0 CG SD CE
REMARK 470 MET I 0 CG SD CE
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 HOH B 406 O HOH B 409 2.15
REMARK 500 O HOH A 350 O HOH H 398 2.16
REMARK 500 O HOH A 490 O HOH A 497 2.17
REMARK 500 O HOH D 403 O HOH D 410 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 LEU A 67 CB - CG - CD2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 ASP A 90 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP H 90 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG H 115 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG H 115 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 115 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 115 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP B 125 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP G 90 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP J 90 CB - CG - OD1 ANGL. DEV. = 5.6 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 ASN F 26 -33.87 66.39
REMARK 500 ASP F 90 -177.67 -67.87
REMARK 500 LYS G 136 -65.89 -104.20
REMARK 500 ASN I 65 60.74 -150.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 501 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH B 504 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 505 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH B 506 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH B 507 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH B 508 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH C 446 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH D 494 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH D 495 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH D 496 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH D 497 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH D 498 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH D 499 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH E 417 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH G 392 DISTANCE = 5.96 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 HIS A 71 ND1 108.2
REMARK 620 3 HIS A 80 ND1 108.9 124.3
REMARK 620 4 ASP A 83 OD1 104.5 96.0 112.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 63 ND1
REMARK 620 2 HIS H 71 ND1 106.1
REMARK 620 3 HIS H 80 ND1 112.1 122.5
REMARK 620 4 ASP H 83 OD1 105.6 85.9 121.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 ND1
REMARK 620 2 HIS B 71 ND1 103.6
REMARK 620 3 HIS B 80 ND1 110.5 125.7
REMARK 620 4 ASP B 83 OD1 104.1 92.4 117.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 63 ND1
REMARK 620 2 HIS C 71 ND1 106.2
REMARK 620 3 HIS C 80 ND1 112.3 124.7
REMARK 620 4 ASP C 83 OD1 105.7 85.2 118.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 63 ND1
REMARK 620 2 HIS D 71 ND1 105.2
REMARK 620 3 HIS D 80 ND1 112.4 123.2
REMARK 620 4 ASP D 83 OD2 105.0 91.5 116.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 63 ND1
REMARK 620 2 HIS E 71 ND1 93.6
REMARK 620 3 HIS E 80 ND1 118.6 115.7
REMARK 620 4 ASP E 83 OD1 106.4 99.5 118.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 63 ND1
REMARK 620 2 HIS F 71 ND1 100.7
REMARK 620 3 HIS F 80 ND1 112.1 124.7
REMARK 620 4 ASP F 83 OD1 103.6 96.2 116.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 63 ND1
REMARK 620 2 HIS G 71 ND1 102.5
REMARK 620 3 HIS G 80 ND1 113.5 120.6
REMARK 620 4 ASP G 83 OD1 114.9 85.9 116.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 63 ND1
REMARK 620 2 HIS I 71 ND1 106.6
REMARK 620 3 HIS I 80 ND1 106.2 127.5
REMARK 620 4 ASP I 83 OD1 106.6 92.9 115.2
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue S4P A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue S4P J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide S4P C 202 and CYS C
REMARK 800 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide S4P D 202 and CYS E
REMARK 800 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide S4P D 202 and CYS D
REMARK 800 111
DBREF 5YUL A 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL H 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL B 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL C 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL D 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL E 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL F 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL G 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL I 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 5YUL J 0 153 UNP P00441 SODC_HUMAN 1 154
SEQRES 1 A 154 MET 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 H 154 MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 H 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 H 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 H 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 H 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 H 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 H 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 H 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 H 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 H 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 H 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 H 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 B 154 MET 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 MET 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 MET 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
SEQRES 1 E 154 MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 E 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 E 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 E 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 E 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 E 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 E 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 E 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 E 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 E 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 E 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 E 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 F 154 MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 F 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 F 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 F 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 F 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 F 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 F 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 F 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 F 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 F 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 F 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 F 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 G 154 MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 G 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 G 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 G 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 G 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 G 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 G 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 G 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 G 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 G 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 G 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 G 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 I 154 MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 I 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 I 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 I 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 I 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 I 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 I 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 I 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 I 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 I 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 I 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 I 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 J 154 MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 J 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 J 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 J 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 J 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 J 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 J 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 J 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 J 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 J 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 J 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 J 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET ZN A 201 1
HET S4P A 202 4
HET ZN H 201 1
HET ZN B 201 1
HET ZN C 201 1
HET S4P C 202 4
HET GOL C 203 6
HET ZN D 201 1
HET S4P D 202 4
HET ZN E 201 1
HET ZN F 201 1
HET ZN G 201 1
HET ZN I 201 1
HET S4P J 201 4
HETNAM ZN ZINC ION
HETNAM S4P DIHYDROGEN TETRASULFIDE
HETNAM GOL GLYCEROL
HETSYN S4P TETRASULFANE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 11 ZN 9(ZN 2+)
FORMUL 12 S4P 4(H2 S4)
FORMUL 17 GOL C3 H8 O3
FORMUL 25 HOH *1377(H2 O)
HELIX 1 AA1 ALA A 55 GLY A 61 5 7
HELIX 2 AA2 SER A 107 CYS A 111 5 5
HELIX 3 AA3 GLU A 133 GLY A 138 1 6
HELIX 4 AA4 ALA H 55 GLY H 61 5 7
HELIX 5 AA5 ASN H 131 GLY H 138 1 8
HELIX 6 AA6 ALA B 55 GLY B 61 5 7
HELIX 7 AA7 SER B 107 CYS B 111 5 5
HELIX 8 AA8 GLU B 133 GLY B 138 1 6
HELIX 9 AA9 ALA C 55 GLY C 61 5 7
HELIX 10 AB1 GLU C 132 LYS C 136 5 5
HELIX 11 AB2 ALA D 55 GLY D 61 5 7
HELIX 12 AB3 SER D 107 CYS D 111 5 5
HELIX 13 AB4 GLU D 133 GLY D 138 1 6
HELIX 14 AB5 ALA E 55 GLY E 61 5 7
HELIX 15 AB6 ASN E 131 GLY E 138 1 8
HELIX 16 AB7 ALA F 55 GLY F 61 5 7
HELIX 17 AB8 SER F 107 CYS F 111 5 5
HELIX 18 AB9 GLU F 133 GLY F 138 1 6
HELIX 19 AC1 ALA G 55 GLY G 61 5 7
HELIX 20 AC2 GLU G 132 LYS G 136 5 5
HELIX 21 AC3 ALA I 55 GLY I 61 5 7
HELIX 22 AC4 ASN I 131 GLY I 138 1 8
HELIX 23 AC5 ALA J 55 GLY J 61 5 7
SHEET 1 AA1 5 ALA A 95 ASP A 101 0
SHEET 2 AA1 5 VAL A 29 LYS A 36 -1 N ILE A 35 O ALA A 95
SHEET 3 AA1 5 GLN A 15 GLU A 21 -1 N ASN A 19 O TRP A 32
SHEET 4 AA1 5 LYS A 3 LEU A 8 -1 N CYS A 6 O ILE A 18
SHEET 5 AA1 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 AA2 4 ASP A 83 ALA A 89 0
SHEET 2 AA2 4 GLY A 41 HIS A 48 -1 N GLY A 41 O ALA A 89
SHEET 3 AA2 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 4 AA2 4 ARG A 143 VAL A 148 -1 O LEU A 144 N VAL A 119
SHEET 1 AA3 5 ALA H 95 ASP H 101 0
SHEET 2 AA3 5 VAL H 29 LYS H 36 -1 N VAL H 29 O ASP H 101
SHEET 3 AA3 5 GLN H 15 GLU H 21 -1 N ASN H 19 O TRP H 32
SHEET 4 AA3 5 LYS H 3 LEU H 8 -1 N LEU H 8 O GLY H 16
SHEET 5 AA3 5 GLY H 150 ILE H 151 -1 O GLY H 150 N VAL H 5
SHEET 1 AA4 4 ASP H 83 ALA H 89 0
SHEET 2 AA4 4 GLY H 41 HIS H 48 -1 N GLY H 41 O ALA H 89
SHEET 3 AA4 4 THR H 116 HIS H 120 -1 O THR H 116 N HIS H 48
SHEET 4 AA4 4 ARG H 143 VAL H 148 -1 O LEU H 144 N VAL H 119
SHEET 1 AA5 5 ALA B 95 ASP B 101 0
SHEET 2 AA5 5 VAL B 29 LYS B 36 -1 N VAL B 31 O ILE B 99
SHEET 3 AA5 5 GLN B 15 GLU B 21 -1 N ASN B 19 O TRP B 32
SHEET 4 AA5 5 LYS B 3 LEU B 8 -1 N LEU B 8 O GLY B 16
SHEET 5 AA5 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 AA6 4 ASP B 83 ALA B 89 0
SHEET 2 AA6 4 GLY B 41 HIS B 48 -1 N GLY B 41 O ALA B 89
SHEET 3 AA6 4 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 4 AA6 4 ARG B 143 VAL B 148 -1 O LEU B 144 N VAL B 119
SHEET 1 AA7 5 ALA C 95 ASP C 101 0
SHEET 2 AA7 5 VAL C 29 LYS C 36 -1 N VAL C 31 O ILE C 99
SHEET 3 AA7 5 GLN C 15 GLU C 21 -1 N ASN C 19 O TRP C 32
SHEET 4 AA7 5 LYS C 3 LEU C 8 -1 N CYS C 6 O ILE C 18
SHEET 5 AA7 5 GLY C 150 ILE C 151 -1 O GLY C 150 N VAL C 5
SHEET 1 AA8 4 ASP C 83 ALA C 89 0
SHEET 2 AA8 4 GLY C 41 HIS C 48 -1 N GLY C 41 O ALA C 89
SHEET 3 AA8 4 THR C 116 HIS C 120 -1 O VAL C 118 N HIS C 46
SHEET 4 AA8 4 ARG C 143 VAL C 148 -1 O ALA C 145 N VAL C 119
SHEET 1 AA9 5 ALA D 95 ASP D 101 0
SHEET 2 AA9 5 VAL D 29 LYS D 36 -1 N VAL D 29 O ASP D 101
SHEET 3 AA9 5 GLN D 15 GLU D 21 -1 N ASN D 19 O TRP D 32
SHEET 4 AA9 5 LYS D 3 LEU D 8 -1 N CYS D 6 O ILE D 18
SHEET 5 AA9 5 GLY D 150 ILE D 151 -1 O GLY D 150 N VAL D 5
SHEET 1 AB1 4 ASP D 83 ALA D 89 0
SHEET 2 AB1 4 GLY D 41 HIS D 48 -1 N GLY D 41 O ALA D 89
SHEET 3 AB1 4 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48
SHEET 4 AB1 4 ARG D 143 VAL D 148 -1 O GLY D 147 N LEU D 117
SHEET 1 AB2 5 ALA E 95 ASP E 101 0
SHEET 2 AB2 5 VAL E 29 LYS E 36 -1 N VAL E 31 O ILE E 99
SHEET 3 AB2 5 GLN E 15 GLU E 21 -1 N ASN E 19 O TRP E 32
SHEET 4 AB2 5 LYS E 3 LEU E 8 -1 N LEU E 8 O GLY E 16
SHEET 5 AB2 5 GLY E 150 ILE E 151 -1 O GLY E 150 N VAL E 5
SHEET 1 AB3 4 ASP E 83 ALA E 89 0
SHEET 2 AB3 4 GLY E 41 HIS E 48 -1 N GLY E 41 O ALA E 89
SHEET 3 AB3 4 THR E 116 HIS E 120 -1 O THR E 116 N HIS E 48
SHEET 4 AB3 4 ARG E 143 VAL E 148 -1 O GLY E 147 N LEU E 117
SHEET 1 AB4 5 ALA F 95 ASP F 101 0
SHEET 2 AB4 5 VAL F 29 LYS F 36 -1 N VAL F 29 O ASP F 101
SHEET 3 AB4 5 GLN F 15 GLU F 21 -1 N ASN F 19 O TRP F 32
SHEET 4 AB4 5 LYS F 3 LYS F 9 -1 N LEU F 8 O GLY F 16
SHEET 5 AB4 5 GLY F 150 ILE F 151 -1 O GLY F 150 N VAL F 5
SHEET 1 AB5 4 ASP F 83 ALA F 89 0
SHEET 2 AB5 4 GLY F 41 HIS F 48 -1 N GLY F 41 O ALA F 89
SHEET 3 AB5 4 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 4 AB5 4 ARG F 143 VAL F 148 -1 O LEU F 144 N VAL F 119
SHEET 1 AB6 5 ALA G 95 ASP G 101 0
SHEET 2 AB6 5 VAL G 29 LYS G 36 -1 N ILE G 35 O ALA G 95
SHEET 3 AB6 5 GLN G 15 GLU G 21 -1 N ASN G 19 O TRP G 32
SHEET 4 AB6 5 LYS G 3 LEU G 8 -1 N LEU G 8 O GLY G 16
SHEET 5 AB6 5 GLY G 150 ILE G 151 -1 O GLY G 150 N VAL G 5
SHEET 1 AB7 4 ASP G 83 ALA G 89 0
SHEET 2 AB7 4 GLY G 41 HIS G 48 -1 N GLY G 41 O ALA G 89
SHEET 3 AB7 4 THR G 116 HIS G 120 -1 O THR G 116 N HIS G 48
SHEET 4 AB7 4 ARG G 143 VAL G 148 -1 O GLY G 147 N LEU G 117
SHEET 1 AB8 5 ALA I 95 ASP I 101 0
SHEET 2 AB8 5 VAL I 29 LYS I 36 -1 N VAL I 31 O ILE I 99
SHEET 3 AB8 5 GLN I 15 GLU I 21 -1 N ASN I 19 O TRP I 32
SHEET 4 AB8 5 LYS I 3 LYS I 9 -1 N CYS I 6 O ILE I 18
SHEET 5 AB8 5 GLY I 150 ILE I 151 -1 O GLY I 150 N VAL I 5
SHEET 1 AB9 4 ASP I 83 ALA I 89 0
SHEET 2 AB9 4 GLY I 41 HIS I 48 -1 N GLY I 41 O ALA I 89
SHEET 3 AB9 4 THR I 116 HIS I 120 -1 O THR I 116 N HIS I 48
SHEET 4 AB9 4 ARG I 143 VAL I 148 -1 O ALA I 145 N VAL I 119
SHEET 1 AC1 5 ALA J 95 ASP J 101 0
SHEET 2 AC1 5 VAL J 29 LYS J 36 -1 N GLY J 33 O VAL J 97
SHEET 3 AC1 5 GLN J 15 GLU J 21 -1 N ASN J 19 O TRP J 32
SHEET 4 AC1 5 LYS J 3 LEU J 8 -1 N LEU J 8 O GLY J 16
SHEET 5 AC1 5 GLY J 150 ILE J 151 -1 O GLY J 150 N VAL J 5
SHEET 1 AC2 4 ASP J 83 ALA J 89 0
SHEET 2 AC2 4 GLY J 41 HIS J 48 -1 N HIS J 43 O VAL J 87
SHEET 3 AC2 4 THR J 116 HIS J 120 -1 O THR J 116 N HIS J 48
SHEET 4 AC2 4 ARG J 143 VAL J 148 -1 O GLY J 147 N LEU J 117
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.31
SSBOND 2 CYS H 57 CYS H 146 1555 1555 2.30
SSBOND 3 CYS B 57 CYS B 146 1555 1555 2.30
SSBOND 4 CYS C 57 CYS C 146 1555 1555 2.33
SSBOND 5 CYS D 57 CYS D 146 1555 1555 2.30
SSBOND 6 CYS E 57 CYS E 146 1555 1555 2.25
SSBOND 7 CYS F 57 CYS F 146 1555 1555 2.16
SSBOND 8 CYS G 57 CYS G 146 1555 1555 2.17
SSBOND 9 CYS I 57 CYS I 146 1555 1555 2.21
SSBOND 10 CYS J 57 CYS J 146 1555 1555 2.27
LINK SG CYS C 111 S4 S4P C 202 1555 1555 2.09
LINK SG CYS D 111 S4 S4P D 202 1555 1555 2.09
LINK S1 S4P D 202 SG CYS E 111 1555 1555 2.20
LINK ND1 HIS A 63 ZN ZN A 201 1555 1555 2.02
LINK ND1 HIS A 71 ZN ZN A 201 1555 1555 2.15
LINK ND1 HIS A 80 ZN ZN A 201 1555 1555 2.07
LINK OD1 ASP A 83 ZN ZN A 201 1555 1555 1.96
LINK ND1 HIS H 63 ZN ZN H 201 1555 1555 2.19
LINK ND1 HIS H 71 ZN ZN H 201 1555 1555 2.34
LINK ND1 HIS H 80 ZN ZN H 201 1555 1555 2.06
LINK OD1 ASP H 83 ZN ZN H 201 1555 1555 1.88
LINK ND1 HIS B 63 ZN ZN B 201 1555 1555 2.05
LINK ND1 HIS B 71 ZN ZN B 201 1555 1555 2.18
LINK ND1 HIS B 80 ZN ZN B 201 1555 1555 2.00
LINK OD1 ASP B 83 ZN ZN B 201 1555 1555 1.87
LINK ND1 HIS C 63 ZN ZN C 201 1555 1555 2.01
LINK ND1 HIS C 71 ZN ZN C 201 1555 1555 2.34
LINK ND1 HIS C 80 ZN ZN C 201 1555 1555 2.04
LINK OD1 ASP C 83 ZN ZN C 201 1555 1555 1.91
LINK ND1 HIS D 63 ZN ZN D 201 1555 1555 2.03
LINK ND1 HIS D 71 ZN ZN D 201 1555 1555 2.17
LINK ND1 HIS D 80 ZN ZN D 201 1555 1555 2.00
LINK OD2 ASP D 83 ZN ZN D 201 1555 1555 1.93
LINK ND1 HIS E 63 ZN ZN E 201 1555 1555 2.25
LINK ND1 HIS E 71 ZN ZN E 201 1555 1555 2.50
LINK ND1 HIS E 80 ZN ZN E 201 1555 1555 2.01
LINK OD1 ASP E 83 ZN ZN E 201 1555 1555 2.03
LINK ND1 HIS F 63 ZN ZN F 201 1555 1555 2.10
LINK ND1 HIS F 71 ZN ZN F 201 1555 1555 2.25
LINK ND1 HIS F 80 ZN ZN F 201 1555 1555 2.07
LINK OD1 ASP F 83 ZN ZN F 201 1555 1555 1.92
LINK ND1 HIS G 63 ZN ZN G 201 1555 1555 1.96
LINK ND1 HIS G 71 ZN ZN G 201 1555 1555 2.35
LINK ND1 HIS G 80 ZN ZN G 201 1555 1555 2.02
LINK OD1 ASP G 83 ZN ZN G 201 1555 1555 1.98
LINK ND1 HIS I 63 ZN ZN I 201 1555 1555 2.10
LINK ND1 HIS I 71 ZN ZN I 201 1555 1555 2.09
LINK ND1 HIS I 80 ZN ZN I 201 1555 1555 2.03
LINK OD1 ASP I 83 ZN ZN I 201 1555 1555 1.89
SITE 1 AC1 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC2 4 CYS A 111 ILE A 113 HOH A 473 CYS H 111
SITE 1 AC3 4 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 1 AC4 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 1 AC5 4 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 1 AC6 8 HIS C 48 HIS C 120 THR C 137 GLY C 141
SITE 2 AC6 8 ARG C 143 HOH C 314 HOH C 347 HOH C 421
SITE 1 AC7 4 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 1 AC8 4 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 1 AC9 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 AD1 4 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 1 AD2 4 HIS I 63 HIS I 71 HIS I 80 ASP I 83
SITE 1 AD3 2 CYS I 111 CYS J 111
SITE 1 AD4 11 CYS B 111 SER C 105 LEU C 106 SER C 107
SITE 2 AD4 11 GLY C 108 ASP C 109 HIS C 110 ILE C 112
SITE 3 AD4 11 ILE C 113 ARG C 115 HOH C 354
SITE 1 AD5 21 PHE D 64 SER D 105 LEU D 106 SER D 107
SITE 2 AD5 21 GLY D 108 ASP D 109 HIS D 110 ILE D 112
SITE 3 AD5 21 ILE D 113 ARG D 115 HOH D 339 SER E 105
SITE 4 AD5 21 SER E 107 GLY E 108 ASP E 109 HIS E 110
SITE 5 AD5 21 ILE E 112 ILE E 113 ARG E 115 HOH E 313
SITE 6 AD5 21 HOH E 320
SITE 1 AD6 12 PHE D 64 SER D 105 LEU D 106 SER D 107
SITE 2 AD6 12 GLY D 108 ASP D 109 HIS D 110 ILE D 112
SITE 3 AD6 12 ILE D 113 ARG D 115 HOH D 339 CYS E 111
CRYST1 242.634 242.634 144.113 90.00 90.00 120.00 P 63 2 2 120
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 0.004121 0.002380 0.000000 0.00000
SCALE2 0.000000 0.004759 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006939 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
