HEADER OXIDOREDUCTASE 23-JUL-98 1FUN
TITLE SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6
TITLE 2 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, F, B, G, C, H, D, I, E, J;
COMPND 4 SYNONYM: SOD;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: FIVE BIOLOGICAL DIMERS ARE PRESENT IN THE
COMPND 9 CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THEY ARE A AND F, B AND G, C AND H,
COMPND 10 D AND I, E AND J.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.LO,J.A.TAINER,E.D.GETZOFF
REVDAT 3 03-NOV-21 1FUN 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1FUN 1 VERSN
REVDAT 1 23-JUL-99 1FUN 0
JRNL AUTH C.L.FISHER,D.E.CABELLI,R.A.HALLEWELL,P.BEROZA,T.P.LO,
JRNL AUTH 2 E.D.GETZOFF,J.A.TAINER
JRNL TITL COMPUTATIONAL, PULSE-RADIOLYTIC, AND STRUCTURAL
JRNL TITL 2 INVESTIGATIONS OF LYSINE-136 AND ITS ROLE IN THE
JRNL TITL 3 ELECTROSTATIC TRIAD OF HUMAN CU,ZN SUPEROXIDE DISMUTASE.
JRNL REF PROTEINS V. 29 103 1997
JRNL REFN ISSN 0887-3585
JRNL PMID 9294870
JRNL DOI 10.1002/(SICI)1097-0134(199709)29:1<103::AID-PROT8>3.0.CO;2-
JRNL DOI 2 G
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 55654
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11090
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 239
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FUN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173425.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 72.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.75000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.75000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 83.50000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.75000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 83.50000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: 1640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 1330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 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: 1580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 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: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I
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: 1390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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 70.14 -150.54
REMARK 500 LYS A 75 40.77 -102.07
REMARK 500 LYS A 91 2.79 -68.88
REMARK 500 SER A 98 73.30 -151.58
REMARK 500 ASP A 125 27.54 -78.01
REMARK 500 LEU A 126 42.14 30.49
REMARK 500 SER F 25 -60.22 -20.03
REMARK 500 ASP F 90 -167.69 -72.33
REMARK 500 SER F 98 90.95 -165.28
REMARK 500 LYS F 128 31.85 -95.85
REMARK 500 THR F 135 32.91 -95.32
REMARK 500 GLU F 136 -42.09 -145.05
REMARK 500 ASP B 11 36.46 -78.28
REMARK 500 GLU B 40 130.78 -26.53
REMARK 500 CYS B 57 -16.06 -44.81
REMARK 500 SER B 68 53.55 33.55
REMARK 500 SER B 98 83.13 -169.33
REMARK 500 ASP B 125 21.58 -77.94
REMARK 500 LEU B 126 16.72 47.16
REMARK 500 GLU B 136 -71.31 -101.97
REMARK 500 SER G 25 7.93 -56.17
REMARK 500 ASN G 26 12.30 -166.65
REMARK 500 ALA G 55 43.69 -94.43
REMARK 500 PHE G 64 102.87 -52.89
REMARK 500 SER G 98 98.19 -162.72
REMARK 500 HIS G 110 38.44 -96.63
REMARK 500 ARG C 69 -162.79 -100.15
REMARK 500 HIS C 110 45.98 -106.15
REMARK 500 GLU C 136 -65.96 -106.99
REMARK 500 LYS H 23 -70.27 -66.13
REMARK 500 LYS H 128 38.34 -96.62
REMARK 500 LYS D 23 -73.37 -82.26
REMARK 500 SER D 25 1.15 -49.04
REMARK 500 ASN D 26 7.35 -155.15
REMARK 500 ALA D 55 40.66 -102.81
REMARK 500 ASN D 65 81.80 -150.99
REMARK 500 SER D 68 16.92 43.89
REMARK 500 GLU D 77 -78.29 -63.52
REMARK 500 ARG D 79 144.53 -177.22
REMARK 500 ASP D 125 47.83 -92.55
REMARK 500 LEU D 126 44.40 35.80
REMARK 500 LYS D 128 43.36 -80.80
REMARK 500 ALA I 60 0.31 -69.57
REMARK 500 SER I 68 48.41 32.61
REMARK 500 SER I 98 84.69 -158.42
REMARK 500 LYS E 75 33.57 -76.87
REMARK 500 ASP E 90 -170.60 -69.44
REMARK 500 SER E 98 92.57 -166.62
REMARK 500 HIS E 110 45.16 -101.64
REMARK 500 GLU E 136 -77.97 -103.89
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 CU A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 138.7
REMARK 620 3 HIS A 63 NE2 70.8 96.5
REMARK 620 4 HIS A 120 NE2 106.7 108.3 137.7
REMARK 620 N 1 2 3
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 71 ND1 109.9
REMARK 620 3 HIS A 80 ND1 118.1 107.6
REMARK 620 4 ASP A 83 OD1 107.2 95.2 116.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU F 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 46 ND1
REMARK 620 2 HIS F 48 NE2 140.6
REMARK 620 3 HIS F 120 NE2 106.0 103.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 63 ND1
REMARK 620 2 HIS F 71 ND1 124.7
REMARK 620 3 HIS F 80 ND1 95.5 123.4
REMARK 620 4 ASP F 83 OD1 91.3 115.4 99.5
REMARK 620 5 ASP F 83 OD2 153.6 71.8 89.3 62.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 48 NE2 145.7
REMARK 620 3 HIS B 63 NE2 69.9 94.6
REMARK 620 4 HIS B 120 NE2 102.3 108.3 140.7
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 71 ND1 111.3
REMARK 620 3 HIS B 80 ND1 104.4 124.8
REMARK 620 4 ASP B 83 OD1 105.6 94.7 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU G 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 46 ND1
REMARK 620 2 HIS G 48 NE2 143.4
REMARK 620 3 HIS G 63 NE2 70.0 100.2
REMARK 620 4 HIS G 120 NE2 104.7 102.5 144.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 63 ND1
REMARK 620 2 HIS G 71 ND1 117.3
REMARK 620 3 HIS G 80 ND1 106.2 112.7
REMARK 620 4 ASP G 83 OD1 98.6 112.8 108.0
REMARK 620 5 ASP G 83 OD2 150.2 72.1 94.1 53.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 46 ND1
REMARK 620 2 HIS C 48 NE2 145.0
REMARK 620 3 HIS C 63 NE2 75.9 93.9
REMARK 620 4 HIS C 120 NE2 96.7 109.9 143.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 63 ND1
REMARK 620 2 HIS C 71 ND1 115.2
REMARK 620 3 HIS C 80 ND1 113.2 121.1
REMARK 620 4 ASP C 83 OD1 93.0 95.7 113.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU H 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 46 ND1
REMARK 620 2 HIS H 48 NE2 138.0
REMARK 620 3 HIS H 63 NE2 71.0 100.8
REMARK 620 4 HIS H 120 NE2 97.3 108.2 146.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 63 ND1
REMARK 620 2 HIS H 71 ND1 114.7
REMARK 620 3 HIS H 80 ND1 111.4 123.7
REMARK 620 4 ASP H 83 OD2 150.0 71.1 84.7
REMARK 620 5 ASP H 83 OD1 100.1 101.3 100.8 50.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU D 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 46 ND1
REMARK 620 2 HIS D 48 NE2 164.6
REMARK 620 3 HIS D 63 NE2 72.6 102.0
REMARK 620 4 HIS D 120 NE2 93.1 101.2 129.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 63 ND1
REMARK 620 2 HIS D 71 ND1 141.4
REMARK 620 3 HIS D 80 ND1 107.8 107.1
REMARK 620 4 ASP D 83 OD1 94.4 97.3 96.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU I 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 46 ND1
REMARK 620 2 HIS I 48 NE2 149.6
REMARK 620 3 HIS I 120 NE2 89.7 113.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 63 ND1
REMARK 620 2 HIS I 71 ND1 120.5
REMARK 620 3 HIS I 80 ND1 105.2 122.6
REMARK 620 4 ASP I 83 OD1 102.1 106.3 95.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU E 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 46 ND1
REMARK 620 2 HIS E 48 NE2 133.4
REMARK 620 3 HIS E 120 NE2 104.9 119.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 63 ND1
REMARK 620 2 HIS E 71 ND1 126.3
REMARK 620 3 HIS E 80 ND1 93.6 111.0
REMARK 620 4 ASP E 83 OD2 164.9 63.0 93.3
REMARK 620 5 ASP E 83 OD1 110.4 100.8 115.7 54.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU J 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 46 ND1
REMARK 620 2 HIS J 48 NE2 126.1
REMARK 620 3 HIS J 63 NE2 84.7 107.5
REMARK 620 4 HIS J 120 NE2 100.9 98.9 142.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 63 ND1
REMARK 620 2 HIS J 71 ND1 118.5
REMARK 620 3 HIS J 80 ND1 112.4 114.0
REMARK 620 4 ASP J 83 OD1 114.6 98.8 95.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU 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 CU F 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 200
DBREF 1FUN A 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN F 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN B 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN G 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN C 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN H 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN D 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN I 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN E 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1FUN J 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 1FUN ALA A 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER A 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU A 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA F 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER F 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU F 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA B 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER B 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU B 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA G 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER G 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU G 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA C 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER C 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU C 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA H 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER H 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU H 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA D 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER D 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU D 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA I 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER I 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU I 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA E 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER E 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU E 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQADV 1FUN ALA J 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1FUN SER J 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1FUN GLU J 136 UNP P00441 LYS 136 ENGINEERED MUTATION
SEQRES 1 A 153 ALA THR LYS ALA VAL ALA 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 SER ILE ILE GLY ARG THR LEU
SEQRES 10 A 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 A 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 A 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 F 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 F 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 F 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 F 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 F 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 F 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 F 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 F 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 F 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 F 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 F 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 F 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 B 153 ALA THR LYS ALA VAL ALA 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 SER ILE ILE GLY ARG THR LEU
SEQRES 10 B 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 B 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 B 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 G 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 G 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 G 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 G 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 G 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 G 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 G 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 G 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 G 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 G 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 G 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 G 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 C 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 C 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 C 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 C 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 C 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 C 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 C 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 C 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 C 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 C 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 C 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 C 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 H 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 H 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 H 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 H 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 H 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 H 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 H 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 H 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 H 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 H 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 H 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 H 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 D 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 D 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 D 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 D 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 D 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 D 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 D 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 D 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 D 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 D 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 D 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 D 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 I 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 I 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 I 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 I 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 I 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 I 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 I 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 I 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 I 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 I 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 I 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 I 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 E 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 E 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 E 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 E 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 E 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 E 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 E 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 E 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 E 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 E 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 E 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 E 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 J 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 J 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 J 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 J 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 J 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 J 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 J 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 J 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 J 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 J 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 J 153 ASN GLU GLU SER THR GLU THR GLY ASN ALA GLY SER ARG
SEQRES 12 J 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET CU A 154 1
HET ZN A 155 1
HET CU F 154 1
HET ZN F 155 1
HET SO4 F 200 5
HET CU B 154 1
HET ZN B 155 1
HET CU G 154 1
HET ZN G 155 1
HET CU C 154 1
HET ZN C 155 1
HET CU H 154 1
HET ZN H 155 1
HET CU D 154 1
HET ZN D 155 1
HET CU I 154 1
HET ZN I 155 1
HET CU E 154 1
HET ZN E 155 1
HET CU J 154 1
HET ZN J 155 1
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 11 CU 10(CU 2+)
FORMUL 12 ZN 10(ZN 2+)
FORMUL 15 SO4 O4 S 2-
FORMUL 32 HOH *239(H2 O)
HELIX 1 1 THR A 58 ALA A 60 5 3
HELIX 2 2 SER A 134 THR A 137 1 4
HELIX 3 3 THR F 58 ALA F 60 5 3
HELIX 4 4 GLU F 133 THR F 135 5 3
HELIX 5 5 GLY B 56 ALA B 60 5 5
HELIX 6 6 GLU B 132 GLU B 136 1 5
HELIX 7 7 GLY G 56 ALA G 60 5 5
HELIX 8 8 GLU G 132 THR G 137 5 6
HELIX 9 9 GLY C 56 ALA C 60 5 5
HELIX 10 10 GLU C 132 GLU C 136 1 5
HELIX 11 11 GLY H 56 ALA H 60 5 5
HELIX 12 12 GLU H 132 THR H 135 5 4
HELIX 13 13 THR D 58 ALA D 60 5 3
HELIX 14 14 GLY D 108 HIS D 110 5 3
HELIX 15 15 GLU D 132 GLU D 136 1 5
HELIX 16 16 GLY I 56 ALA I 60 5 5
HELIX 17 17 GLU I 132 THR I 135 5 4
HELIX 18 18 THR E 58 ALA E 60 5 3
HELIX 19 19 GLU E 132 THR E 135 5 4
HELIX 20 20 THR J 58 ALA J 60 5 3
HELIX 21 21 GLU J 132 THR J 135 5 4
SHEET 1 A 4 LYS A 3 LEU A 8 0
SHEET 2 A 4 GLN A 15 GLU A 21 -1 N PHE A 20 O ALA A 4
SHEET 3 A 4 VAL A 29 LYS A 36 -1 N LYS A 36 O GLN A 15
SHEET 4 A 4 ALA A 95 ASP A 101 -1 N ASP A 101 O VAL A 29
SHEET 1 B 2 GLY A 41 GLY A 44 0
SHEET 2 B 2 ASN A 86 ALA A 89 -1 N ALA A 89 O GLY A 41
SHEET 1 C 3 PHE A 45 HIS A 48 0
SHEET 2 C 3 THR A 116 HIS A 120 -1 N VAL A 118 O HIS A 46
SHEET 3 C 3 ARG A 143 VAL A 148 -1 N GLY A 147 O LEU A 117
SHEET 1 D 5 ILE F 149 ILE F 151 0
SHEET 2 D 5 LYS F 3 LEU F 8 -1 N VAL F 5 O GLY F 150
SHEET 3 D 5 GLN F 15 GLN F 22 -1 N PHE F 20 O ALA F 4
SHEET 4 D 5 VAL F 29 LYS F 36 -1 N LYS F 36 O GLN F 15
SHEET 5 D 5 VAL F 94 ASP F 101 -1 N ASP F 101 O VAL F 29
SHEET 1 E 2 GLY F 41 GLY F 44 0
SHEET 2 E 2 ASN F 86 ALA F 89 -1 N ALA F 89 O GLY F 41
SHEET 1 F 3 PHE F 45 HIS F 48 0
SHEET 2 F 3 THR F 116 HIS F 120 -1 N VAL F 118 O HIS F 46
SHEET 3 F 3 ARG F 143 VAL F 148 -1 N GLY F 147 O LEU F 117
SHEET 1 G 4 LYS B 3 LEU B 8 0
SHEET 2 G 4 GLN B 15 GLU B 21 -1 N PHE B 20 O ALA B 4
SHEET 3 G 4 TRP B 32 LYS B 36 -1 N LYS B 36 O GLN B 15
SHEET 4 G 4 ALA B 95 SER B 98 -1 N VAL B 97 O GLY B 33
SHEET 1 H 2 GLY B 41 GLY B 44 0
SHEET 2 H 2 ASN B 86 ALA B 89 -1 N ALA B 89 O GLY B 41
SHEET 1 I 3 PHE B 45 VAL B 47 0
SHEET 2 I 3 THR B 116 HIS B 120 -1 N VAL B 118 O HIS B 46
SHEET 3 I 3 ARG B 143 VAL B 148 -1 N GLY B 147 O LEU B 117
SHEET 1 J 4 LYS G 3 LEU G 8 0
SHEET 2 J 4 GLN G 15 GLU G 21 -1 N PHE G 20 O ALA G 4
SHEET 3 J 4 VAL G 29 LYS G 36 -1 N LYS G 36 O GLN G 15
SHEET 4 J 4 ALA G 95 ASP G 101 -1 N ASP G 101 O VAL G 29
SHEET 1 K 2 GLY G 41 GLY G 44 0
SHEET 2 K 2 ASN G 86 ALA G 89 -1 N ALA G 89 O GLY G 41
SHEET 1 L 3 PHE G 45 HIS G 48 0
SHEET 2 L 3 THR G 116 HIS G 120 -1 N VAL G 118 O HIS G 46
SHEET 3 L 3 ARG G 143 VAL G 148 -1 N GLY G 147 O LEU G 117
SHEET 1 M 4 LYS C 3 LYS C 9 0
SHEET 2 M 4 GLN C 15 GLN C 22 -1 N PHE C 20 O ALA C 4
SHEET 3 M 4 VAL C 29 LYS C 36 -1 N LYS C 36 O GLN C 15
SHEET 4 M 4 SER C 98 ASP C 101 -1 N ASP C 101 O VAL C 29
SHEET 1 N 2 GLY C 41 GLY C 44 0
SHEET 2 N 2 ASN C 86 ALA C 89 -1 N ALA C 89 O GLY C 41
SHEET 1 O 3 PHE C 45 HIS C 48 0
SHEET 2 O 3 THR C 116 HIS C 120 -1 N VAL C 118 O HIS C 46
SHEET 3 O 3 ARG C 143 VAL C 148 -1 N GLY C 147 O LEU C 117
SHEET 1 P 5 ILE H 149 ILE H 151 0
SHEET 2 P 5 LYS H 3 LYS H 9 -1 N VAL H 5 O GLY H 150
SHEET 3 P 5 GLN H 15 GLU H 21 -1 N PHE H 20 O ALA H 4
SHEET 4 P 5 VAL H 29 LYS H 36 -1 N LYS H 36 O GLN H 15
SHEET 5 P 5 SER H 98 ASP H 101 -1 N ASP H 101 O VAL H 29
SHEET 1 Q 2 GLY H 41 GLY H 44 0
SHEET 2 Q 2 ASN H 86 ALA H 89 -1 N ALA H 89 O GLY H 41
SHEET 1 R 3 PHE H 45 HIS H 48 0
SHEET 2 R 3 THR H 116 HIS H 120 -1 N VAL H 118 O HIS H 46
SHEET 3 R 3 ARG H 143 VAL H 148 -1 N GLY H 147 O LEU H 117
SHEET 1 S 5 ILE D 149 ILE D 151 0
SHEET 2 S 5 LYS D 3 LYS D 9 -1 N VAL D 5 O GLY D 150
SHEET 3 S 5 GLN D 15 GLU D 21 -1 N PHE D 20 O ALA D 4
SHEET 4 S 5 VAL D 29 LYS D 36 -1 N LYS D 36 O GLN D 15
SHEET 5 S 5 ALA D 95 ASP D 101 -1 N ASP D 101 O VAL D 29
SHEET 1 T 2 GLY D 41 GLY D 44 0
SHEET 2 T 2 ASN D 86 ALA D 89 -1 N ALA D 89 O GLY D 41
SHEET 1 U 3 PHE D 45 HIS D 48 0
SHEET 2 U 3 THR D 116 HIS D 120 -1 N VAL D 118 O HIS D 46
SHEET 3 U 3 ARG D 143 VAL D 148 -1 N GLY D 147 O LEU D 117
SHEET 1 V 5 ILE I 149 ILE I 151 0
SHEET 2 V 5 LYS I 3 LEU I 8 -1 N VAL I 5 O GLY I 150
SHEET 3 V 5 GLN I 15 GLN I 22 -1 N PHE I 20 O ALA I 4
SHEET 4 V 5 VAL I 29 LYS I 36 -1 N LYS I 36 O GLN I 15
SHEET 5 V 5 VAL I 94 ASP I 101 -1 N ASP I 101 O VAL I 29
SHEET 1 W 2 GLY I 41 GLY I 44 0
SHEET 2 W 2 ASN I 86 ALA I 89 -1 N ALA I 89 O GLY I 41
SHEET 1 X 3 PHE I 45 HIS I 48 0
SHEET 2 X 3 THR I 116 HIS I 120 -1 N VAL I 118 O HIS I 46
SHEET 3 X 3 ARG I 143 VAL I 148 -1 N GLY I 147 O LEU I 117
SHEET 1 Y 4 LYS E 3 LEU E 8 0
SHEET 2 Y 4 GLN E 15 GLU E 21 -1 N PHE E 20 O ALA E 4
SHEET 3 Y 4 VAL E 29 LYS E 36 -1 N LYS E 36 O GLN E 15
SHEET 4 Y 4 ALA E 95 ASP E 101 -1 N ASP E 101 O VAL E 29
SHEET 1 Z 2 GLY E 41 GLY E 44 0
SHEET 2 Z 2 ASN E 86 ALA E 89 -1 N ALA E 89 O GLY E 41
SHEET 1 AA 3 PHE E 45 VAL E 47 0
SHEET 2 AA 3 THR E 116 HIS E 120 -1 N VAL E 118 O HIS E 46
SHEET 3 AA 3 ARG E 143 VAL E 148 -1 N GLY E 147 O LEU E 117
SHEET 1 AB 4 SER J 98 ASP J 101 0
SHEET 2 AB 4 VAL J 29 LYS J 36 -1 N VAL J 31 O ILE J 99
SHEET 3 AB 4 GLY J 12 GLU J 21 -1 N ASN J 19 O TRP J 32
SHEET 4 AB 4 LYS J 3 GLY J 10 -1 N GLY J 10 O GLY J 12
SHEET 1 AC 2 GLY J 41 GLY J 44 0
SHEET 2 AC 2 ASN J 86 ALA J 89 -1 N ALA J 89 O GLY J 41
SHEET 1 AD 3 PHE J 45 HIS J 48 0
SHEET 2 AD 3 THR J 116 HIS J 120 -1 N VAL J 118 O HIS J 46
SHEET 3 AD 3 ARG J 143 VAL J 148 -1 N GLY J 147 O LEU J 117
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.02
SSBOND 2 CYS F 57 CYS F 146 1555 1555 2.02
SSBOND 3 CYS B 57 CYS B 146 1555 1555 2.00
SSBOND 4 CYS G 57 CYS G 146 1555 1555 2.02
SSBOND 5 CYS C 57 CYS C 146 1555 1555 2.01
SSBOND 6 CYS H 57 CYS H 146 1555 1555 2.02
SSBOND 7 CYS D 57 CYS D 146 1555 1555 2.03
SSBOND 8 CYS I 57 CYS I 146 1555 1555 2.01
SSBOND 9 CYS E 57 CYS E 146 1555 1555 2.04
SSBOND 10 CYS J 57 CYS J 146 1555 1555 2.03
LINK ND1 HIS A 46 CU CU A 154 1555 1555 2.15
LINK NE2 HIS A 48 CU CU A 154 1555 1555 2.09
LINK NE2 HIS A 63 CU CU A 154 1555 1555 2.63
LINK ND1 HIS A 63 ZN ZN A 155 1555 1555 1.96
LINK ND1 HIS A 71 ZN ZN A 155 1555 1555 2.01
LINK ND1 HIS A 80 ZN ZN A 155 1555 1555 2.08
LINK OD1 ASP A 83 ZN ZN A 155 1555 1555 1.89
LINK NE2 HIS A 120 CU CU A 154 1555 1555 2.07
LINK ND1 HIS F 46 CU CU F 154 1555 1555 2.06
LINK NE2 HIS F 48 CU CU F 154 1555 1555 2.10
LINK ND1 HIS F 63 ZN ZN F 155 1555 1555 1.62
LINK ND1 HIS F 71 ZN ZN F 155 1555 1555 1.94
LINK ND1 HIS F 80 ZN ZN F 155 1555 1555 1.86
LINK OD1 ASP F 83 ZN ZN F 155 1555 1555 1.89
LINK OD2 ASP F 83 ZN ZN F 155 1555 1555 2.29
LINK NE2 HIS F 120 CU CU F 154 1555 1555 2.15
LINK ND1 HIS B 46 CU CU B 154 1555 1555 2.10
LINK NE2 HIS B 48 CU CU B 154 1555 1555 2.14
LINK NE2 HIS B 63 CU CU B 154 1555 1555 2.45
LINK ND1 HIS B 63 ZN ZN B 155 1555 1555 2.23
LINK ND1 HIS B 71 ZN ZN B 155 1555 1555 1.99
LINK ND1 HIS B 80 ZN ZN B 155 1555 1555 1.84
LINK OD1 ASP B 83 ZN ZN B 155 1555 1555 1.91
LINK NE2 HIS B 120 CU CU B 154 1555 1555 1.94
LINK ND1 HIS G 46 CU CU G 154 1555 1555 2.20
LINK NE2 HIS G 48 CU CU G 154 1555 1555 2.19
LINK NE2 HIS G 63 CU CU G 154 1555 1555 2.43
LINK ND1 HIS G 63 ZN ZN G 155 1555 1555 2.10
LINK ND1 HIS G 71 ZN ZN G 155 1555 1555 1.98
LINK ND1 HIS G 80 ZN ZN G 155 1555 1555 1.91
LINK OD1 ASP G 83 ZN ZN G 155 1555 1555 1.96
LINK OD2 ASP G 83 ZN ZN G 155 1555 1555 2.67
LINK NE2 HIS G 120 CU CU G 154 1555 1555 2.05
LINK ND1 HIS C 46 CU CU C 154 1555 1555 1.93
LINK NE2 HIS C 48 CU CU C 154 1555 1555 2.11
LINK NE2 HIS C 63 CU CU C 154 1555 1555 2.42
LINK ND1 HIS C 63 ZN ZN C 155 1555 1555 1.99
LINK ND1 HIS C 71 ZN ZN C 155 1555 1555 2.03
LINK ND1 HIS C 80 ZN ZN C 155 1555 1555 1.90
LINK OD1 ASP C 83 ZN ZN C 155 1555 1555 1.91
LINK NE2 HIS C 120 CU CU C 154 1555 1555 1.95
LINK ND1 HIS H 46 CU CU H 154 1555 1555 1.96
LINK NE2 HIS H 48 CU CU H 154 1555 1555 2.12
LINK NE2 HIS H 63 CU CU H 154 1555 1555 2.50
LINK ND1 HIS H 63 ZN ZN H 155 1555 1555 1.97
LINK ND1 HIS H 71 ZN ZN H 155 1555 1555 1.95
LINK ND1 HIS H 80 ZN ZN H 155 1555 1555 1.94
LINK OD2 ASP H 83 ZN ZN H 155 1555 1555 2.77
LINK OD1 ASP H 83 ZN ZN H 155 1555 1555 1.93
LINK NE2 HIS H 120 CU CU H 154 1555 1555 2.00
LINK ND1 HIS D 46 CU CU D 154 1555 1555 2.32
LINK NE2 HIS D 48 CU CU D 154 1555 1555 2.20
LINK NE2 HIS D 63 CU CU D 154 1555 1555 2.56
LINK ND1 HIS D 63 ZN ZN D 155 1555 1555 2.05
LINK ND1 HIS D 71 ZN ZN D 155 1555 1555 2.09
LINK ND1 HIS D 80 ZN ZN D 155 1555 1555 2.23
LINK OD1 ASP D 83 ZN ZN D 155 1555 1555 2.23
LINK NE2 HIS D 120 CU CU D 154 1555 1555 2.00
LINK ND1 HIS I 46 CU CU I 154 1555 1555 1.86
LINK NE2 HIS I 48 CU CU I 154 1555 1555 1.92
LINK ND1 HIS I 63 ZN ZN I 155 1555 1555 1.85
LINK ND1 HIS I 71 ZN ZN I 155 1555 1555 1.82
LINK ND1 HIS I 80 ZN ZN I 155 1555 1555 1.70
LINK OD1 ASP I 83 ZN ZN I 155 1555 1555 1.81
LINK NE2 HIS I 120 CU CU I 154 1555 1555 2.04
LINK ND1 HIS E 46 CU CU E 154 1555 1555 2.33
LINK NE2 HIS E 48 CU CU E 154 1555 1555 2.38
LINK ND1 HIS E 63 ZN ZN E 155 1555 1555 2.24
LINK ND1 HIS E 71 ZN ZN E 155 1555 1555 2.50
LINK ND1 HIS E 80 ZN ZN E 155 1555 1555 2.17
LINK OD2 ASP E 83 ZN ZN E 155 1555 1555 2.59
LINK OD1 ASP E 83 ZN ZN E 155 1555 1555 2.13
LINK NE2 HIS E 120 CU CU E 154 1555 1555 1.90
LINK ND1 HIS J 46 CU CU J 154 1555 1555 2.07
LINK NE2 HIS J 48 CU CU J 154 1555 1555 2.35
LINK NE2 HIS J 63 CU CU J 154 1555 1555 2.34
LINK ND1 HIS J 63 ZN ZN J 155 1555 1555 2.27
LINK ND1 HIS J 71 ZN ZN J 155 1555 1555 2.08
LINK ND1 HIS J 80 ZN ZN J 155 1555 1555 1.97
LINK OD1 ASP J 83 ZN ZN J 155 1555 1555 2.04
LINK NE2 HIS J 120 CU CU J 154 1555 1555 2.05
SITE 1 AC1 4 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 1 AC2 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC3 4 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 1 AC4 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 AC5 4 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 1 AC6 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 1 AC7 4 HIS G 46 HIS G 48 HIS G 63 HIS G 120
SITE 1 AC8 4 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 1 AC9 4 HIS C 46 HIS C 48 HIS C 63 HIS C 120
SITE 1 BC1 4 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 1 BC2 4 HIS H 46 HIS H 48 HIS H 63 HIS H 120
SITE 1 BC3 4 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 1 BC4 4 HIS D 46 HIS D 48 HIS D 63 HIS D 120
SITE 1 BC5 4 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 1 BC6 4 HIS I 46 HIS I 48 HIS I 63 HIS I 120
SITE 1 BC7 4 HIS I 63 HIS I 71 HIS I 80 ASP I 83
SITE 1 BC8 4 HIS E 46 HIS E 48 HIS E 63 HIS E 120
SITE 1 BC9 4 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 1 CC1 4 HIS J 46 HIS J 48 HIS J 63 HIS J 120
SITE 1 CC2 4 HIS J 63 HIS J 71 HIS J 80 ASP J 83
SITE 1 CC3 4 LYS F 75 LYS F 128 LYS G 128 LYS H 128
CRYST1 205.200 167.000 145.500 90.00 90.00 90.00 C 2 2 21 80
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 0.004873 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006873 0.00000
(ATOM LINES ARE NOT SHOWN.)
END