HEADER OXIDOREDUCTASE 16-OCT-02 1N18
TITLE THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,
TITLE 2 C111S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GREEK KEY BETA BARREL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.F.CARDOSO,M.M.THAYER,M.DIDONATO,T.P.LO,C.K.BRUNS,
AUTHOR 2 E.D.GETZOFF,J.A.TAINER
REVDAT 2 24-FEB-09 1N18 1 VERSN
REVDAT 1 27-NOV-02 1N18 0
JRNL AUTH R.M.F.CARDOSO,M.M.THAYER,M.DIDONATO,T.P.LO,
JRNL AUTH 2 C.K.BRUNS,E.D.GETZOFF,J.A.TAINER
JRNL TITL INSIGHTS INTO LOU GEHRIG'S DISEASE FROM THE
JRNL TITL 2 STRUCTURE AND INSTABILITY OF THE A4V MUTANT OF
JRNL TITL 3 HUMAN CU,ZN SUPEROXIDE DISMUTASE.
JRNL REF J.MOL.BIOL. V. 324 247 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12441104
JRNL DOI 10.1016/S0022-2836(02)01090-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.E.PARGE,R.A.HALLEWELL,J.A.TAINER
REMARK 1 TITL ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE
REMARK 1 TITL 2 MUTANT RECOMBINANT HUMAN CU,ZN SUPEROXIDE DISMUTASE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 6109 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.86
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) (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 161466
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 SET) : 0.218
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8091
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 25418
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1301
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
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 : 1389
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 5.25000
REMARK 3 B33 (A**2) : -5.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.68
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.160 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.140 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 51.86
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N18 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-02.
REMARK 100 THE RCSB ID CODE IS RCSB017391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 : SI (111)
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 162732
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41600
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, NACL, TRIS, EDTA,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 72.15000
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 72.15000
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 101.60000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.60000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 101.60000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.60000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.15000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 101.60000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.60000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.15000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 101.60000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.60000
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: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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
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: 14040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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: 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: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 A 0
REMARK 465 MET B 0
REMARK 465 MET C 0
REMARK 465 MET D 0
REMARK 465 MET E 0
REMARK 465 MET F 0
REMARK 465 MET G 0
REMARK 465 MET H 0
REMARK 465 MET I 0
REMARK 465 MET J 0
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ALA A 1 N CA CB
REMARK 480 LYS A 9 CD
REMARK 480 LYS A 91 CE NZ
REMARK 480 GLU A 132 CD OE1 OE2
REMARK 480 LYS A 136 CD
REMARK 480 ALA B 1 N CA CB
REMARK 480 LYS B 23 NZ
REMARK 480 LYS B 91 NZ
REMARK 480 ALA C 1 N CA CB
REMARK 480 LYS C 23 CD CE NZ
REMARK 480 LYS C 30 CD
REMARK 480 LYS C 36 CD
REMARK 480 ARG C 69 CB CG
REMARK 480 ASP C 76 CG OD1 OD2
REMARK 480 ARG C 79 CB
REMARK 480 LYS C 91 CD CE NZ
REMARK 480 LYS C 122 CE NZ
REMARK 480 LYS C 136 CE NZ
REMARK 480 ALA D 1 N CA CB
REMARK 480 LYS D 23 CD CE NZ
REMARK 480 LYS D 36 NZ
REMARK 480 LYS D 70 CE NZ
REMARK 480 LYS D 136 CE NZ
REMARK 480 ALA E 1 N CA CB
REMARK 480 LYS E 3 NZ
REMARK 480 LYS E 23 CG CD CE
REMARK 480 LYS E 91 NZ
REMARK 480 LYS E 136 CE
REMARK 480 ALA F 1 N CA CB
REMARK 480 LYS F 36 NZ
REMARK 480 LYS F 70 NZ
REMARK 480 GLU F 77 CD OE1 OE2
REMARK 480 ALA G 1 N CA CB
REMARK 480 LYS G 3 CD
REMARK 480 LYS G 23 CB CG CD CE NZ
REMARK 480 GLU G 24 CD OE1 OE2
REMARK 480 ASN G 26 CB
REMARK 480 LYS G 30 CD CE
REMARK 480 ASN G 65 CA CB
REMARK 480 LEU G 67 CG CD1 CD2
REMARK 480 LYS G 75 CD
REMARK 480 GLU G 77 CB CG CD OE1 OE2
REMARK 480 LYS G 91 CG CE NZ
REMARK 480 SER G 98 OG
REMARK 480 LYS G 122 CE NZ
REMARK 480 GLU G 132 CD OE1 OE2
REMARK 480 LYS H 9 CE
REMARK 480 LYS H 23 CE NZ
REMARK 480 LYS H 91 CD CE
REMARK 480 ASP H 109 CB CG OD1
REMARK 480 LYS H 122 CE NZ
REMARK 480 ALA I 1 N CA CB
REMARK 480 LYS I 9 CD
REMARK 480 ASN I 26 CB CG OD1 ND2
REMARK 480 LYS I 70 CD
REMARK 480 GLU I 77 CG
REMARK 480 LYS I 91 CD CE NZ
REMARK 480 ALA J 1 N CA CB
REMARK 480 LYS J 9 CE
REMARK 480 LYS J 23 CE NZ
REMARK 480 GLU J 24 CG CD OE1 OE2
REMARK 480 SER J 25 O OG
REMARK 480 ASN J 26 CB CG OD1 ND2
REMARK 480 LYS J 36 NZ
REMARK 480 LYS J 70 CD
REMARK 480 LYS J 75 CD CE NZ
REMARK 480 ASP J 109 CB
REMARK 480 GLU J 132 CG
REMARK 480 LYS J 136 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 OD1 ASP C 76 O HOH C 243 2.07
REMARK 500 O HOH A 213 O HOH A 284 2.16
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 D 1567 O HOH D 1567 4555 1.44
REMARK 500 NZ LYS F 36 O ASP G 92 3655 2.10
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 SER B 25 -0.92 -43.96
REMARK 500 ASN B 26 -16.35 -147.05
REMARK 500 THR E 2 -36.97 -147.92
REMARK 500 ASP E 109 -35.82 -37.56
REMARK 500 LYS E 136 -56.52 -120.11
REMARK 500 SER G 98 94.78 -160.54
REMARK 500 ALA I 55 66.32 -115.98
REMARK 500 LEU I 126 19.51 59.82
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 CU1 A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 141.4
REMARK 620 3 HIS A 120 NE2 102.2 116.3
REMARK 620 N 1 2
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 ASP A 83 OD1
REMARK 620 2 HIS A 71 ND1 91.0
REMARK 620 3 HIS A 80 ND1 117.9 121.2
REMARK 620 4 HIS A 63 ND1 101.7 107.9 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 B 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 48 NE2
REMARK 620 2 HIS B 46 ND1 140.8
REMARK 620 3 HIS B 120 NE2 119.9 99.3
REMARK 620 N 1 2
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 106.8
REMARK 620 3 HIS B 80 ND1 108.8 122.3
REMARK 620 4 ASP B 83 OD1 104.6 97.0 115.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 C 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 48 NE2
REMARK 620 2 HIS C 63 NE2 88.0
REMARK 620 3 HIS C 120 NE2 116.7 113.5
REMARK 620 4 HIS C 46 ND1 144.8 72.8 98.1
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 80 ND1
REMARK 620 2 HIS C 63 ND1 108.0
REMARK 620 3 ASP C 83 OD1 122.6 109.8
REMARK 620 4 HIS C 71 ND1 114.7 101.7 97.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 D 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 46 ND1
REMARK 620 2 HIS D 120 NE2 97.2
REMARK 620 3 HIS D 48 NE2 145.7 115.9
REMARK 620 N 1 2
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 ASP D 83 OD1
REMARK 620 2 HIS D 80 ND1 115.8
REMARK 620 3 HIS D 71 ND1 99.8 121.8
REMARK 620 4 HIS D 63 ND1 102.1 109.2 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 E 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 120 NE2
REMARK 620 2 HIS E 48 NE2 117.2
REMARK 620 3 HIS E 46 ND1 100.0 142.7
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 71 ND1
REMARK 620 2 HIS E 80 ND1 122.1
REMARK 620 3 HIS E 63 ND1 105.3 112.1
REMARK 620 4 ASP E 83 OD1 90.9 116.0 108.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 F 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 46 ND1
REMARK 620 2 HIS F 120 NE2 97.3
REMARK 620 3 HIS F 48 NE2 143.8 118.8
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 ASP F 83 OD1
REMARK 620 2 HIS F 63 ND1 103.6
REMARK 620 3 HIS F 80 ND1 119.4 109.2
REMARK 620 4 HIS F 71 ND1 94.9 104.2 123.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 G 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 120 NE2
REMARK 620 2 HIS G 48 NE2 116.0
REMARK 620 3 HIS G 46 ND1 97.8 145.7
REMARK 620 N 1 2
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 80 ND1
REMARK 620 2 HIS G 71 ND1 125.8
REMARK 620 3 ASP G 83 OD1 123.1 87.1
REMARK 620 4 HIS G 63 ND1 110.4 100.7 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 H 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 120 NE2
REMARK 620 2 HIS H 48 NE2 120.4
REMARK 620 3 HIS H 46 ND1 96.7 142.6
REMARK 620 N 1 2
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 71 ND1
REMARK 620 2 ASP H 83 OD1 100.0
REMARK 620 3 HIS H 80 ND1 127.8 114.2
REMARK 620 4 HIS H 63 ND1 102.9 108.7 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 I 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 120 NE2
REMARK 620 2 HIS I 48 NE2 118.8
REMARK 620 3 HIS I 46 ND1 100.3 140.7
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 112.5
REMARK 620 3 HIS I 80 ND1 105.2 122.7
REMARK 620 4 ASP I 83 OD1 109.5 98.5 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 J 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 46 ND1
REMARK 620 2 HIS J 120 NE2 92.3
REMARK 620 3 HIS J 48 NE2 148.6 118.9
REMARK 620 N 1 2
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 80 ND1
REMARK 620 2 ASP J 83 OD1 118.6
REMARK 620 3 HIS J 63 ND1 109.1 104.9
REMARK 620 4 HIS J 71 ND1 119.3 96.7 106.5
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 CU1 A 154
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 154
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 C 154
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 D 154
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 E 154
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 F 154
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 G 154
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 H 154
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 I 154
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 J 154
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M19 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT
DBREF 1N18 A 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 B 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 C 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 D 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 E 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 F 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 G 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 H 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 I 0 153 UNP P00441 SODC_HUMAN 0 153
DBREF 1N18 J 0 153 UNP P00441 SODC_HUMAN 0 153
SEQADV 1N18 ALA A 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER A 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA B 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER B 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA C 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER C 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA D 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER D 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA E 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER E 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA F 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER F 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA G 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER G 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA H 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER H 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA I 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER I 111 UNP P00441 CYS 111 ENGINEERED
SEQADV 1N18 ALA J 6 UNP P00441 CYS 6 ENGINEERED
SEQADV 1N18 SER J 111 UNP P00441 CYS 111 ENGINEERED
SEQRES 1 A 154 MET ALA THR LYS ALA VAL ALA 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 SER 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 MET ALA THR LYS ALA VAL ALA 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 SER 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 ALA 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 SER 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 ALA 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 SER 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 ALA 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 SER 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 ALA 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 SER 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 ALA 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 SER 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 H 154 MET ALA THR LYS ALA VAL ALA 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 SER 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 I 154 MET ALA THR LYS ALA VAL ALA 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 SER 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 ALA 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 SER 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 CU1 A 154 1
HET ZN A 155 1
HET CU1 B 154 1
HET ZN B 155 1
HET CU1 C 154 1
HET ZN C 155 1
HET CU1 D 154 1
HET ZN D 155 1
HET CU1 E 154 1
HET ZN E 155 1
HET CU1 F 154 1
HET ZN F 155 1
HET CU1 G 154 1
HET ZN G 155 1
HET CU1 H 154 1
HET ZN H 155 1
HET CU1 I 154 1
HET ZN I 155 1
HET CU1 J 154 1
HET ZN J 155 1
HET SO4 D1400 5
HETNAM CU1 COPPER (I) ION
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 11 CU1 10(CU 1+)
FORMUL 12 ZN 10(ZN 2+)
FORMUL 31 SO4 O4 S 2-
FORMUL 32 HOH *1389(H2 O)
HELIX 1 1 ALA A 55 GLY A 61 5 7
HELIX 2 2 ASN A 131 THR A 135 5 5
HELIX 3 3 ALA B 55 GLY B 61 5 7
HELIX 4 4 ALA C 55 GLY C 61 5 7
HELIX 5 5 ASN C 131 THR C 137 1 7
HELIX 6 6 CYS D 57 GLY D 61 5 5
HELIX 7 7 GLU D 132 LYS D 136 5 5
HELIX 8 8 ALA E 55 GLY E 61 5 7
HELIX 9 9 GLU E 132 LYS E 136 5 5
HELIX 10 10 ALA F 55 GLY F 61 5 7
HELIX 11 11 ASN F 131 THR F 135 5 5
HELIX 12 12 CYS G 57 GLY G 61 5 5
HELIX 13 13 CYS H 57 GLY H 61 5 5
HELIX 14 14 GLU H 132 LYS H 136 5 5
HELIX 15 15 ALA I 55 GLY I 61 5 7
HELIX 16 16 GLU I 132 LYS I 136 5 5
HELIX 17 17 ALA J 55 GLY J 61 5 7
HELIX 18 18 SER J 107 SER J 111 5 5
HELIX 19 19 GLU J 132 LYS J 136 5 5
SHEET 1 A 5 ALA A 95 ASP A 101 0
SHEET 2 A 5 VAL A 29 LYS A 36 -1 N VAL A 31 O ILE A 99
SHEET 3 A 5 GLN A 15 GLN A 22 -1 N ASN A 19 O TRP A 32
SHEET 4 A 5 LYS A 3 LEU A 8 -1 N ALA A 4 O PHE A 20
SHEET 5 A 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 B 4 ASP A 83 ALA A 89 0
SHEET 2 B 4 GLY A 41 HIS A 48 -1 N GLY A 41 O ALA A 89
SHEET 3 B 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 4 B 4 ARG A 143 VAL A 148 -1 O GLY A 147 N LEU A 117
SHEET 1 C 5 ALA B 95 ASP B 101 0
SHEET 2 C 5 VAL B 29 LYS B 36 -1 N VAL B 31 O ILE B 99
SHEET 3 C 5 GLN B 15 GLU B 21 -1 N ASN B 19 O TRP B 32
SHEET 4 C 5 LYS B 3 LYS B 9 -1 N LEU B 8 O GLY B 16
SHEET 5 C 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 D 4 ASP B 83 ALA B 89 0
SHEET 2 D 4 GLY B 41 HIS B 48 -1 N GLY B 41 O ALA B 89
SHEET 3 D 4 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 4 D 4 ARG B 143 VAL B 148 -1 O GLY B 147 N LEU B 117
SHEET 1 E 5 ALA C 95 ASP C 101 0
SHEET 2 E 5 VAL C 29 LYS C 36 -1 N VAL C 31 O ILE C 99
SHEET 3 E 5 GLN C 15 GLU C 21 -1 N ASN C 19 O TRP C 32
SHEET 4 E 5 LYS C 3 LEU C 8 -1 N ALA C 6 O ILE C 18
SHEET 5 E 5 GLY C 150 ILE C 151 -1 O GLY C 150 N VAL C 5
SHEET 1 F 4 ASP C 83 ALA C 89 0
SHEET 2 F 4 GLY C 41 HIS C 48 -1 N GLY C 41 O ALA C 89
SHEET 3 F 4 THR C 116 HIS C 120 -1 O THR C 116 N HIS C 48
SHEET 4 F 4 ARG C 143 VAL C 148 -1 O GLY C 147 N LEU C 117
SHEET 1 G 5 ALA D 95 ASP D 101 0
SHEET 2 G 5 VAL D 29 LYS D 36 -1 N VAL D 29 O ASP D 101
SHEET 3 G 5 GLN D 15 GLU D 21 -1 N ASN D 19 O TRP D 32
SHEET 4 G 5 LYS D 3 LEU D 8 -1 N ALA D 4 O PHE D 20
SHEET 5 G 5 GLY D 150 ILE D 151 -1 O GLY D 150 N VAL D 5
SHEET 1 H 4 ASP D 83 ALA D 89 0
SHEET 2 H 4 GLY D 41 HIS D 48 -1 N GLY D 41 O ALA D 89
SHEET 3 H 4 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48
SHEET 4 H 4 ARG D 143 VAL D 148 -1 O GLY D 147 N LEU D 117
SHEET 1 I 5 ALA E 95 ASP E 101 0
SHEET 2 I 5 VAL E 29 LYS E 36 -1 N VAL E 31 O ILE E 99
SHEET 3 I 5 GLN E 15 GLU E 21 -1 N ASN E 19 O TRP E 32
SHEET 4 I 5 LYS E 3 LEU E 8 -1 N LEU E 8 O GLY E 16
SHEET 5 I 5 GLY E 150 ILE E 151 -1 O GLY E 150 N VAL E 5
SHEET 1 J 4 ASP E 83 ALA E 89 0
SHEET 2 J 4 GLY E 41 HIS E 48 -1 N GLY E 41 O ALA E 89
SHEET 3 J 4 THR E 116 HIS E 120 -1 O THR E 116 N HIS E 48
SHEET 4 J 4 ARG E 143 VAL E 148 -1 O GLY E 147 N LEU E 117
SHEET 1 K 5 ALA F 95 ASP F 101 0
SHEET 2 K 5 VAL F 29 LYS F 36 -1 N VAL F 31 O ILE F 99
SHEET 3 K 5 GLN F 15 GLU F 21 -1 N ASN F 19 O TRP F 32
SHEET 4 K 5 LYS F 3 LEU F 8 -1 N ALA F 6 O ILE F 18
SHEET 5 K 5 GLY F 150 ILE F 151 -1 O GLY F 150 N VAL F 5
SHEET 1 L 4 ASP F 83 ALA F 89 0
SHEET 2 L 4 GLY F 41 HIS F 48 -1 N GLY F 41 O ALA F 89
SHEET 3 L 4 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 4 L 4 ARG F 143 VAL F 148 -1 O GLY F 147 N LEU F 117
SHEET 1 M 5 ALA G 95 ASP G 101 0
SHEET 2 M 5 VAL G 29 LYS G 36 -1 N VAL G 31 O ILE G 99
SHEET 3 M 5 GLN G 15 GLU G 21 -1 N ASN G 19 O TRP G 32
SHEET 4 M 5 LYS G 3 LEU G 8 -1 N LEU G 8 O GLY G 16
SHEET 5 M 5 GLY G 150 ALA G 152 -1 O GLY G 150 N VAL G 5
SHEET 1 N 4 ASP G 83 ALA G 89 0
SHEET 2 N 4 GLY G 41 HIS G 48 -1 N GLY G 41 O ALA G 89
SHEET 3 N 4 THR G 116 HIS G 120 -1 O THR G 116 N HIS G 48
SHEET 4 N 4 ARG G 143 VAL G 148 -1 O ALA G 145 N VAL G 119
SHEET 1 O 5 ALA H 95 ASP H 101 0
SHEET 2 O 5 VAL H 29 LYS H 36 -1 N ILE H 35 O ALA H 95
SHEET 3 O 5 GLN H 15 GLU H 21 -1 N ASN H 19 O TRP H 32
SHEET 4 O 5 LYS H 3 LEU H 8 -1 N LEU H 8 O GLY H 16
SHEET 5 O 5 GLY H 150 GLN H 153 -1 O ALA H 152 N LYS H 3
SHEET 1 P 4 ASP H 83 ALA H 89 0
SHEET 2 P 4 GLY H 41 HIS H 48 -1 N GLY H 41 O ALA H 89
SHEET 3 P 4 THR H 116 HIS H 120 -1 O THR H 116 N HIS H 48
SHEET 4 P 4 ARG H 143 VAL H 148 -1 O GLY H 147 N LEU H 117
SHEET 1 Q 5 ALA I 95 ASP I 101 0
SHEET 2 Q 5 VAL I 29 LYS I 36 -1 N VAL I 31 O ILE I 99
SHEET 3 Q 5 GLN I 15 GLN I 22 -1 N ASN I 19 O TRP I 32
SHEET 4 Q 5 LYS I 3 LEU I 8 -1 N ALA I 4 O PHE I 20
SHEET 5 Q 5 GLY I 150 ALA I 152 -1 O GLY I 150 N VAL I 5
SHEET 1 R 4 ASP I 83 ALA I 89 0
SHEET 2 R 4 GLY I 41 HIS I 48 -1 N GLY I 41 O ALA I 89
SHEET 3 R 4 THR I 116 HIS I 120 -1 O THR I 116 N HIS I 48
SHEET 4 R 4 ARG I 143 VAL I 148 -1 O GLY I 147 N LEU I 117
SHEET 1 S 5 ALA J 95 ASP J 101 0
SHEET 2 S 5 VAL J 29 LYS J 36 -1 N VAL J 31 O ILE J 99
SHEET 3 S 5 GLN J 15 GLU J 21 -1 N ASN J 19 O TRP J 32
SHEET 4 S 5 LYS J 3 LEU J 8 -1 N ALA J 4 O PHE J 20
SHEET 5 S 5 GLY J 150 ILE J 151 -1 O GLY J 150 N VAL J 5
SHEET 1 T 4 ASP J 83 ALA J 89 0
SHEET 2 T 4 GLY J 41 HIS J 48 -1 N GLY J 41 O ALA J 89
SHEET 3 T 4 THR J 116 HIS J 120 -1 O THR J 116 N HIS J 48
SHEET 4 T 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 2.05
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.04
SSBOND 3 CYS C 57 CYS C 146 1555 1555 2.04
SSBOND 4 CYS D 57 CYS D 146 1555 1555 2.04
SSBOND 5 CYS E 57 CYS E 146 1555 1555 2.04
SSBOND 6 CYS F 57 CYS F 146 1555 1555 2.04
SSBOND 7 CYS G 57 CYS G 146 1555 1555 2.04
SSBOND 8 CYS H 57 CYS H 146 1555 1555 2.04
SSBOND 9 CYS I 57 CYS I 146 1555 1555 2.04
SSBOND 10 CYS J 57 CYS J 146 1555 1555 2.03
LINK CU CU1 A 154 ND1 HIS A 46 1555 1555 2.15
LINK CU CU1 A 154 NE2 HIS A 48 1555 1555 2.14
LINK CU CU1 A 154 NE2 HIS A 120 1555 1555 2.12
LINK ZN ZN A 155 OD1 ASP A 83 1555 1555 1.90
LINK ZN ZN A 155 ND1 HIS A 71 1555 1555 2.04
LINK ZN ZN A 155 ND1 HIS A 80 1555 1555 2.06
LINK ZN ZN A 155 ND1 HIS A 63 1555 1555 2.01
LINK CU CU1 B 154 NE2 HIS B 48 1555 1555 2.02
LINK CU CU1 B 154 ND1 HIS B 46 1555 1555 2.04
LINK CU CU1 B 154 NE2 HIS B 120 1555 1555 2.02
LINK ZN ZN B 155 ND1 HIS B 63 1555 1555 2.00
LINK ZN ZN B 155 ND1 HIS B 71 1555 1555 2.02
LINK ZN ZN B 155 ND1 HIS B 80 1555 1555 2.13
LINK ZN ZN B 155 OD1 ASP B 83 1555 1555 1.96
LINK CU CU1 C 154 NE2 HIS C 48 1555 1555 2.11
LINK CU CU1 C 154 NE2 HIS C 63 1555 1555 2.66
LINK CU CU1 C 154 NE2 HIS C 120 1555 1555 2.06
LINK CU CU1 C 154 ND1 HIS C 46 1555 1555 2.17
LINK ZN ZN C 155 ND1 HIS C 80 1555 1555 2.07
LINK ZN ZN C 155 ND1 HIS C 63 1555 1555 2.36
LINK ZN ZN C 155 OD1 ASP C 83 1555 1555 1.81
LINK ZN ZN C 155 ND1 HIS C 71 1555 1555 2.05
LINK CU CU1 D 154 ND1 HIS D 46 1555 1555 2.15
LINK CU CU1 D 154 NE2 HIS D 120 1555 1555 2.01
LINK CU CU1 D 154 NE2 HIS D 48 1555 1555 2.04
LINK ZN ZN D 155 OD1 ASP D 83 1555 1555 1.94
LINK ZN ZN D 155 ND1 HIS D 80 1555 1555 2.04
LINK ZN ZN D 155 ND1 HIS D 71 1555 1555 2.00
LINK ZN ZN D 155 ND1 HIS D 63 1555 1555 1.95
LINK CU CU1 E 154 NE2 HIS E 120 1555 1555 1.97
LINK CU CU1 E 154 NE2 HIS E 48 1555 1555 2.09
LINK CU CU1 E 154 ND1 HIS E 46 1555 1555 2.13
LINK ZN ZN E 155 ND1 HIS E 71 1555 1555 2.10
LINK ZN ZN E 155 ND1 HIS E 80 1555 1555 1.98
LINK ZN ZN E 155 ND1 HIS E 63 1555 1555 2.06
LINK ZN ZN E 155 OD1 ASP E 83 1555 1555 1.85
LINK CU CU1 F 154 ND1 HIS F 46 1555 1555 2.16
LINK CU CU1 F 154 NE2 HIS F 120 1555 1555 2.01
LINK CU CU1 F 154 NE2 HIS F 48 1555 1555 2.02
LINK ZN ZN F 155 OD1 ASP F 83 1555 1555 1.92
LINK ZN ZN F 155 ND1 HIS F 63 1555 1555 2.07
LINK ZN ZN F 155 ND1 HIS F 80 1555 1555 2.06
LINK ZN ZN F 155 ND1 HIS F 71 1555 1555 2.10
LINK CU CU1 G 154 NE2 HIS G 120 1555 1555 2.10
LINK CU CU1 G 154 NE2 HIS G 48 1555 1555 2.17
LINK CU CU1 G 154 ND1 HIS G 46 1555 1555 2.23
LINK ZN ZN G 155 ND1 HIS G 80 1555 1555 2.06
LINK ZN ZN G 155 ND1 HIS G 71 1555 1555 2.13
LINK ZN ZN G 155 OD1 ASP G 83 1555 1555 1.92
LINK ZN ZN G 155 ND1 HIS G 63 1555 1555 2.16
LINK CU CU1 H 154 NE2 HIS H 120 1555 1555 2.06
LINK CU CU1 H 154 NE2 HIS H 48 1555 1555 2.04
LINK CU CU1 H 154 ND1 HIS H 46 1555 1555 2.15
LINK ZN ZN H 155 ND1 HIS H 71 1555 1555 2.07
LINK ZN ZN H 155 OD1 ASP H 83 1555 1555 1.92
LINK ZN ZN H 155 ND1 HIS H 80 1555 1555 2.11
LINK ZN ZN H 155 ND1 HIS H 63 1555 1555 2.00
LINK CU CU1 I 154 NE2 HIS I 120 1555 1555 1.93
LINK CU CU1 I 154 NE2 HIS I 48 1555 1555 2.13
LINK CU CU1 I 154 ND1 HIS I 46 1555 1555 2.20
LINK ZN ZN I 155 ND1 HIS I 63 1555 1555 2.10
LINK ZN ZN I 155 ND1 HIS I 71 1555 1555 1.97
LINK ZN ZN I 155 ND1 HIS I 80 1555 1555 2.14
LINK ZN ZN I 155 OD1 ASP I 83 1555 1555 2.01
LINK CU CU1 J 154 ND1 HIS J 46 1555 1555 2.36
LINK CU CU1 J 154 NE2 HIS J 120 1555 1555 1.92
LINK CU CU1 J 154 NE2 HIS J 48 1555 1555 2.08
LINK ZN ZN J 155 ND1 HIS J 80 1555 1555 2.02
LINK ZN ZN J 155 OD1 ASP J 83 1555 1555 1.92
LINK ZN ZN J 155 ND1 HIS J 63 1555 1555 2.01
LINK ZN ZN J 155 ND1 HIS J 71 1555 1555 1.97
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 B 46 HIS B 48 HIS B 63 HIS B 120
SITE 1 AC4 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 1 AC5 4 HIS C 46 HIS C 48 HIS C 63 HIS C 120
SITE 1 AC6 4 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 1 AC7 4 HIS D 46 HIS D 48 HIS D 63 HIS D 120
SITE 1 AC8 4 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 1 AC9 4 HIS E 46 HIS E 48 HIS E 63 HIS E 120
SITE 1 BC1 4 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 1 BC2 4 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 1 BC3 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 BC4 4 HIS G 46 HIS G 48 HIS G 63 HIS G 120
SITE 1 BC5 4 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 1 BC6 4 HIS H 46 HIS H 48 HIS H 63 HIS H 120
SITE 1 BC7 4 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 1 BC8 4 HIS I 46 HIS I 48 HIS I 63 HIS I 120
SITE 1 BC9 4 HIS I 63 HIS I 71 HIS I 80 ASP I 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 5 LYS B 75 LYS D 128 HOH D1429 HOH D1450
SITE 2 CC3 5 HOH D1515
CRYST1 203.200 165.200 144.300 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 0.004921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006930 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
