HEADER OXIDOREDUCTASE 31-MAR-08 2ZKW
TITLE CRYSTAL STRUCTURE OF HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G85R IN
TITLE 2 SPACE GROUP P21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SOD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P
KEYWDS OXIDOREDUCTASE, HUMAN CU-ZN SUPEROXIDE DISMUTASE, ALS, FALS, METAL-
KEYWDS 2 BINDING, DISEASE MUTATION, E.C.1.15.1.1, AMYOTROPHIC LATERAL
KEYWDS 3 SCLEROSIS, ANTIOXIDANT, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 4 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 5 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR S.YOSHIKAWA,M.KUKIMOTO-NIINO,K.ITO,L.CHEN,Z.Q.FU,J.CHRZAS,B.C.WANG,
AUTHOR 2 M.SHIROUZU,M.URUSHITANI,R.TAKAHASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 2 04-APR-12 2ZKW 1 SPRSDE VERSN
REVDAT 1 24-MAR-09 2ZKW 0
SPRSDE 04-APR-12 2ZKW 2YQV
JRNL AUTH S.YOSHIKAWA,M.KUKIMOTO-NIINO,K.ITO,L.CHEN,Z.Q.FU,J.CHRZAS,
JRNL AUTH 2 B.C.WANG,M.SHIROUZU,M.URUSHITANI,R.TAKAHASHI,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT
JRNL TITL 2 G85R IN SPACE GROUP P21
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 185773.230
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 17328
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) : 0.193
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1707
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2226
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 242
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2151
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.66000
REMARK 3 B22 (A**2) : -1.89000
REMARK 3 B33 (A**2) : -8.76000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.13
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.94
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) : 4.440 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.490 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.830 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.760 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.42
REMARK 3 BSOL : 54.25
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 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-08.
REMARK 100 THE RCSB ID CODE IS RCSB028100.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 17839
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.583
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3670
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) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1HL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM IODIDE, 20%(W/V)
REMARK 280 PEG3350, PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.11650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -5
REMARK 465 PRO A -4
REMARK 465 LEU A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 LYS A 23
REMARK 465 GLU A 24
REMARK 465 GLN A 153
REMARK 465 GLY B -5
REMARK 465 PRO B -4
REMARK 465 LEU B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 MET B 0
REMARK 465 LYS B 23
REMARK 465 GLU B 24
REMARK 465 SER B 25
REMARK 465 THR B 54
REMARK 465 ALA B 55
REMARK 465 GLY B 56
REMARK 465 GLN B 153
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 OE1 GLU B 78 OE2 GLU B 121 2547 2.16
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 HIS A 110 22.51 -75.25
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 301 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 138.9
REMARK 620 3 HIS A 120 NE2 97.9 121.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 HIS A 71 ND1 101.3
REMARK 620 3 HIS A 80 ND1 110.6 123.0
REMARK 620 4 ASP A 83 OD1 98.2 97.4 122.1
REMARK 620 5 ASP A 83 OD2 150.9 76.3 94.1 54.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 B 302 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 48 NE2 139.0
REMARK 620 3 HIS B 120 NE2 100.4 120.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 ND1
REMARK 620 2 HIS B 71 ND1 101.5
REMARK 620 3 HIS B 80 ND1 112.4 121.5
REMARK 620 4 ASP B 83 OD1 105.6 102.6 111.5
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZKX RELATED DB: PDB
REMARK 900 HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G85R IN SPACE GROUP
REMARK 900 I212121
REMARK 900 RELATED ID: 2ZKY RELATED DB: PDB
REMARK 900 HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G93A
REMARK 900 RELATED ID: AR_001000134.2 RELATED DB: TARGETDB
DBREF 2ZKW A 0 153 UNP P00441 SODC_HUMAN 1 154
DBREF 2ZKW B 0 153 UNP P00441 SODC_HUMAN 1 154
SEQADV 2ZKW GLY A -5 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW PRO A -4 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW LEU A -3 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW GLY A -2 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW SER A -1 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW ARG A 85 UNP P00441 GLY 86 ENGINEERED
SEQADV 2ZKW GLY B -5 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW PRO B -4 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW LEU B -3 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW GLY B -2 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW SER B -1 UNP P00441 EXPRESSION TAG
SEQADV 2ZKW ARG B 85 UNP P00441 GLY 86 ENGINEERED
SEQRES 1 A 159 GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL
SEQRES 2 A 159 LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE
SEQRES 3 A 159 GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY
SEQRES 4 A 159 SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS
SEQRES 5 A 159 VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER
SEQRES 6 A 159 ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY
SEQRES 7 A 159 GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU ARG
SEQRES 8 A 159 ASN VAL THR ALA ASP LYS ASP GLY VAL ALA ASP VAL SER
SEQRES 9 A 159 ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS
SEQRES 10 A 159 ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP
SEQRES 11 A 159 ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR
SEQRES 12 A 159 GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY
SEQRES 13 A 159 ILE ALA GLN
SEQRES 1 B 159 GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL
SEQRES 2 B 159 LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE
SEQRES 3 B 159 GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY
SEQRES 4 B 159 SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS
SEQRES 5 B 159 VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER
SEQRES 6 B 159 ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY
SEQRES 7 B 159 GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU ARG
SEQRES 8 B 159 ASN VAL THR ALA ASP LYS ASP GLY VAL ALA ASP VAL SER
SEQRES 9 B 159 ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS
SEQRES 10 B 159 ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP
SEQRES 11 B 159 ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR
SEQRES 12 B 159 GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY
SEQRES 13 B 159 ILE ALA GLN
HET CU1 A 301 1
HET ZN A 401 1
HET CU1 B 302 1
HET ZN B 402 1
HETNAM CU1 COPPER (I) ION
HETNAM ZN ZINC ION
FORMUL 3 CU1 2(CU 1+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 7 HOH *46(H2 O)
HELIX 1 1 ALA A 55 GLY A 61 5 7
HELIX 2 2 GLU A 132 LYS A 136 5 5
HELIX 3 3 CYS B 57 GLY B 61 5 5
HELIX 4 4 SER B 107 CYS B 111 5 5
HELIX 5 5 GLU B 132 LYS B 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 GLU A 21 -1 N ASN A 19 O TRP A 32
SHEET 4 A 5 LYS A 3 LYS A 9 -1 N ALA A 4 O PHE A 20
SHEET 5 A 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 B 2 GLY A 41 HIS A 43 0
SHEET 2 B 2 VAL A 87 ALA A 89 -1 O VAL A 87 N HIS A 43
SHEET 1 C 3 PHE A 45 HIS A 48 0
SHEET 2 C 3 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 3 C 3 ARG A 143 VAL A 148 -1 O GLY A 147 N LEU A 117
SHEET 1 D 5 ALA B 95 ASP B 101 0
SHEET 2 D 5 VAL B 29 LYS B 36 -1 N GLY B 33 O VAL B 97
SHEET 3 D 5 GLN B 15 GLN B 22 -1 N ASN B 19 O TRP B 32
SHEET 4 D 5 THR B 2 LYS B 9 -1 N ALA B 4 O PHE B 20
SHEET 5 D 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 E 2 GLY B 41 HIS B 43 0
SHEET 2 E 2 VAL B 87 ALA B 89 -1 O VAL B 87 N HIS B 43
SHEET 1 F 3 PHE B 45 HIS B 48 0
SHEET 2 F 3 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 3 F 3 ARG B 143 VAL B 148 -1 O GLY B 147 N LEU B 117
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.05
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.07
LINK ND1 HIS A 46 CU CU1 A 301 1555 1555 1.94
LINK NE2 HIS A 48 CU CU1 A 301 1555 1555 2.01
LINK ND1 HIS A 63 ZN ZN A 401 1555 1555 2.11
LINK ND1 HIS A 71 ZN ZN A 401 1555 1555 1.97
LINK ND1 HIS A 80 ZN ZN A 401 1555 1555 1.93
LINK OD1 ASP A 83 ZN ZN A 401 1555 1555 2.03
LINK NE2 HIS A 120 CU CU1 A 301 1555 1555 2.09
LINK ND1 HIS B 46 CU CU1 B 302 1555 1555 2.07
LINK NE2 HIS B 48 CU CU1 B 302 1555 1555 1.93
LINK ND1 HIS B 63 ZN ZN B 402 1555 1555 1.96
LINK ND1 HIS B 71 ZN ZN B 402 1555 1555 2.00
LINK ND1 HIS B 80 ZN ZN B 402 1555 1555 2.16
LINK OD1 ASP B 83 ZN ZN B 402 1555 1555 2.07
LINK NE2 HIS B 120 CU CU1 B 302 1555 1555 2.11
LINK OD2 ASP A 83 ZN ZN A 401 1555 1555 2.69
SITE 1 AC1 4 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 1 AC2 4 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 1 AC3 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC4 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
CRYST1 48.616 46.233 52.818 90.00 94.42 90.00 P 1 21 1 4
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 0.020569 0.000000 0.001588 0.00000
SCALE2 0.000000 0.021630 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018989 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
