HEADER ELECTRON TRANSPORT 11-AUG-09 3IN0
TITLE CRYSTAL STRUCTURE OF THE F114P/M121Q VARIANT OF PSEUDOMONAS AERUGINOSA
TITLE 2 AZURIN IN THE CU(II) STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AZURIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: OXIDIZED F114P/M121Q AZURIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: AZU, PA4922;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET9A
KEYWDS CUPREDOXIN, AZURIN, GREEK KEY, BETA BARREL, ELECTRON TRANSFER,
KEYWDS 2 COPPER, DISULFIDE BOND, ELECTRON TRANSPORT, METAL-BINDING,
KEYWDS 3 PERIPLASM, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.G.GAO,H.ROBINSON
REVDAT 3 13-OCT-21 3IN0 1 REMARK SEQADV
REVDAT 2 17-NOV-09 3IN0 1 JRNL
REVDAT 1 27-OCT-09 3IN0 0
JRNL AUTH N.M.MARSHALL,D.K.GARNER,T.D.WILSON,Y.G.GAO,H.ROBINSON,
JRNL AUTH 2 M.J.NILGES,Y.LU
JRNL TITL RATIONALLY TUNING THE REDUCTION POTENTIAL OF A SINGLE
JRNL TITL 2 CUPREDOXIN BEYOND THE NATURAL RANGE.
JRNL REF NATURE V. 462 113 2009
JRNL REFN ISSN 0028-0836
JRNL PMID 19890331
JRNL DOI 10.1038/NATURE08551
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.253
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.248
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 0.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 17609
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.248
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.246
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 16390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3880
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 134
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 4022.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 12215
REMARK 3 NUMBER OF RESTRAINTS : 16036
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 ANGLE DISTANCES (A) : 1.662
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.023
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.020
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.028
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.007
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.057
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 4
REMARK 4 3IN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054614.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : CRYOGENICALLY COOLED DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR WITH
REMARK 200 HORIZONTALLY FOCUSING SAGITALLY
REMARK 200 BENT SECOND MONO CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29479
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06500
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, 0.08M NAOAC, 0.2M LITHIUM
REMARK 280 NITRATE, 0.2M CALCIUM CHLORIDE, PH 6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLU A 2 91.23 -62.94
REMARK 500 SER A 25 29.26 -71.41
REMARK 500 MET A 44 59.04 -155.13
REMARK 500 TYR A 72 31.90 70.82
REMARK 500 ALA A 82 155.31 178.97
REMARK 500 ASN B 10 -151.88 -119.38
REMARK 500 CYS B 26 107.54 -51.03
REMARK 500 LEU B 39 132.95 137.30
REMARK 500 MET B 44 58.83 -159.06
REMARK 500 ASP B 77 112.51 -35.13
REMARK 500 GLU B 91 153.36 -39.55
REMARK 500 ASP B 98 105.62 -53.24
REMARK 500 LEU B 102 70.12 -114.72
REMARK 500 GLN B 121 62.02 -109.54
REMARK 500 LEU B 127 82.08 -58.39
REMARK 500 ASN C 18 14.76 -154.88
REMARK 500 ALA C 19 58.57 -167.46
REMARK 500 LYS C 24 -57.57 -26.91
REMARK 500 ASN C 38 23.60 -147.44
REMARK 500 MET C 44 39.53 -167.96
REMARK 500 ASP C 77 108.26 -45.26
REMARK 500 HIS C 83 136.57 -178.83
REMARK 500 GLU C 91 174.09 -53.35
REMARK 500 LEU C 120 -77.34 -96.49
REMARK 500 GLN C 121 74.43 -60.03
REMARK 500 ASN D 10 -158.69 -132.63
REMARK 500 ASN D 16 45.39 -90.31
REMARK 500 THR D 17 143.04 175.94
REMARK 500 PRO D 36 175.49 -53.40
REMARK 500 ASN D 38 55.66 -148.26
REMARK 500 MET D 44 46.11 -142.72
REMARK 500 ASP D 93 109.54 -167.68
REMARK 500 LEU D 127 99.37 -68.51
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 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 117 ND1 105.3
REMARK 620 3 GLN A 121 NE2 76.9 104.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 117 ND1 112.0
REMARK 620 3 GLN B 121 NE2 90.3 108.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 46 ND1
REMARK 620 2 HIS C 117 ND1 104.1
REMARK 620 3 GLN C 121 NE2 74.4 122.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU D 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 46 ND1
REMARK 620 2 HIS D 117 ND1 111.2
REMARK 620 3 GLN D 121 NE2 109.1 78.9
REMARK 620 N 1 2
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IN2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF N47S/M121L VARIANT OF PSEUDOMONAS AERUGINOSA
REMARK 900 AZURIN IN THE CU(II) STATE
DBREF 3IN0 A 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 3IN0 B 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 3IN0 C 1 128 UNP P00282 AZUR_PSEAE 21 148
DBREF 3IN0 D 1 128 UNP P00282 AZUR_PSEAE 21 148
SEQADV 3IN0 PRO A 114 UNP P00282 PHE 134 ENGINEERED MUTATION
SEQADV 3IN0 GLN A 121 UNP P00282 MET 141 ENGINEERED MUTATION
SEQADV 3IN0 PRO B 114 UNP P00282 PHE 134 ENGINEERED MUTATION
SEQADV 3IN0 GLN B 121 UNP P00282 MET 141 ENGINEERED MUTATION
SEQADV 3IN0 PRO C 114 UNP P00282 PHE 134 ENGINEERED MUTATION
SEQADV 3IN0 GLN C 121 UNP P00282 MET 141 ENGINEERED MUTATION
SEQADV 3IN0 PRO D 114 UNP P00282 PHE 134 ENGINEERED MUTATION
SEQADV 3IN0 GLN D 121 UNP P00282 MET 141 ENGINEERED MUTATION
SEQRES 1 A 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 A 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 A 128 LYS GLN PHE THR VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 A 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 A 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 A 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 A 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 A 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 A 128 GLY GLU GLN TYR MET PHE PHE CYS THR PRO PRO GLY HIS
SEQRES 10 A 128 SER ALA LEU GLN LYS GLY THR LEU THR LEU LYS
SEQRES 1 B 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 B 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 B 128 LYS GLN PHE THR VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 B 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 B 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 B 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 B 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 B 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 B 128 GLY GLU GLN TYR MET PHE PHE CYS THR PRO PRO GLY HIS
SEQRES 10 B 128 SER ALA LEU GLN LYS GLY THR LEU THR LEU LYS
SEQRES 1 C 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 C 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 C 128 LYS GLN PHE THR VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 C 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 C 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 C 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 C 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 C 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 C 128 GLY GLU GLN TYR MET PHE PHE CYS THR PRO PRO GLY HIS
SEQRES 10 C 128 SER ALA LEU GLN LYS GLY THR LEU THR LEU LYS
SEQRES 1 D 128 ALA GLU CYS SER VAL ASP ILE GLN GLY ASN ASP GLN MET
SEQRES 2 D 128 GLN PHE ASN THR ASN ALA ILE THR VAL ASP LYS SER CYS
SEQRES 3 D 128 LYS GLN PHE THR VAL ASN LEU SER HIS PRO GLY ASN LEU
SEQRES 4 D 128 PRO LYS ASN VAL MET GLY HIS ASN TRP VAL LEU SER THR
SEQRES 5 D 128 ALA ALA ASP MET GLN GLY VAL VAL THR ASP GLY MET ALA
SEQRES 6 D 128 SER GLY LEU ASP LYS ASP TYR LEU LYS PRO ASP ASP SER
SEQRES 7 D 128 ARG VAL ILE ALA HIS THR LYS LEU ILE GLY SER GLY GLU
SEQRES 8 D 128 LYS ASP SER VAL THR PHE ASP VAL SER LYS LEU LYS GLU
SEQRES 9 D 128 GLY GLU GLN TYR MET PHE PHE CYS THR PRO PRO GLY HIS
SEQRES 10 D 128 SER ALA LEU GLN LYS GLY THR LEU THR LEU LYS
HET CU A 201 1
HET CU B 201 1
HET CU C 201 1
HET CU D 201 1
HETNAM CU COPPER (II) ION
FORMUL 5 CU 4(CU 2+)
FORMUL 9 HOH *134(H2 O)
HELIX 1 1 PRO A 40 GLY A 45 1 6
HELIX 2 2 ASP A 55 GLY A 67 1 13
HELIX 3 3 LEU A 68 ASP A 71 5 4
HELIX 4 4 SER A 100 LEU A 102 5 3
HELIX 5 5 GLY A 116 LEU A 120 5 5
HELIX 6 6 PRO B 40 GLY B 45 1 6
HELIX 7 7 ASP B 55 ALA B 65 1 11
HELIX 8 8 GLY B 67 ASP B 71 5 5
HELIX 9 9 SER B 100 LEU B 102 5 3
HELIX 10 10 GLY B 116 LEU B 120 5 5
HELIX 11 11 PRO C 40 GLY C 45 1 6
HELIX 12 12 ASP C 55 GLY C 67 1 13
HELIX 13 13 LEU C 68 ASP C 71 5 4
HELIX 14 14 SER C 100 LEU C 102 5 3
HELIX 15 15 GLY C 116 GLN C 121 1 6
HELIX 16 16 PRO D 40 GLY D 45 1 6
HELIX 17 17 ASP D 55 ALA D 65 1 11
HELIX 18 18 GLY D 67 ASP D 71 5 5
HELIX 19 19 SER D 100 LEU D 102 5 3
HELIX 20 20 GLY D 116 GLN D 121 1 6
SHEET 1 A 3 SER A 4 GLN A 8 0
SHEET 2 A 3 GLN A 28 SER A 34 1 O SER A 34 N ILE A 7
SHEET 3 A 3 LYS A 92 ASP A 98 -1 O VAL A 95 N VAL A 31
SHEET 1 B 5 ALA A 19 THR A 21 0
SHEET 2 B 5 LYS A 122 THR A 126 1 O THR A 126 N ILE A 20
SHEET 3 B 5 TYR A 108 PHE A 111 -1 N TYR A 108 O LEU A 125
SHEET 4 B 5 VAL A 49 THR A 52 -1 N SER A 51 O MET A 109
SHEET 5 B 5 ALA A 82 HIS A 83 -1 O ALA A 82 N LEU A 50
SHEET 1 C 3 SER B 4 GLN B 8 0
SHEET 2 C 3 GLN B 28 SER B 34 1 O ASN B 32 N ILE B 7
SHEET 3 C 3 LYS B 92 ASP B 98 -1 O VAL B 95 N VAL B 31
SHEET 1 D 5 ALA B 19 VAL B 22 0
SHEET 2 D 5 LYS B 122 LEU B 127 1 O THR B 126 N ILE B 20
SHEET 3 D 5 TYR B 108 PHE B 111 -1 N PHE B 110 O GLY B 123
SHEET 4 D 5 VAL B 49 THR B 52 -1 N SER B 51 O MET B 109
SHEET 5 D 5 ALA B 82 HIS B 83 -1 O ALA B 82 N LEU B 50
SHEET 1 E 3 SER C 4 GLN C 8 0
SHEET 2 E 3 GLN C 28 SER C 34 1 O SER C 34 N ILE C 7
SHEET 3 E 3 LYS C 92 ASP C 98 -1 O VAL C 95 N VAL C 31
SHEET 1 F 5 ALA C 19 THR C 21 0
SHEET 2 F 5 LYS C 122 THR C 126 1 O THR C 126 N ILE C 20
SHEET 3 F 5 TYR C 108 PHE C 111 -1 N TYR C 108 O LEU C 125
SHEET 4 F 5 VAL C 49 THR C 52 -1 N VAL C 49 O PHE C 111
SHEET 5 F 5 ALA C 82 HIS C 83 -1 O ALA C 82 N LEU C 50
SHEET 1 G 3 SER D 4 GLN D 8 0
SHEET 2 G 3 GLN D 28 SER D 34 1 O ASN D 32 N ILE D 7
SHEET 3 G 3 LYS D 92 ASP D 98 -1 O VAL D 95 N VAL D 31
SHEET 1 H 5 ALA D 19 VAL D 22 0
SHEET 2 H 5 LYS D 122 LEU D 127 1 O THR D 124 N ILE D 20
SHEET 3 H 5 TYR D 108 PHE D 111 -1 N PHE D 110 O GLY D 123
SHEET 4 H 5 VAL D 49 THR D 52 -1 N SER D 51 O MET D 109
SHEET 5 H 5 ALA D 82 HIS D 83 -1 O ALA D 82 N LEU D 50
SSBOND 1 CYS A 3 CYS A 26 1555 1555 2.17
SSBOND 2 CYS B 3 CYS B 26 1555 1555 2.04
SSBOND 3 CYS C 3 CYS C 26 1555 1555 2.03
SSBOND 4 CYS D 3 CYS D 26 1555 1555 2.03
LINK ND1 HIS A 46 CU CU A 201 1555 1555 1.96
LINK ND1 HIS A 117 CU CU A 201 1555 1555 1.95
LINK NE2 GLN A 121 CU CU A 201 1555 1555 2.16
LINK ND1 HIS B 46 CU CU B 201 1555 1555 1.95
LINK ND1 HIS B 117 CU CU B 201 1555 1555 1.95
LINK NE2 GLN B 121 CU CU B 201 1555 1555 2.15
LINK ND1 HIS C 46 CU CU C 201 1555 1555 1.95
LINK ND1 HIS C 117 CU CU C 201 1555 1555 1.95
LINK NE2 GLN C 121 CU CU C 201 1555 1555 2.15
LINK ND1 HIS D 46 CU CU D 201 1555 1555 1.96
LINK ND1 HIS D 117 CU CU D 201 1555 1555 1.95
LINK NE2 GLN D 121 CU CU D 201 1555 1555 2.15
SITE 1 AC1 5 GLY A 45 HIS A 46 CYS A 112 HIS A 117
SITE 2 AC1 5 GLN A 121
SITE 1 AC2 5 GLY B 45 HIS B 46 CYS B 112 HIS B 117
SITE 2 AC2 5 GLN B 121
SITE 1 AC3 5 GLY C 45 HIS C 46 CYS C 112 HIS C 117
SITE 2 AC3 5 GLN C 121
SITE 1 AC4 5 GLY D 45 HIS D 46 CYS D 112 HIS D 117
SITE 2 AC4 5 GLN D 121
CRYST1 44.260 49.590 60.510 100.39 103.42 104.31 P 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 0.022594 0.005763 0.007073 0.00000
SCALE2 0.000000 0.020811 0.005424 0.00000
SCALE3 0.000000 0.000000 0.017558 0.00000
(ATOM LINES ARE NOT SHOWN.)
END