HEADER OXIDOREDUCTASE 01-JUN-05 1ZV2
TITLE CU-CONTAINING NITRITE REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-CONTAINING NITRITE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 44-371;
COMPND 5 SYNONYM: CU-NIR;
COMPND 6 EC: 1.7.2.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 1063;
SOURCE 4 GENE: NIRK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS COPPER PROTEIN, NITRITE REDUCTION, DENITRIFICATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.JACOBSON,H.GUO,K.OLESEN,M.OKVIST,R.NEUTZE,L.SJOLIN
REVDAT 6 23-AUG-23 1ZV2 1 REMARK LINK
REVDAT 5 11-OCT-17 1ZV2 1 REMARK
REVDAT 4 13-JUL-11 1ZV2 1 VERSN
REVDAT 3 24-FEB-09 1ZV2 1 VERSN
REVDAT 2 23-AUG-05 1ZV2 1 JRNL
REVDAT 1 21-JUN-05 1ZV2 0
JRNL AUTH F.JACOBSON,H.GUO,K.OLESEN,M.OKVIST,R.NEUTZE,L.SJOLIN
JRNL TITL STRUCTURES OF THE OXIDIZED AND REDUCED FORMS OF NITRITE
JRNL TITL 2 REDUCTASE FROM RHODOBACTER SPHAEROIDES 2.4.3 AT HIGH PH:
JRNL TITL 3 CHANGES IN THE INTERACTIONS OF THE TYPE 2 COPPER.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 61 1190 2005
JRNL REFN ISSN 0907-4449
JRNL PMID 16131751
JRNL DOI 10.1107/S0907444905017488
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 27569
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1465
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.74
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1822
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2522
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 295
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.115
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.002
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2615 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3567 ; 1.438 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 331 ; 6.977 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;35.419 ;24.250
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 397 ;13.033 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;17.852 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2053 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1185 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1742 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 253 ; 0.125 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.072 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 106 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 52 ; 0.192 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1688 ; 0.776 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2636 ; 1.147 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1062 ; 2.030 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 929 ; 3.071 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.007
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 : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29034
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 26.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1NIF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, MGCL2, TRIS, PH 8.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.19050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.89459
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.16967
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 36.19050
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 20.89459
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.16967
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 36.19050
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 20.89459
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.16967
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.78919
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 98.33933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 41.78919
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 98.33933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 41.78919
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 98.33933
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: -Y, X-Y, Z AND -X+
REMARK 300 Y, -X, Z.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 13650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 72.38100
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 36.19050
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 62.68378
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 636 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 700 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 770 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 786 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 745 O HOH A 755 2.18
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 A 558 O HOH A 787 2655 1.73
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 ALA A 168 69.48 -158.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 338 ASN A 339 148.13
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 401 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 126 ND1
REMARK 620 2 CYS A 167 SG 133.8
REMARK 620 3 HIS A 177 ND1 97.1 102.5
REMARK 620 4 MET A 182 SD 88.8 109.7 128.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 402 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 131 NE2
REMARK 620 2 HIS A 166 NE2 96.3
REMARK 620 3 HIS A 287 NE2 85.7 163.9
REMARK 620 4 HIS A 338 NE2 101.3 103.3 91.9
REMARK 620 5 HOH A 780 O 162.6 91.0 83.0 92.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 220 OD1
REMARK 620 2 THR A 224 OG1 99.6
REMARK 620 3 HOH A 537 O 93.3 93.7
REMARK 620 4 HOH A 733 O 90.9 167.4 92.7
REMARK 620 5 HOH A 778 O 178.1 80.3 88.5 89.0
REMARK 620 6 HOH A 783 O 91.0 84.1 175.4 88.8 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 535 O
REMARK 620 2 HOH A 625 O 90.4
REMARK 620 3 HOH A 697 O 91.9 80.0
REMARK 620 4 HOH A 769 O 92.6 86.5 165.7
REMARK 620 5 HOH A 779 O 90.5 170.8 90.8 102.7
REMARK 620 6 HOH A 784 O 177.4 92.2 88.2 87.9 86.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 528 O
REMARK 620 2 HOH A 648 O 85.9
REMARK 620 3 HOH A 663 O 84.8 170.5
REMARK 620 4 HOH A 715 O 168.3 87.4 101.5
REMARK 620 5 HOH A 781 O 95.8 99.3 83.3 94.7
REMARK 620 6 HOH A 785 O 85.2 85.6 92.0 84.7 175.1
REMARK 620 N 1 2 3 4 5
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHOR STATES THAT RESIDUES ASP 230, ASN 281, SER 319,
REMARK 999 HIS 351, VAL 367, ALA 368 ARE CORRECT BASED ON THE ELECTRON
REMARK 999 DENSITY.
DBREF 1ZV2 A 44 371 UNP Q53239 NIR_RHOSH 44 371
SEQADV 1ZV2 ASP A 230 UNP Q53239 THR 230 SEE REMARK 999
SEQADV 1ZV2 ASN A 281 UNP Q53239 LYS 281 SEE REMARK 999
SEQADV 1ZV2 SER A 319 UNP Q53239 THR 319 SEE REMARK 999
SEQADV 1ZV2 HIS A 351 UNP Q53239 SER 351 SEE REMARK 999
SEQADV 1ZV2 VAL A 367 UNP Q53239 TRP 367 SEE REMARK 999
SEQADV 1ZV2 ALA A 368 UNP Q53239 PRO 368 SEE REMARK 999
SEQRES 1 A 328 LEU PRO ARG VAL LYS HIS THR LEU VAL PRO PRO PRO PHE
SEQRES 2 A 328 ALA HIS ALA HIS GLU GLN VAL ALA ALA SER GLY PRO VAL
SEQRES 3 A 328 ILE ASN GLU PHE GLU MET ARG ILE ILE GLU LYS GLU VAL
SEQRES 4 A 328 GLN LEU ASP GLU ASP ALA TYR LEU GLN ALA MET THR PHE
SEQRES 5 A 328 ASP GLY SER ILE PRO GLY PRO LEU MET ILE VAL HIS GLU
SEQRES 6 A 328 GLY ASP TYR VAL GLU LEU THR LEU ILE ASN PRO PRO GLU
SEQRES 7 A 328 ASN THR MET PRO HIS ASN ILE ASP PHE HIS ALA ALA THR
SEQRES 8 A 328 GLY ALA LEU GLY GLY GLY GLY LEU THR LEU ILE ASN PRO
SEQRES 9 A 328 GLY GLU LYS VAL VAL LEU ARG PHE LYS ALA THR ARG ALA
SEQRES 10 A 328 GLY ALA PHE VAL TYR HIS CYS ALA PRO GLY GLY PRO MET
SEQRES 11 A 328 ILE PRO TRP HIS VAL VAL SER GLY MET ALA GLY CYS ILE
SEQRES 12 A 328 MET VAL LEU PRO ARG ASP GLY LEU LYS ASP HIS GLU GLY
SEQRES 13 A 328 LYS PRO VAL ARG TYR ASP THR VAL TYR TYR ILE GLY GLU
SEQRES 14 A 328 SER ASP HIS TYR ILE PRO LYS ASP GLU ASP GLY THR TYR
SEQRES 15 A 328 MET ARG PHE SER ASP PRO SER GLU GLY TYR GLU ASP MET
SEQRES 16 A 328 VAL ALA VAL MET ASP THR LEU ILE PRO SER HIS ILE VAL
SEQRES 17 A 328 PHE ASN GLY ALA VAL GLY ALA LEU THR GLY GLU GLY ALA
SEQRES 18 A 328 LEU LYS ALA LYS VAL GLY ASP ASN VAL LEU PHE VAL HIS
SEQRES 19 A 328 SER GLN PRO ASN ARG ASP SER ARG PRO HIS LEU ILE GLY
SEQRES 20 A 328 GLY HIS GLY ASP LEU VAL TRP GLU THR GLY LYS PHE HIS
SEQRES 21 A 328 ASN ALA PRO GLU ARG ASP LEU GLU THR TRP PHE ILE ARG
SEQRES 22 A 328 GLY GLY SER ALA GLY ALA ALA LEU TYR LYS PHE LEU GLN
SEQRES 23 A 328 PRO GLY VAL TYR ALA TYR VAL ASN HIS ASN LEU ILE GLU
SEQRES 24 A 328 ALA VAL HIS LYS GLY ALA THR ALA HIS VAL LEU VAL GLU
SEQRES 25 A 328 GLY GLU TRP ASP ASN ASP LEU MET GLU GLN VAL VAL ALA
SEQRES 26 A 328 PRO VAL GLY
HET CU A 401 1
HET CU A 402 1
HET MG A 501 1
HET MG A 502 1
HET MG A 503 1
HETNAM CU COPPER (II) ION
HETNAM MG MAGNESIUM ION
FORMUL 2 CU 2(CU 2+)
FORMUL 4 MG 3(MG 2+)
FORMUL 7 HOH *295(H2 O)
HELIX 1 1 GLY A 135 THR A 143 5 9
HELIX 2 2 PRO A 172 SER A 180 1 9
HELIX 3 3 ASP A 230 THR A 244 1 15
HELIX 4 4 THR A 260 ALA A 264 5 5
HELIX 5 5 ASN A 339 HIS A 345 1 7
SHEET 1 A 3 ARG A 46 LYS A 48 0
SHEET 2 A 3 ILE A 70 ASP A 85 1 O GLU A 72 N VAL A 47
SHEET 3 A 3 ALA A 88 PHE A 95 -1 O LEU A 90 N VAL A 82
SHEET 1 B 4 ARG A 46 LYS A 48 0
SHEET 2 B 4 ILE A 70 ASP A 85 1 O GLU A 72 N VAL A 47
SHEET 3 B 4 TYR A 111 ASN A 118 1 O GLU A 113 N ASN A 71
SHEET 4 B 4 GLU A 149 LYS A 156 -1 O PHE A 155 N VAL A 112
SHEET 1 C 4 LEU A 103 HIS A 107 0
SHEET 2 C 4 ALA A 183 LEU A 189 1 O MET A 187 N MET A 104
SHEET 3 C 4 GLY A 161 HIS A 166 -1 N GLY A 161 O VAL A 188
SHEET 4 C 4 ASP A 129 PHE A 130 -1 N ASP A 129 O HIS A 166
SHEET 1 D 5 HIS A 249 PHE A 252 0
SHEET 2 D 5 THR A 206 HIS A 215 -1 N HIS A 215 O HIS A 249
SHEET 3 D 5 ASN A 272 GLN A 279 1 O VAL A 276 N ILE A 210
SHEET 4 D 5 SER A 319 LYS A 326 -1 O ALA A 323 N PHE A 275
SHEET 5 D 5 LEU A 295 TRP A 297 -1 N LEU A 295 O LEU A 324
SHEET 1 E 4 LEU A 265 LYS A 268 0
SHEET 2 E 4 THR A 349 GLU A 355 1 O LEU A 353 N LEU A 265
SHEET 3 E 4 GLY A 331 ASN A 337 -1 N TYR A 335 O ALA A 350
SHEET 4 E 4 PRO A 286 ILE A 289 -1 N ILE A 289 O ALA A 334
LINK ND1 HIS A 126 CU CU A 401 1555 1555 2.04
LINK NE2 HIS A 131 CU CU A 402 1555 1555 2.04
LINK NE2 HIS A 166 CU CU A 402 1555 1555 2.07
LINK SG CYS A 167 CU CU A 401 1555 1555 2.21
LINK ND1 HIS A 177 CU CU A 401 1555 1555 2.04
LINK SD MET A 182 CU CU A 401 1555 1555 2.48
LINK OD1 ASP A 220 MG MG A 502 1555 1555 1.98
LINK OG1 THR A 224 MG MG A 502 1555 1555 2.21
LINK NE2AHIS A 287 CU CU A 402 2655 1555 2.67
LINK NE2 HIS A 338 CU CU A 402 2655 1555 2.16
LINK CU CU A 402 O HOH A 780 1555 1555 2.02
LINK MG MG A 501 O HOH A 535 1555 1555 2.02
LINK MG MG A 501 O HOH A 625 1555 1555 2.06
LINK MG MG A 501 O HOH A 697 1555 1555 2.11
LINK MG MG A 501 O HOH A 769 1555 1555 2.14
LINK MG MG A 501 O HOH A 779 1555 1555 2.06
LINK MG MG A 501 O HOH A 784 1555 5655 2.17
LINK MG MG A 502 O HOH A 537 1555 1555 2.06
LINK MG MG A 502 O HOH A 733 1555 1555 2.02
LINK MG MG A 502 O HOH A 778 1555 1555 2.04
LINK MG MG A 502 O HOH A 783 1555 1555 2.16
LINK MG MG A 503 O HOH A 528 1555 1555 2.21
LINK MG MG A 503 O HOH A 648 1555 1555 2.12
LINK MG MG A 503 O HOH A 663 1555 1555 1.89
LINK MG MG A 503 O HOH A 715 1555 1555 2.07
LINK MG MG A 503 O HOH A 781 1555 1555 2.02
LINK MG MG A 503 O HOH A 785 1555 1555 2.27
CISPEP 1 PRO A 54 PRO A 55 0 5.90
CISPEP 2 ILE A 99 PRO A 100 0 -4.11
SITE 1 AC1 4 HIS A 126 CYS A 167 HIS A 177 MET A 182
SITE 1 AC2 6 ASP A 129 HIS A 131 HIS A 166 HIS A 287
SITE 2 AC2 6 HIS A 338 HOH A 780
SITE 1 AC3 6 HOH A 535 HOH A 625 HOH A 697 HOH A 769
SITE 2 AC3 6 HOH A 779 HOH A 784
SITE 1 AC4 6 ASP A 220 THR A 224 HOH A 537 HOH A 733
SITE 2 AC4 6 HOH A 778 HOH A 783
SITE 1 AC5 6 HOH A 528 HOH A 648 HOH A 663 HOH A 715
SITE 2 AC5 6 HOH A 781 HOH A 785
CRYST1 72.381 72.381 147.509 90.00 90.00 120.00 H 3 9
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 0.013816 0.007977 0.000000 0.00000
SCALE2 0.000000 0.015953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006779 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
