HEADER OXIDOREDUCTASE 18-AUG-05 2AQN
TITLE CU/ZN SUPEROXIDE DISMUTASE FROM NEISSERIA MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 487;
SOURCE 4 GENE: SODC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SUPEROXIDE DISMUTASE, NEISSERIA MENINGITIDIS.,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DIDONATO,C.J.KASSMANN,C.K.BRUNS,D.E.CABELLI,Z.CAO,
AUTHOR 2 L.B.TABATABAI,J.S.KROLL,E.D.GETZOFF
REVDAT 2 24-FEB-09 2AQN 1 VERSN
REVDAT 1 31-OCT-06 2AQN 0
JRNL AUTH M.DIDONATO,C.J.KASSMANN,C.K.BRUNS,D.E.CABELLI,
JRNL AUTH 2 Z.CAO,L.B.TABATABAI,J.S.KROLL,E.D.GETZOFF
JRNL TITL CU/ZN SUPEROXIDE DISMUTASE FROM NEISSERIA
JRNL TITL 2 MENINGITIDIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
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) : 0.128
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.129
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4009
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 80120
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.118
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.119
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3325
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 66643
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3482
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 530
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3994.32
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 3303.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 9
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 36222
REMARK 3 NUMBER OF RESTRAINTS : 43967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 ANGLE DISTANCES (A) : 0.028
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.030
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.058
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.064
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.022
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.003
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.051
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.079
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 REFINEMENT DECREASED R
REMARK 3 BY 5.24 %
REMARK 4
REMARK 4 2AQN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-05.
REMARK 100 THE RCSB ID CODE IS RCSB034199.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 96
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 : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
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 : 80120
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25200
REMARK 200 R SYM FOR SHELL (I) : 0.25200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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 2APS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMSO4, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.89550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.29600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.89550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.29600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 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 BIOMT1 2 -1.000000 0.000000 0.000000 51.24533
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 66.98934
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL
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 64.59200
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 51.24533
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 64.59200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 66.98934
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 51.24533
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 66.98934
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 CU CU C 301 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 850 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 831 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 874 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 948 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 825 LIES ON A SPECIAL POSITION.
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 HIS A 23
REMARK 465 GLU A 24
REMARK 465 HIS A 25
REMARK 465 ASN A 26
REMARK 465 THR A 27
REMARK 465 ILE A 28
REMARK 465 PRO A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 HIS B 23
REMARK 465 GLU B 24
REMARK 465 HIS B 25
REMARK 465 ASN B 26
REMARK 465 THR B 27
REMARK 465 ILE B 28
REMARK 465 PRO B 29
REMARK 465 LYS B 30
REMARK 465 GLY B 31
REMARK 465 HIS C 23
REMARK 465 GLU C 24
REMARK 465 HIS C 25
REMARK 465 ASN C 26
REMARK 465 THR C 27
REMARK 465 ILE C 28
REMARK 465 PRO C 29
REMARK 465 LYS C 30
REMARK 465 GLY C 31
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA A 32 CA - C - O ANGL. DEV. = -15.6 DEGREES
REMARK 500 ALA A 32 CA - C - N ANGL. DEV. = 17.7 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 145 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 145 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG C 179 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG C 179 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
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 A 33 130.34 -171.62
REMARK 500 ASP C 106 58.03 -148.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 817 DISTANCE = 5.94 ANGSTROMS
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 200 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 79 ND1
REMARK 620 2 HIS A 81 NE2 143.8
REMARK 620 3 HIS A 160 NE2 99.4 116.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 104 ND1
REMARK 620 2 HIS A 113 ND1 103.8
REMARK 620 3 HIS A 122 ND1 103.1 124.6
REMARK 620 4 ASP A 125 OD1 108.7 98.7 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 B 200 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 79 ND1
REMARK 620 2 HIS B 81 NE2 142.6
REMARK 620 3 HIS B 160 NE2 98.3 119.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 104 ND1
REMARK 620 2 HIS B 113 ND1 102.3
REMARK 620 3 HIS B 122 ND1 105.8 120.7
REMARK 620 4 ASP B 125 OD1 109.3 100.0 117.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 C 200 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 79 ND1
REMARK 620 2 HIS C 81 NE2 142.2
REMARK 620 3 HIS C 160 NE2 98.4 119.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 104 ND1
REMARK 620 2 HIS C 113 ND1 107.6
REMARK 620 3 HIS C 122 ND1 102.4 124.2
REMARK 620 4 ASP C 125 OD1 108.7 98.8 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 300 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 73 OE1
REMARK 620 2 HIS A 133 ND1 110.6
REMARK 620 3 GLU B 73 OE1 75.9 117.4
REMARK 620 4 HIS B 133 ND1 123.1 113.8 111.2
REMARK 620 5 GLU A 73 OE2 51.8 87.0 127.6 97.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 301 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 73 OE1
REMARK 620 2 HIS C 133 ND1 101.3
REMARK 620 3 GLU C 73 OE2 52.1 86.2
REMARK 620 4 GLU C 73 OE1 85.1 125.5 132.8
REMARK 620 5 GLU C 73 OE2 132.9 91.1 174.9 52.1
REMARK 620 6 HIS C 133 ND1 125.5 116.3 91.0 101.4 86.3
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 CU1 A 200
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 200
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 C 200
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 300
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 301
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AQM RELATED DB: PDB
REMARK 900 RELATED ID: 2AQP RELATED DB: PDB
REMARK 900 RELATED ID: 2AQQ RELATED DB: PDB
REMARK 900 RELATED ID: 2AQR RELATED DB: PDB
REMARK 900 RELATED ID: 2AQS RELATED DB: PDB
REMARK 900 RELATED ID: 2AQT RELATED DB: PDB
DBREF 2AQN A 23 186 UNP Q59623 SODC_NEIMB 23 186
DBREF 2AQN B 23 186 UNP Q59623 SODC_NEIMB 23 186
DBREF 2AQN C 23 186 UNP Q59623 SODC_NEIMB 23 186
SEQRES 1 A 164 HIS GLU HIS ASN THR ILE PRO LYS GLY ALA SER ILE GLU
SEQRES 2 A 164 VAL LYS VAL GLN GLN LEU ASP PRO VAL ASN GLY ASN LYS
SEQRES 3 A 164 ASP VAL GLY THR VAL THR ILE THR GLU SER ASN TYR GLY
SEQRES 4 A 164 LEU VAL PHE THR PRO ASP LEU GLN GLY LEU SER GLU GLY
SEQRES 5 A 164 LEU HIS GLY PHE HIS ILE HIS GLU ASN PRO SER CYS GLU
SEQRES 6 A 164 PRO LYS GLU LYS GLU GLY LYS LEU THR ALA GLY LEU GLY
SEQRES 7 A 164 ALA GLY GLY HIS TRP ASP PRO LYS GLY ALA LYS GLN HIS
SEQRES 8 A 164 GLY TYR PRO TRP GLN ASP ASP ALA HIS LEU GLY ASP LEU
SEQRES 9 A 164 PRO ALA LEU THR VAL LEU HIS ASP GLY THR ALA THR ASN
SEQRES 10 A 164 PRO VAL LEU ALA PRO ARG LEU LYS HIS LEU ASP ASP VAL
SEQRES 11 A 164 ARG GLY HIS SER ILE MET ILE HIS THR GLY GLY ASP ASN
SEQRES 12 A 164 HIS SER ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO
SEQRES 13 A 164 ARG MET ALA CYS GLY VAL ILE LYS
SEQRES 1 B 164 HIS GLU HIS ASN THR ILE PRO LYS GLY ALA SER ILE GLU
SEQRES 2 B 164 VAL LYS VAL GLN GLN LEU ASP PRO VAL ASN GLY ASN LYS
SEQRES 3 B 164 ASP VAL GLY THR VAL THR ILE THR GLU SER ASN TYR GLY
SEQRES 4 B 164 LEU VAL PHE THR PRO ASP LEU GLN GLY LEU SER GLU GLY
SEQRES 5 B 164 LEU HIS GLY PHE HIS ILE HIS GLU ASN PRO SER CYS GLU
SEQRES 6 B 164 PRO LYS GLU LYS GLU GLY LYS LEU THR ALA GLY LEU GLY
SEQRES 7 B 164 ALA GLY GLY HIS TRP ASP PRO LYS GLY ALA LYS GLN HIS
SEQRES 8 B 164 GLY TYR PRO TRP GLN ASP ASP ALA HIS LEU GLY ASP LEU
SEQRES 9 B 164 PRO ALA LEU THR VAL LEU HIS ASP GLY THR ALA THR ASN
SEQRES 10 B 164 PRO VAL LEU ALA PRO ARG LEU LYS HIS LEU ASP ASP VAL
SEQRES 11 B 164 ARG GLY HIS SER ILE MET ILE HIS THR GLY GLY ASP ASN
SEQRES 12 B 164 HIS SER ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO
SEQRES 13 B 164 ARG MET ALA CYS GLY VAL ILE LYS
SEQRES 1 C 164 HIS GLU HIS ASN THR ILE PRO LYS GLY ALA SER ILE GLU
SEQRES 2 C 164 VAL LYS VAL GLN GLN LEU ASP PRO VAL ASN GLY ASN LYS
SEQRES 3 C 164 ASP VAL GLY THR VAL THR ILE THR GLU SER ASN TYR GLY
SEQRES 4 C 164 LEU VAL PHE THR PRO ASP LEU GLN GLY LEU SER GLU GLY
SEQRES 5 C 164 LEU HIS GLY PHE HIS ILE HIS GLU ASN PRO SER CYS GLU
SEQRES 6 C 164 PRO LYS GLU LYS GLU GLY LYS LEU THR ALA GLY LEU GLY
SEQRES 7 C 164 ALA GLY GLY HIS TRP ASP PRO LYS GLY ALA LYS GLN HIS
SEQRES 8 C 164 GLY TYR PRO TRP GLN ASP ASP ALA HIS LEU GLY ASP LEU
SEQRES 9 C 164 PRO ALA LEU THR VAL LEU HIS ASP GLY THR ALA THR ASN
SEQRES 10 C 164 PRO VAL LEU ALA PRO ARG LEU LYS HIS LEU ASP ASP VAL
SEQRES 11 C 164 ARG GLY HIS SER ILE MET ILE HIS THR GLY GLY ASP ASN
SEQRES 12 C 164 HIS SER ASP HIS PRO ALA PRO LEU GLY GLY GLY GLY PRO
SEQRES 13 C 164 ARG MET ALA CYS GLY VAL ILE LYS
HET CU1 A 200 1
HET ZN A 201 1
HET CU1 B 200 1
HET ZN B 201 1
HET CU1 C 200 1
HET ZN C 201 1
HET CU A 300 1
HET CU C 301 1
HET SO4 B 400 5
HETNAM CU1 COPPER (I) ION
HETNAM ZN ZINC ION
HETNAM CU COPPER (II) ION
HETNAM SO4 SULFATE ION
FORMUL 4 CU1 3(CU 1+)
FORMUL 5 ZN 3(ZN 2+)
FORMUL 10 CU 2(CU 2+)
FORMUL 12 SO4 O4 S 2-
FORMUL 13 HOH *530(H2 O)
HELIX 1 1 GLY A 98 GLY A 102 5 5
HELIX 2 2 HIS A 148 ARG A 153 1 6
HELIX 3 3 ALA A 171 GLY A 176 5 6
HELIX 4 4 GLY B 98 GLY B 102 5 5
HELIX 5 5 HIS B 148 VAL B 152 5 5
HELIX 6 6 ALA B 171 GLY B 176 5 6
HELIX 7 7 GLY C 98 GLY C 102 5 5
HELIX 8 8 HIS C 148 ARG C 153 1 6
HELIX 9 9 ALA C 171 GLY C 176 5 6
SHEET 1 A 7 PHE A 78 HIS A 81 0
SHEET 2 A 7 HIS A 155 HIS A 160 -1 O MET A 158 N HIS A 79
SHEET 3 A 7 ARG A 179 ILE A 185 -1 O GLY A 183 N ILE A 157
SHEET 4 A 7 ILE A 34 GLN A 40 -1 N GLN A 39 O CYS A 182
SHEET 5 A 7 LYS A 48 SER A 58 -1 O VAL A 53 N VAL A 36
SHEET 6 A 7 GLY A 61 LEU A 68 -1 O THR A 65 N THR A 54
SHEET 7 A 7 VAL A 141 ALA A 143 -1 O VAL A 141 N PHE A 64
SHEET 1 B 2 GLY A 74 HIS A 76 0
SHEET 2 B 2 LEU A 129 VAL A 131 -1 O VAL A 131 N GLY A 74
SHEET 1 C 2 LYS A 89 LYS A 91 0
SHEET 2 C 2 LYS A 94 THR A 96 -1 O THR A 96 N LYS A 89
SHEET 1 D 7 PHE B 78 HIS B 81 0
SHEET 2 D 7 HIS B 155 HIS B 160 -1 O MET B 158 N HIS B 79
SHEET 3 D 7 ARG B 179 ILE B 185 -1 O ALA B 181 N ILE B 159
SHEET 4 D 7 ILE B 34 GLN B 40 -1 N GLN B 39 O CYS B 182
SHEET 5 D 7 LYS B 48 SER B 58 -1 O LYS B 48 N GLN B 40
SHEET 6 D 7 GLY B 61 LEU B 68 -1 O THR B 65 N THR B 54
SHEET 7 D 7 VAL B 141 ALA B 143 -1 O VAL B 141 N PHE B 64
SHEET 1 E 2 GLY B 74 HIS B 76 0
SHEET 2 E 2 LEU B 129 VAL B 131 -1 O VAL B 131 N GLY B 74
SHEET 1 F 2 LYS B 89 LYS B 91 0
SHEET 2 F 2 LYS B 94 THR B 96 -1 O LYS B 94 N LYS B 91
SHEET 1 G 7 PHE C 78 HIS C 81 0
SHEET 2 G 7 HIS C 155 HIS C 160 -1 O MET C 158 N HIS C 79
SHEET 3 G 7 ARG C 179 ILE C 185 -1 O GLY C 183 N ILE C 157
SHEET 4 G 7 SER C 33 GLN C 40 -1 N GLN C 39 O CYS C 182
SHEET 5 G 7 LYS C 48 SER C 58 -1 O VAL C 53 N VAL C 36
SHEET 6 G 7 GLY C 61 LEU C 68 -1 O THR C 65 N THR C 54
SHEET 7 G 7 VAL C 141 ALA C 143 -1 O VAL C 141 N PHE C 64
SHEET 1 H 2 GLY C 74 HIS C 76 0
SHEET 2 H 2 LEU C 129 VAL C 131 -1 O VAL C 131 N GLY C 74
SHEET 1 I 2 LYS C 89 LYS C 91 0
SHEET 2 I 2 LYS C 94 THR C 96 -1 O THR C 96 N LYS C 89
SSBOND 1 CYS A 86 CYS A 182 1555 1555 2.06
SSBOND 2 CYS B 86 CYS B 182 1555 1555 2.04
SSBOND 3 CYS C 86 CYS C 182 1555 1555 2.04
LINK CU CU1 A 200 ND1 HIS A 79 1555 1555 1.99
LINK CU CU1 A 200 NE2 HIS A 81 1555 1555 1.95
LINK CU CU1 A 200 NE2 HIS A 160 1555 1555 2.05
LINK ZN ZN A 201 ND1 HIS A 104 1555 1555 2.03
LINK ZN ZN A 201 ND1 HIS A 113 1555 1555 2.05
LINK ZN ZN A 201 ND1 HIS A 122 1555 1555 2.03
LINK ZN ZN A 201 OD1 ASP A 125 1555 1555 1.92
LINK CU CU1 B 200 ND1 HIS B 79 1555 1555 1.98
LINK CU CU1 B 200 NE2 HIS B 81 1555 1555 1.98
LINK CU CU1 B 200 NE2 HIS B 160 1555 1555 2.03
LINK ZN ZN B 201 ND1 HIS B 104 1555 1555 2.09
LINK ZN ZN B 201 ND1 HIS B 113 1555 1555 2.09
LINK ZN ZN B 201 ND1 HIS B 122 1555 1555 2.02
LINK ZN ZN B 201 OD1 ASP B 125 1555 1555 1.89
LINK CU CU1 C 200 ND1 HIS C 79 1555 1555 2.02
LINK CU CU1 C 200 NE2 HIS C 81 1555 1555 1.97
LINK CU CU1 C 200 NE2 HIS C 160 1555 1555 1.94
LINK ZN ZN C 201 ND1 HIS C 104 1555 1555 1.96
LINK ZN ZN C 201 ND1 HIS C 113 1555 1555 1.97
LINK ZN ZN C 201 ND1 HIS C 122 1555 1555 2.08
LINK ZN ZN C 201 OD1 ASP C 125 1555 1555 1.91
LINK CU CU A 300 OE1 GLU A 73 1555 1555 1.94
LINK CU CU A 300 ND1 HIS A 133 1555 1555 2.01
LINK CU CU A 300 OE1 GLU B 73 1555 1555 2.02
LINK CU CU A 300 ND1 HIS B 133 1555 1555 1.95
LINK CU CU C 301 OE1 GLU C 73 1555 1555 2.13
LINK CU CU C 301 ND1 HIS C 133 1555 1555 2.07
LINK CU CU A 300 OE2 GLU A 73 1555 1555 2.76
LINK CU CU C 301 OE2 GLU C 73 1555 1555 2.67
LINK CU CU C 301 OE1 GLU C 73 1555 2656 2.13
LINK CU CU C 301 OE2 GLU C 73 1555 2656 2.67
LINK CU CU C 301 ND1 HIS C 133 1555 2656 2.07
CISPEP 1 HIS A 169 PRO A 170 0 4.54
CISPEP 2 HIS B 169 PRO B 170 0 2.46
CISPEP 3 HIS C 169 PRO C 170 0 0.40
SITE 1 AC1 4 HIS A 79 HIS A 81 HIS A 104 HIS A 160
SITE 1 AC2 4 HIS A 104 HIS A 113 HIS A 122 ASP A 125
SITE 1 AC3 4 HIS B 79 HIS B 81 HIS B 104 HIS B 160
SITE 1 AC4 4 HIS B 104 HIS B 113 HIS B 122 ASP B 125
SITE 1 AC5 4 HIS C 79 HIS C 81 HIS C 104 HIS C 160
SITE 1 AC6 4 HIS C 104 HIS C 113 HIS C 122 ASP C 125
SITE 1 AC7 4 GLU A 73 HIS A 133 GLU B 73 HIS B 133
SITE 1 AC8 2 GLU C 73 HIS C 133
SITE 1 AC9 6 ASN A 59 LYS A 111 GLN B 118 ASP B 119
SITE 2 AC9 6 ASP B 120 HOH B 527
CRYST1 99.791 64.592 82.730 90.00 125.93 90.00 C 1 2 1 12
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 0.010021 0.000000 0.007262 0.00000
SCALE2 0.000000 0.015482 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014928 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
