HEADER OXIDOREDUCTASE 27-MAY-08 2ZOO
TITLE CRYSTAL STRUCTURE OF NITRITE REDUCTASE FROM PSEUDOALTEROMONAS
TITLE 2 HALOPLANKTIS TAC125
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE NITRITE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 26-467;
COMPND 5 EC: 1.7.99.3, 1.7.2.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOALTEROMONAS HALOPLANKTIS;
SOURCE 3 ORGANISM_TAXID: 326442;
SOURCE 4 STRAIN: TAC125
KEYWDS NITRITE, ELECTRON TRANSFER, ELECTRON TRANSPORT, HEME, IRON, METAL-
KEYWDS 2 BINDING, OXIDOREDUCTASE, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NOJIRI,A.TSUDA,K.YAMAGUCHI,S.SUZUKI
REVDAT 5 01-NOV-23 2ZOO 1 HETSYN
REVDAT 4 29-JUL-20 2ZOO 1 COMPND REMARK HET HETNAM
REVDAT 4 2 1 HETSYN FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 13-JUL-11 2ZOO 1 VERSN
REVDAT 2 25-AUG-10 2ZOO 1
REVDAT 1 09-JUN-09 2ZOO 0
JRNL AUTH M.NOJIRI,H.KOTEISHI,A.TSUDA,T.NAKAGAMI,K.KOBAYASHI,T.INOUE,
JRNL AUTH 2 K.YAMAGUCHI,S.SUZUKI
JRNL TITL ELECTRON TRANSFER PROCESSES WITHIN AND BETWEEN PROTEINS
JRNL TITL 2 CONTAINING THE HEME C AND BLUE CU
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 63885
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 7167
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4436
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 522
REMARK 3 BIN FREE R VALUE : 0.2280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3326
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 83
REMARK 3 SOLVENT ATOMS : 402
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.094
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.092
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.967
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3489 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4766 ; 1.519 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 437 ; 6.960 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 157 ;37.990 ;25.414
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 527 ;15.454 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;18.419 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 524 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2693 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1614 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2389 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 323 ; 0.120 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.065 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 153 ; 0.191 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 74 ; 0.201 ; 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): 2226 ; 0.993 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3497 ; 1.365 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1418 ; 2.334 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1267 ; 3.643 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2ZOO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000028232.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTALS SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72995
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 43.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1KBW, 1C52
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, AMMONIUM SULFATE,
REMARK 280 SODIUM CITRATE, SUCROSE, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
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 90.16900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.16900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.16900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.16900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 90.16900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.16900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 90.16900
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 90.16900
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 90.16900
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 90.16900
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 90.16900
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 90.16900
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 90.16900
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 90.16900
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 90.16900
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 90.16900
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 90.16900
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 90.16900
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 135.25350
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 45.08450
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 45.08450
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 135.25350
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 135.25350
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 135.25350
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 45.08450
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 45.08450
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 135.25350
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 45.08450
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 135.25350
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 45.08450
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 135.25350
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 45.08450
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 45.08450
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 45.08450
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 135.25350
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 45.08450
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 135.25350
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 135.25350
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 135.25350
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 45.08450
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 45.08450
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 135.25350
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 135.25350
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 45.08450
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 45.08450
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 45.08450
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 45.08450
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 135.25350
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 45.08450
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 135.25350
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 45.08450
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 135.25350
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 135.25350
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 135.25350
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -240.0 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 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 A1054 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1139 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 ALA A 1
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 LYS A 442
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 SG CYS A 353 CAC HEM A 600 1.86
REMARK 500 SG CYS A 350 CAB HEM A 600 1.87
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 999 O HOH A 999 5555 1.89
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 215 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 215 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 THR A 254 CB - CA - C ANGL. DEV. = -17.0 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 ASN A 22 52.42 -110.72
REMARK 500 GLU A 55 -23.98 82.51
REMARK 500 ASP A 202 -123.74 54.37
REMARK 500 ALA A 309 4.73 -163.84
REMARK 500 GLN A 355 162.60 78.52
REMARK 500 ALA A 364 -57.86 -136.10
REMARK 500 ASN A 377 89.60 -156.41
REMARK 500 ASN A 401 40.99 -144.45
REMARK 500 ASN A 408 43.73 -80.06
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 SER A 280 ILE A 281 -143.46
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 500 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 84 ND1
REMARK 620 2 CYS A 125 SG 138.3
REMARK 620 3 HIS A 133 ND1 99.5 109.4
REMARK 620 4 MET A 138 SD 81.8 111.9 113.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 501 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 89 NE2
REMARK 620 2 HIS A 124 NE2 118.6
REMARK 620 3 HIS A 279 NE2 107.6 107.5
REMARK 620 4 HOH A1201 O 99.3 104.3 120.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 600 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 354 NE2
REMARK 620 2 HEM A 600 NA 91.0
REMARK 620 3 HEM A 600 NB 90.4 87.8
REMARK 620 4 HEM A 600 NC 89.9 179.0 91.7
REMARK 620 5 HEM A 600 ND 90.0 92.5 179.5 88.0
REMARK 620 6 MET A 404 SD 176.7 85.8 90.4 93.3 89.2
REMARK 620 N 1 2 3 4 5
DBREF 2ZOO A 1 442 UNP Q3IGF7 Q3IGF7_PSEHT 26 467
SEQRES 1 A 442 ALA SER ASN LEU LYS THR GLU GLN ALA ILE LEU THR PRO
SEQRES 2 A 442 PRO PRO MET VAL PRO PRO ALA ILE ASN ARG ASP HIS SER
SEQRES 3 A 442 ALA LYS VAL VAL ILE ASN LEU GLU THR ARG GLU GLN VAL
SEQRES 4 A 442 GLY ARG ILE ALA ASP GLY VAL GLU TYR VAL PHE TRP SER
SEQRES 5 A 442 PHE GLY GLU THR VAL PRO GLY SER PHE ILE ARG VAL ARG
SEQRES 6 A 442 GLU GLY ASP GLU ILE GLU PHE ASN LEU SER ASN HIS PRO
SEQRES 7 A 442 SER SER LYS MET PRO HIS ASN ILE ASP LEU HIS ALA VAL
SEQRES 8 A 442 THR GLY PRO GLY GLY GLY ALA GLU SER SER PHE THR ALA
SEQRES 9 A 442 PRO GLY HIS THR SER THR PHE ASN PHE LYS ALA LEU ASN
SEQRES 10 A 442 PRO GLY LEU TYR ILE TYR HIS CYS ALA THR ALA PRO VAL
SEQRES 11 A 442 GLY MET HIS ILE ALA ASN GLY MET TYR GLY LEU ILE LEU
SEQRES 12 A 442 VAL GLU PRO LYS GLU GLY LEU ALA PRO VAL ASP ARG GLU
SEQRES 13 A 442 TYR TYR LEU VAL GLN GLY ASP PHE TYR THR LYS GLY GLU
SEQRES 14 A 442 PHE GLY GLU ALA GLY LEU GLN PRO PHE ASP MET ALA LYS
SEQRES 15 A 442 ALA ILE ASP GLU ASP ALA ASP TYR VAL VAL PHE ASN GLY
SEQRES 16 A 442 SER VAL GLY SER THR THR ASP GLU ASN SER LEU THR ALA
SEQRES 17 A 442 LYS VAL GLY GLU THR VAL ARG LEU TYR ILE GLY ASN GLY
SEQRES 18 A 442 GLY PRO ASN LEU VAL SER SER PHE HIS VAL ILE GLY GLU
SEQRES 19 A 442 ILE PHE ASP THR VAL TYR VAL GLU GLY GLY SER LEU LYS
SEQRES 20 A 442 ASN HIS ASN VAL GLN THR THR LEU ILE PRO ALA GLY GLY
SEQRES 21 A 442 ALA ALA ILE VAL GLU PHE LYS VAL GLU VAL PRO GLY THR
SEQRES 22 A 442 PHE ILE LEU VAL ASP HIS SER ILE PHE ARG ALA PHE ASN
SEQRES 23 A 442 LYS GLY ALA LEU ALA MET LEU LYS VAL GLU GLY PRO ASP
SEQRES 24 A 442 ASP HIS SER ILE PHE THR GLY LYS THR ALA GLU ASN VAL
SEQRES 25 A 442 TYR LEU PRO GLU GLY SER ALA ILE GLN SER LEU ASP ASN
SEQRES 26 A 442 THR PHE THR LYS ILE THR ALA ASN ASN LYS ASP GLU GLN
SEQRES 27 A 442 ILE ARG PHE GLY GLN ARG VAL TYR GLU ALA ASN CYS MET
SEQRES 28 A 442 ALA CYS HIS GLN ALA ASN GLY GLU GLY ILE PRO GLY ALA
SEQRES 29 A 442 PHE PRO PRO LEU ALA LYS SER ASP TYR LEU ASN ASN ASN
SEQRES 30 A 442 PRO LEU LEU GLY VAL ASN ALA ILE ILE LYS GLY LEU SER
SEQRES 31 A 442 GLY PRO ILE LYS VAL ASN ASN VAL ASN TYR ASN GLY VAL
SEQRES 32 A 442 MET PRO ALA MET ASN LEU ASN ASP GLU ASP ILE ALA ASN
SEQRES 33 A 442 VAL ILE THR PHE VAL LEU ASN ASN TRP ASP ASN ALA GLY
SEQRES 34 A 442 GLY LYS VAL SER ALA GLU GLN VAL ALA LYS GLN ARG LYS
HET GLC B 1 11
HET FRU B 2 12
HET CU A 500 1
HET CU A 501 1
HET HEM A 600 43
HET SO4 A 801 5
HET SO4 A 802 5
HET SO4 A 803 5
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM FRU BETA-D-FRUCTOFURANOSE
HETNAM CU COPPER (II) ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN FRU BETA-D-FRUCTOSE; D-FRUCTOSE; FRUCTOSE
HETSYN HEM HEME
FORMUL 2 GLC C6 H12 O6
FORMUL 2 FRU C6 H12 O6
FORMUL 3 CU 2(CU 2+)
FORMUL 5 HEM C34 H32 FE N4 O4
FORMUL 6 SO4 3(O4 S 2-)
FORMUL 9 HOH *402(H2 O)
HELIX 1 1 GLY A 93 SER A 101 5 9
HELIX 2 2 PRO A 129 ASN A 136 1 8
HELIX 3 3 ASP A 179 ASP A 185 1 7
HELIX 4 4 THR A 201 SER A 205 5 5
HELIX 5 5 GLU A 242 GLY A 244 5 3
HELIX 6 6 ILE A 281 ASN A 286 1 6
HELIX 7 7 ASN A 334 CYS A 350 1 17
HELIX 8 8 CYS A 350 GLN A 355 1 6
HELIX 9 9 SER A 371 ASN A 377 1 7
HELIX 10 10 ASN A 377 GLY A 388 1 12
HELIX 11 11 ASN A 410 ASN A 423 1 14
HELIX 12 12 SER A 433 ARG A 441 1 9
SHEET 1 A 4 THR A 6 GLN A 8 0
SHEET 2 A 4 LYS A 28 ALA A 43 1 O LYS A 28 N GLU A 7
SHEET 3 A 4 GLU A 69 ASN A 76 1 O GLU A 71 N VAL A 29
SHEET 4 A 4 THR A 108 LYS A 114 -1 O PHE A 113 N ILE A 70
SHEET 1 B 4 THR A 6 GLN A 8 0
SHEET 2 B 4 LYS A 28 ALA A 43 1 O LYS A 28 N GLU A 7
SHEET 3 B 4 VAL A 46 PHE A 53 -1 O SER A 52 N ARG A 36
SHEET 4 B 4 GLY A 174 GLN A 176 1 O GLY A 174 N GLU A 47
SHEET 1 C 4 ILE A 62 ARG A 65 0
SHEET 2 C 4 TYR A 139 GLU A 145 1 O LEU A 143 N ILE A 62
SHEET 3 C 4 GLY A 119 HIS A 124 -1 N GLY A 119 O VAL A 144
SHEET 4 C 4 ASP A 87 LEU A 88 -1 N ASP A 87 O HIS A 124
SHEET 1 D 6 TYR A 190 PHE A 193 0
SHEET 2 D 6 ARG A 155 PHE A 164 -1 N PHE A 164 O TYR A 190
SHEET 3 D 6 THR A 213 GLY A 222 1 O TYR A 217 N TYR A 157
SHEET 4 D 6 GLY A 260 LYS A 267 -1 O VAL A 264 N LEU A 216
SHEET 5 D 6 THR A 238 TYR A 240 -1 N TYR A 240 O ILE A 263
SHEET 6 D 6 LYS A 247 ASN A 248 -1 O ASN A 248 N VAL A 239
SHEET 1 E 5 LEU A 206 LYS A 209 0
SHEET 2 E 5 LEU A 290 GLU A 296 1 O MET A 292 N LEU A 206
SHEET 3 E 5 GLY A 272 ASP A 278 -1 N GLY A 272 O VAL A 295
SHEET 4 E 5 SER A 227 ILE A 232 -1 N ILE A 232 O ILE A 275
SHEET 5 E 5 THR A 253 ILE A 256 -1 O ILE A 256 N SER A 227
SHEET 1 F 2 LEU A 389 SER A 390 0
SHEET 2 F 2 VAL A 403 MET A 404 -1 O MET A 404 N LEU A 389
SHEET 1 G 2 ILE A 393 VAL A 395 0
SHEET 2 G 2 VAL A 398 TYR A 400 -1 O TYR A 400 N ILE A 393
LINK C1 GLC B 1 O2 FRU B 2 1555 1555 1.45
LINK ND1 HIS A 84 CU CU A 500 1555 1555 2.13
LINK NE2 HIS A 89 CU CU A 501 1555 1555 1.94
LINK NE2 HIS A 124 CU CU A 501 1555 1555 2.00
LINK SG CYS A 125 CU CU A 500 1555 1555 2.22
LINK ND1 HIS A 133 CU CU A 500 1555 1555 2.06
LINK SD MET A 138 CU CU A 500 1555 1555 2.54
LINK NE2 HIS A 279 CU CU A 501 9555 1555 2.08
LINK NE2 HIS A 354 FE HEM A 600 1555 1555 2.01
LINK SD MET A 404 FE HEM A 600 1555 1555 2.37
LINK CU CU A 501 O HOH A1201 1555 1555 2.10
CISPEP 1 PRO A 14 PRO A 15 0 1.58
CISPEP 2 VAL A 57 PRO A 58 0 -2.04
CISPEP 3 ALA A 128 PRO A 129 0 -3.09
CISPEP 4 GLY A 222 PRO A 223 0 11.15
CRYST1 180.338 180.338 180.338 90.00 90.00 90.00 P 41 3 2 24
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 0.005545 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005545 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005545 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
