HEADER TRANSFERASE 06-NOV-08 2W37
TITLE CRYSTAL STRUCTURE OF THE HEXAMERIC CATABOLIC ORNITHINE
TITLE 2 TRANSCARBAMYLASE FROM LACTOBACILLUS HILGARDII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ORNITHINE TRANSCARBAMYLASE, OTCASE;
COMPND 5 EC: 2.1.3.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS HILGARDII;
SOURCE 3 ORGANISM_TAXID: 1588;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109(DE3)
KEYWDS TRANSCARBAMYLASE, METAL BINDING-SITE, HEXAMER, CYTOPLASM, ORNITHINE,
KEYWDS 2 TRANSFERASE, ARGININE METABOLISM, CARBAMOYL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.DE LAS RIVAS,G.C.FOX,I.ANGULO,H.RODRIGUEZ,R.MUNOZ,J.M.MANCHENO
REVDAT 2 13-DEC-23 2W37 1 REMARK LINK
REVDAT 1 17-NOV-09 2W37 0
JRNL AUTH B.DE LAS RIVAS,G.C.FOX,I.ANGULO,M.M.RIPOLL,H.RODRIGUEZ,
JRNL AUTH 2 R.MUNOZ,J.M.MANCHENO
JRNL TITL CRYSTAL STRUCTURE OF THE HEXAMERIC CATABOLIC ORNITHINE
JRNL TITL 2 TRANSCARBAMYLASE FROM LACTOBACILLUS HILGARDII: STRUCTURAL
JRNL TITL 3 INSIGHTS INTO THE OLIGOMERIC ASSEMBLY AND METAL BINDING.
JRNL REF J.MOL.BIOL. V. 393 425 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19666033
JRNL DOI 10.1016/J.JMB.2009.08.002
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 60594
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3216
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3391
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 162
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8031
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 333
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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): 0.236
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.197
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.501
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8190 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11052 ; 1.360 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1020 ; 5.536 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 381 ;38.139 ;25.118
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1467 ;17.800 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;20.141 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1221 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6162 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3969 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5505 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 482 ; 0.138 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 81 ; 0.191 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.139 ; 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): 5217 ; 0.710 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8133 ; 1.182 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3360 ; 1.638 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2919 ; 2.526 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 343 5
REMARK 3 1 B 3 B 343 5
REMARK 3 1 C 3 C 343 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1364 ; 0.16 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1364 ; 0.16 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1364 ; 0.14 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1313 ; 0.41 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 1313 ; 0.37 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 1313 ; 0.36 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1364 ; 0.80 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1364 ; 0.96 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1364 ; 0.89 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1313 ; 1.53 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1313 ; 1.81 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 1313 ; 1.67 ; 10.00
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 2W37 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1290038044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM16
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63810
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 78.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1DXH
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-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 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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -80.62300
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 MET A -15
REMARK 465 GLY A -14
REMARK 465 GLY A -13
REMARK 465 SER A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 GLY A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 LYS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 MET B -15
REMARK 465 GLY B -14
REMARK 465 GLY B -13
REMARK 465 SER B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 GLY B -5
REMARK 465 ASP B -4
REMARK 465 ASP B -3
REMARK 465 ASP B -2
REMARK 465 ASP B -1
REMARK 465 LYS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 MET C -15
REMARK 465 GLY C -14
REMARK 465 GLY C -13
REMARK 465 SER C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 GLY C -5
REMARK 465 ASP C -4
REMARK 465 ASP C -3
REMARK 465 ASP C -2
REMARK 465 ASP C -1
REMARK 465 LYS C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
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 8 107.40 -168.52
REMARK 500 HIS A 46 58.32 -152.17
REMARK 500 LEU A 135 120.11 145.15
REMARK 500 LYS A 157 115.29 -170.42
REMARK 500 ASN A 245 37.85 35.94
REMARK 500 LEU A 279 155.81 69.36
REMARK 500 ASN A 284 -167.79 -165.03
REMARK 500 MET A 302 -110.02 -117.08
REMARK 500 ASN B 8 114.90 -164.62
REMARK 500 HIS B 46 56.38 -152.61
REMARK 500 SER B 62 69.87 -160.80
REMARK 500 LEU B 135 120.06 138.69
REMARK 500 LYS B 157 116.63 -19.35
REMARK 500 ASP B 168 97.71 -65.17
REMARK 500 MET B 241 73.44 46.69
REMARK 500 ASN B 245 39.87 36.28
REMARK 500 LEU B 279 159.91 65.51
REMARK 500 ASN B 284 -164.43 -161.65
REMARK 500 MET B 302 -102.82 -112.49
REMARK 500 ASN C 8 113.58 -165.71
REMARK 500 HIS C 46 55.53 -155.30
REMARK 500 SER C 62 77.73 -154.14
REMARK 500 LEU C 135 122.49 146.75
REMARK 500 LEU C 279 159.37 68.89
REMARK 500 ASN C 284 -168.21 -160.54
REMARK 500 ASP C 286 38.30 -80.41
REMARK 500 MET C 302 -107.53 -112.93
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 NI A1344 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 79 NE2
REMARK 620 2 HOH A2058 O 86.3
REMARK 620 3 HIS B 79 NE2 95.9 91.7
REMARK 620 4 HOH B2048 O 169.1 83.2 87.2
REMARK 620 5 HIS C 79 NE2 98.7 171.7 94.3 91.4
REMARK 620 6 HOH C2034 O 99.7 84.3 163.6 76.6 88.4
REMARK 620 N 1 2 3 4 5
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1344
DBREF 2W37 A -15 0 PDB 2W37 2W37 -15 0
DBREF 2W37 A 1 343 UNP Q8G998 OTCC_LACHI 1 343
DBREF 2W37 B -15 0 PDB 2W37 2W37 -15 0
DBREF 2W37 B 1 343 UNP Q8G998 OTCC_LACHI 1 343
DBREF 2W37 C -15 0 PDB 2W37 2W37 -15 0
DBREF 2W37 C 1 343 UNP Q8G998 OTCC_LACHI 1 343
SEQRES 1 A 359 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY ASP ASP
SEQRES 2 A 359 ASP ASP LYS MET THR LYS ASP PHE ARG GLN ASN VAL PHE
SEQRES 3 A 359 GLN GLY ARG SER VAL LEU ALA GLU LYS ASP PHE SER ALA
SEQRES 4 A 359 ALA GLU LEU GLU TYR LEU ILE ASP PHE GLY LEU HIS LEU
SEQRES 5 A 359 LYS ALA LEU LYS LYS ALA GLY ILE PRO HIS HIS TYR LEU
SEQRES 6 A 359 GLU GLY LYS ASN ILE ALA LEU LEU PHE GLU LYS SER SER
SEQRES 7 A 359 THR ARG THR ARG SER ALA PHE THR THR ALA SER ILE ASP
SEQRES 8 A 359 LEU GLY ALA HIS PRO GLU TYR LEU GLY GLN ASN ASP ILE
SEQRES 9 A 359 GLN LEU GLY LYS LYS GLU SER THR SER ASP THR ALA LYS
SEQRES 10 A 359 VAL LEU GLY SER MET PHE ASP GLY ILE GLU PHE ARG GLY
SEQRES 11 A 359 PHE LYS GLN SER ASP ALA GLU ILE LEU ALA ARG ASP SER
SEQRES 12 A 359 GLY VAL PRO VAL TRP ASN GLY LEU THR ASP GLU TRP HIS
SEQRES 13 A 359 PRO THR GLN MET LEU ALA ASP PHE MET THR VAL LYS GLU
SEQRES 14 A 359 ASN PHE GLY LYS LEU GLN GLY LEU THR LEU THR PHE MET
SEQRES 15 A 359 GLY ASP GLY ARG ASN ASN VAL ALA ASN SER LEU LEU VAL
SEQRES 16 A 359 THR GLY ALA ILE LEU GLY VAL ASN ILE HIS ILE VAL ALA
SEQRES 17 A 359 PRO LYS ALA LEU PHE PRO THR GLU GLU THR GLN ASN ILE
SEQRES 18 A 359 ALA LYS GLY PHE ALA GLU LYS SER GLY ALA LYS LEU VAL
SEQRES 19 A 359 ILE THR ASP ASP LEU ASP GLU GLY LEU LYS GLY SER ASN
SEQRES 20 A 359 VAL VAL TYR THR ASP VAL TRP VAL SER MET GLY GLU SER
SEQRES 21 A 359 ASN TRP GLU GLU ARG VAL LYS GLU LEU THR PRO TYR GLN
SEQRES 22 A 359 VAL ASN MET GLU ALA MET LYS LYS THR GLY THR PRO ASP
SEQRES 23 A 359 ASP GLN LEU ILE PHE MET HIS CYS LEU PRO ALA PHE HIS
SEQRES 24 A 359 ASN THR ASP THR GLN TYR GLY LYS GLU ILE LYS GLU LYS
SEQRES 25 A 359 TYR GLY ILE THR GLU MET GLU VAL THR ASP GLU VAL PHE
SEQRES 26 A 359 THR SER LYS TYR ALA ARG GLN PHE GLU GLU ALA GLU ASN
SEQRES 27 A 359 ARG MET HIS SER ILE LYS ALA MET MET ALA ALA THR LEU
SEQRES 28 A 359 GLY ASN LEU PHE ILE PRO ARG VAL
SEQRES 1 B 359 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY ASP ASP
SEQRES 2 B 359 ASP ASP LYS MET THR LYS ASP PHE ARG GLN ASN VAL PHE
SEQRES 3 B 359 GLN GLY ARG SER VAL LEU ALA GLU LYS ASP PHE SER ALA
SEQRES 4 B 359 ALA GLU LEU GLU TYR LEU ILE ASP PHE GLY LEU HIS LEU
SEQRES 5 B 359 LYS ALA LEU LYS LYS ALA GLY ILE PRO HIS HIS TYR LEU
SEQRES 6 B 359 GLU GLY LYS ASN ILE ALA LEU LEU PHE GLU LYS SER SER
SEQRES 7 B 359 THR ARG THR ARG SER ALA PHE THR THR ALA SER ILE ASP
SEQRES 8 B 359 LEU GLY ALA HIS PRO GLU TYR LEU GLY GLN ASN ASP ILE
SEQRES 9 B 359 GLN LEU GLY LYS LYS GLU SER THR SER ASP THR ALA LYS
SEQRES 10 B 359 VAL LEU GLY SER MET PHE ASP GLY ILE GLU PHE ARG GLY
SEQRES 11 B 359 PHE LYS GLN SER ASP ALA GLU ILE LEU ALA ARG ASP SER
SEQRES 12 B 359 GLY VAL PRO VAL TRP ASN GLY LEU THR ASP GLU TRP HIS
SEQRES 13 B 359 PRO THR GLN MET LEU ALA ASP PHE MET THR VAL LYS GLU
SEQRES 14 B 359 ASN PHE GLY LYS LEU GLN GLY LEU THR LEU THR PHE MET
SEQRES 15 B 359 GLY ASP GLY ARG ASN ASN VAL ALA ASN SER LEU LEU VAL
SEQRES 16 B 359 THR GLY ALA ILE LEU GLY VAL ASN ILE HIS ILE VAL ALA
SEQRES 17 B 359 PRO LYS ALA LEU PHE PRO THR GLU GLU THR GLN ASN ILE
SEQRES 18 B 359 ALA LYS GLY PHE ALA GLU LYS SER GLY ALA LYS LEU VAL
SEQRES 19 B 359 ILE THR ASP ASP LEU ASP GLU GLY LEU LYS GLY SER ASN
SEQRES 20 B 359 VAL VAL TYR THR ASP VAL TRP VAL SER MET GLY GLU SER
SEQRES 21 B 359 ASN TRP GLU GLU ARG VAL LYS GLU LEU THR PRO TYR GLN
SEQRES 22 B 359 VAL ASN MET GLU ALA MET LYS LYS THR GLY THR PRO ASP
SEQRES 23 B 359 ASP GLN LEU ILE PHE MET HIS CYS LEU PRO ALA PHE HIS
SEQRES 24 B 359 ASN THR ASP THR GLN TYR GLY LYS GLU ILE LYS GLU LYS
SEQRES 25 B 359 TYR GLY ILE THR GLU MET GLU VAL THR ASP GLU VAL PHE
SEQRES 26 B 359 THR SER LYS TYR ALA ARG GLN PHE GLU GLU ALA GLU ASN
SEQRES 27 B 359 ARG MET HIS SER ILE LYS ALA MET MET ALA ALA THR LEU
SEQRES 28 B 359 GLY ASN LEU PHE ILE PRO ARG VAL
SEQRES 1 C 359 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY ASP ASP
SEQRES 2 C 359 ASP ASP LYS MET THR LYS ASP PHE ARG GLN ASN VAL PHE
SEQRES 3 C 359 GLN GLY ARG SER VAL LEU ALA GLU LYS ASP PHE SER ALA
SEQRES 4 C 359 ALA GLU LEU GLU TYR LEU ILE ASP PHE GLY LEU HIS LEU
SEQRES 5 C 359 LYS ALA LEU LYS LYS ALA GLY ILE PRO HIS HIS TYR LEU
SEQRES 6 C 359 GLU GLY LYS ASN ILE ALA LEU LEU PHE GLU LYS SER SER
SEQRES 7 C 359 THR ARG THR ARG SER ALA PHE THR THR ALA SER ILE ASP
SEQRES 8 C 359 LEU GLY ALA HIS PRO GLU TYR LEU GLY GLN ASN ASP ILE
SEQRES 9 C 359 GLN LEU GLY LYS LYS GLU SER THR SER ASP THR ALA LYS
SEQRES 10 C 359 VAL LEU GLY SER MET PHE ASP GLY ILE GLU PHE ARG GLY
SEQRES 11 C 359 PHE LYS GLN SER ASP ALA GLU ILE LEU ALA ARG ASP SER
SEQRES 12 C 359 GLY VAL PRO VAL TRP ASN GLY LEU THR ASP GLU TRP HIS
SEQRES 13 C 359 PRO THR GLN MET LEU ALA ASP PHE MET THR VAL LYS GLU
SEQRES 14 C 359 ASN PHE GLY LYS LEU GLN GLY LEU THR LEU THR PHE MET
SEQRES 15 C 359 GLY ASP GLY ARG ASN ASN VAL ALA ASN SER LEU LEU VAL
SEQRES 16 C 359 THR GLY ALA ILE LEU GLY VAL ASN ILE HIS ILE VAL ALA
SEQRES 17 C 359 PRO LYS ALA LEU PHE PRO THR GLU GLU THR GLN ASN ILE
SEQRES 18 C 359 ALA LYS GLY PHE ALA GLU LYS SER GLY ALA LYS LEU VAL
SEQRES 19 C 359 ILE THR ASP ASP LEU ASP GLU GLY LEU LYS GLY SER ASN
SEQRES 20 C 359 VAL VAL TYR THR ASP VAL TRP VAL SER MET GLY GLU SER
SEQRES 21 C 359 ASN TRP GLU GLU ARG VAL LYS GLU LEU THR PRO TYR GLN
SEQRES 22 C 359 VAL ASN MET GLU ALA MET LYS LYS THR GLY THR PRO ASP
SEQRES 23 C 359 ASP GLN LEU ILE PHE MET HIS CYS LEU PRO ALA PHE HIS
SEQRES 24 C 359 ASN THR ASP THR GLN TYR GLY LYS GLU ILE LYS GLU LYS
SEQRES 25 C 359 TYR GLY ILE THR GLU MET GLU VAL THR ASP GLU VAL PHE
SEQRES 26 C 359 THR SER LYS TYR ALA ARG GLN PHE GLU GLU ALA GLU ASN
SEQRES 27 C 359 ARG MET HIS SER ILE LYS ALA MET MET ALA ALA THR LEU
SEQRES 28 C 359 GLY ASN LEU PHE ILE PRO ARG VAL
HET NI A1344 1
HETNAM NI NICKEL (II) ION
FORMUL 4 NI NI 2+
FORMUL 5 HOH *333(H2 O)
HELIX 1 1 ALA A 23 ALA A 42 1 20
HELIX 2 2 THR A 63 ASP A 75 1 13
HELIX 3 3 THR A 96 MET A 106 1 11
HELIX 4 4 GLN A 117 ASP A 126 1 10
HELIX 5 5 PRO A 141 PHE A 155 1 15
HELIX 6 6 ASN A 172 LEU A 184 1 13
HELIX 7 7 GLU A 200 SER A 213 1 14
HELIX 8 8 LEU A 223 LEU A 227 1 5
HELIX 9 9 TRP A 246 LEU A 253 1 8
HELIX 10 10 MET A 260 LYS A 265 1 6
HELIX 11 11 GLN A 288 TYR A 297 1 10
HELIX 12 12 ASP A 306 PHE A 309 1 4
HELIX 13 13 GLN A 316 LEU A 335 1 20
HELIX 14 14 ALA B 23 ALA B 42 1 20
HELIX 15 15 THR B 63 ASP B 75 1 13
HELIX 16 16 THR B 96 MET B 106 1 11
HELIX 17 17 GLN B 117 ASP B 126 1 10
HELIX 18 18 PRO B 141 PHE B 155 1 15
HELIX 19 19 ASN B 172 LEU B 184 1 13
HELIX 20 20 GLU B 200 SER B 213 1 14
HELIX 21 21 LEU B 223 LEU B 227 1 5
HELIX 22 22 TRP B 246 LEU B 253 1 8
HELIX 23 23 MET B 260 LYS B 265 1 6
HELIX 24 24 GLN B 288 TYR B 297 1 10
HELIX 25 25 ASP B 306 PHE B 309 1 4
HELIX 26 26 GLN B 316 LEU B 335 1 20
HELIX 27 27 ALA C 23 ALA C 42 1 20
HELIX 28 28 THR C 63 ASP C 75 1 13
HELIX 29 29 THR C 96 MET C 106 1 11
HELIX 30 30 GLN C 117 ASP C 126 1 10
HELIX 31 31 PRO C 141 PHE C 155 1 15
HELIX 32 32 ASN C 172 LEU C 184 1 13
HELIX 33 33 GLU C 200 SER C 213 1 14
HELIX 34 34 LEU C 223 LEU C 227 1 5
HELIX 35 35 TRP C 246 LEU C 253 1 8
HELIX 36 36 MET C 260 LYS C 265 1 6
HELIX 37 37 GLN C 288 TYR C 297 1 10
HELIX 38 38 ASP C 306 PHE C 309 1 4
HELIX 39 39 GLN C 316 LEU C 335 1 20
SHEET 1 AA 4 HIS A 79 LEU A 83 0
SHEET 2 AA 4 ASN A 53 GLU A 59 1 O ILE A 54 N GLU A 81
SHEET 3 AA 4 GLY A 109 ARG A 113 1 O GLY A 109 N ALA A 55
SHEET 4 AA 4 VAL A 131 LEU A 135 1 O TRP A 132 N PHE A 112
SHEET 1 AB 5 LEU A 217 THR A 220 0
SHEET 2 AB 5 ASN A 187 VAL A 191 1 O ILE A 188 N VAL A 218
SHEET 3 AB 5 THR A 162 MET A 166 1 O LEU A 163 N HIS A 189
SHEET 4 AB 5 VAL A 232 THR A 235 1 O VAL A 232 N THR A 164
SHEET 5 AB 5 ILE A 274 HIS A 277 1 O ILE A 274 N VAL A 233
SHEET 1 BA 4 HIS B 79 LEU B 83 0
SHEET 2 BA 4 ASN B 53 GLU B 59 1 O ILE B 54 N GLU B 81
SHEET 3 BA 4 GLY B 109 ARG B 113 1 O GLY B 109 N ALA B 55
SHEET 4 BA 4 VAL B 131 LEU B 135 1 O TRP B 132 N PHE B 112
SHEET 1 BB 5 LEU B 217 THR B 220 0
SHEET 2 BB 5 ASN B 187 VAL B 191 1 O ILE B 188 N VAL B 218
SHEET 3 BB 5 THR B 162 MET B 166 1 O LEU B 163 N HIS B 189
SHEET 4 BB 5 VAL B 232 THR B 235 1 O VAL B 232 N THR B 164
SHEET 5 BB 5 ILE B 274 HIS B 277 1 O ILE B 274 N VAL B 233
SHEET 1 CA 4 HIS C 79 LEU C 83 0
SHEET 2 CA 4 ASN C 53 GLU C 59 1 O ILE C 54 N GLU C 81
SHEET 3 CA 4 GLY C 109 ARG C 113 1 O GLY C 109 N ALA C 55
SHEET 4 CA 4 VAL C 131 LEU C 135 1 O TRP C 132 N PHE C 112
SHEET 1 CB 5 LEU C 217 THR C 220 0
SHEET 2 CB 5 ASN C 187 VAL C 191 1 O ILE C 188 N VAL C 218
SHEET 3 CB 5 THR C 162 MET C 166 1 O LEU C 163 N HIS C 189
SHEET 4 CB 5 VAL C 232 THR C 235 1 O VAL C 232 N THR C 164
SHEET 5 CB 5 ILE C 274 HIS C 277 1 O ILE C 274 N VAL C 233
LINK NE2 HIS A 79 NI NI A1344 1555 1555 2.17
LINK NI NI A1344 O HOH A2058 1555 1555 2.22
LINK NI NI A1344 NE2 HIS B 79 1555 1555 2.24
LINK NI NI A1344 O HOH B2048 1555 1555 2.11
LINK NI NI A1344 NE2 HIS C 79 1555 1555 2.21
LINK NI NI A1344 O HOH C2034 1555 1555 2.19
CISPEP 1 LEU A 279 PRO A 280 0 -6.34
CISPEP 2 LEU B 279 PRO B 280 0 -10.00
CISPEP 3 LEU C 279 PRO C 280 0 -9.74
SITE 1 AC1 6 HIS A 79 HOH A2058 HIS B 79 HOH B2048
SITE 2 AC1 6 HIS C 79 HOH C2034
CRYST1 156.805 156.805 80.623 90.00 90.00 120.00 P 3 2 1 18
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 0.006377 0.003682 0.000000 0.00000
SCALE2 0.000000 0.007364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012403 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
