HEADER OXIDOREDUCTASE 13-AUG-13 4M87
TITLE CRYSTAL STRUCTURE OF ENOYL-ACYL CARRIER PROTEIN REDUCTASE (FABI) FROM
TITLE 2 NEISSERIA MENINGITIDIS IN COMPLEX WITH NAD+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.3.1.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 272831;
SOURCE 4 STRAIN: FAM18;
SOURCE 5 GENE: FABI, NMC1834;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENOYL, ACYL CARRIER PROTEIN, ACP, NEISSERIA, ROSSMANN FOLD,
KEYWDS 2 REDUCTASE, NAD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.NANSON,J.K.FORWOOD
REVDAT 2 28-FEB-24 4M87 1 REMARK
REVDAT 1 02-OCT-13 4M87 0
JRNL AUTH J.D.NANSON,J.K.FORWOOD
JRNL TITL CRYSTAL STRUCTURE OF ENOYL-ACYL CARRIER PROTEIN REDUCTASE
JRNL TITL 2 (FABI) FROM NEISSERIA MENINGITIDIS IN COMPLEX WITH NAD+
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 27446
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1468
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1943
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.1740
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.1950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3752
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.30
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) : -0.01000
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): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.474
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3904 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3754 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5281 ; 1.249 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8614 ; 0.901 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 500 ; 5.609 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;30.027 ;23.526
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 646 ;12.189 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;13.938 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 601 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4415 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 883 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2009 ; 0.908 ; 1.990
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2008 ; 0.905 ; 1.988
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2506 ; 1.543 ; 2.978
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2507 ; 1.544 ; 2.979
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1893 ; 1.324 ; 2.267
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1894 ; 1.324 ; 2.268
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2776 ; 2.267 ; 3.319
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4593 ; 4.451 ;16.901
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4501 ; 4.278 ;16.639
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 258 B 2 258 14107 0.11 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 258
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2815 -31.6941 -1.4627
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0291
REMARK 3 T33: 0.0216 T12: -0.0274
REMARK 3 T13: -0.0043 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.0958 L22: 0.1663
REMARK 3 L33: 0.4929 L12: -0.0541
REMARK 3 L13: 0.0280 L23: -0.1063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0369 S12: 0.0311 S13: 0.0304
REMARK 3 S21: -0.0157 S22: -0.0225 S23: -0.0111
REMARK 3 S31: 0.0180 S32: 0.0129 S33: 0.0594
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 258
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2438 -56.4422 16.3473
REMARK 3 T TENSOR
REMARK 3 T11: 0.0698 T22: 0.0033
REMARK 3 T33: 0.0398 T12: 0.0027
REMARK 3 T13: 0.0377 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.3015 L22: 0.0818
REMARK 3 L33: 0.4208 L12: -0.0766
REMARK 3 L13: -0.0403 L23: 0.0384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0349 S12: -0.0241 S13: -0.0288
REMARK 3 S21: -0.0249 S22: -0.0025 S23: -0.0013
REMARK 3 S31: 0.1144 S32: -0.0063 S33: 0.0375
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 4M87 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081588.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : SILICON DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29052
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 35.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
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) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3M AMMONIUM SULFATE, 12.5% GLYCEROL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 80.28000
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 160.56000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 120.42000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 200.70000
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 40.14000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 80.28000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 160.56000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 200.70000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 120.42000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 40.14000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 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 0.500000 0.866025 0.000000 45.55000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -78.89491
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.14000
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 1
REMARK 465 THR A 259
REMARK 465 GLU A 260
REMARK 465 GLY A 261
REMARK 465 MET B 1
REMARK 465 LYS B 194
REMARK 465 THR B 195
REMARK 465 LEU B 196
REMARK 465 ALA B 197
REMARK 465 ALA B 198
REMARK 465 SER B 199
REMARK 465 GLY B 200
REMARK 465 ILE B 201
REMARK 465 ALA B 202
REMARK 465 ASP B 203
REMARK 465 PHE B 204
REMARK 465 THR B 259
REMARK 465 GLU B 260
REMARK 465 GLY B 261
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 156 -27.52 77.98
REMARK 500 ASN A 158 -122.32 52.28
REMARK 500 VAL A 248 74.04 -111.76
REMARK 500 ASN B 156 -27.87 79.87
REMARK 500 ASN B 158 -123.79 52.73
REMARK 500 VAL B 248 74.43 -111.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M86 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN UNBOUND FORM
REMARK 900 RELATED ID: 4M89 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH NAD+ AND TRICLOSAN
DBREF 4M87 A 1 261 UNP A1KVU8 A1KVU8_NEIMF 1 261
DBREF 4M87 B 1 261 UNP A1KVU8 A1KVU8_NEIMF 1 261
SEQRES 1 A 261 MET GLY PHE LEU GLN GLY LYS LYS ILE LEU ILE THR GLY
SEQRES 2 A 261 MET ILE SER GLU ARG SER ILE ALA TYR GLY ILE ALA LYS
SEQRES 3 A 261 ALA CYS ARG GLU GLN GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 A 261 VAL VAL ASP LYS LEU GLU GLU ARG VAL ARG LYS MET ALA
SEQRES 5 A 261 ALA GLU LEU ASP SER GLU LEU VAL PHE ARG CYS ASP VAL
SEQRES 6 A 261 ALA SER ASP ASP GLU ILE ASN GLN VAL PHE ALA ASP LEU
SEQRES 7 A 261 GLY LYS HIS TRP ASP GLY LEU ASP GLY LEU VAL HIS SER
SEQRES 8 A 261 ILE GLY PHE ALA PRO LYS GLU ALA LEU SER GLY ASP PHE
SEQRES 9 A 261 LEU ASP SER ILE SER ARG GLU ALA PHE ASN THR ALA HIS
SEQRES 10 A 261 GLU ILE SER ALA TYR SER LEU PRO ALA LEU ALA LYS ALA
SEQRES 11 A 261 ALA ARG PRO MET MET ARG GLY ARG ASN SER ALA ILE VAL
SEQRES 12 A 261 ALA LEU SER TYR LEU GLY ALA VAL ARG ALA ILE PRO ASN
SEQRES 13 A 261 TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU GLU ALA
SEQRES 14 A 261 GLY ILE ARG PHE THR ALA ALA CYS LEU GLY LYS GLU GLY
SEQRES 15 A 261 ILE ARG CYS ASN GLY ILE SER ALA GLY PRO ILE LYS THR
SEQRES 16 A 261 LEU ALA ALA SER GLY ILE ALA ASP PHE GLY LYS LEU LEU
SEQRES 17 A 261 GLY HIS VAL ALA ALA HIS ASN PRO LEU ARG ARG ASN VAL
SEQRES 18 A 261 THR ILE GLU GLU VAL GLY ASN THR ALA ALA PHE LEU LEU
SEQRES 19 A 261 SER ASP LEU SER SER GLY ILE THR GLY GLU ILE THR TYR
SEQRES 20 A 261 VAL ASP GLY GLY TYR SER ILE ASN ALA LEU SER THR GLU
SEQRES 21 A 261 GLY
SEQRES 1 B 261 MET GLY PHE LEU GLN GLY LYS LYS ILE LEU ILE THR GLY
SEQRES 2 B 261 MET ILE SER GLU ARG SER ILE ALA TYR GLY ILE ALA LYS
SEQRES 3 B 261 ALA CYS ARG GLU GLN GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 B 261 VAL VAL ASP LYS LEU GLU GLU ARG VAL ARG LYS MET ALA
SEQRES 5 B 261 ALA GLU LEU ASP SER GLU LEU VAL PHE ARG CYS ASP VAL
SEQRES 6 B 261 ALA SER ASP ASP GLU ILE ASN GLN VAL PHE ALA ASP LEU
SEQRES 7 B 261 GLY LYS HIS TRP ASP GLY LEU ASP GLY LEU VAL HIS SER
SEQRES 8 B 261 ILE GLY PHE ALA PRO LYS GLU ALA LEU SER GLY ASP PHE
SEQRES 9 B 261 LEU ASP SER ILE SER ARG GLU ALA PHE ASN THR ALA HIS
SEQRES 10 B 261 GLU ILE SER ALA TYR SER LEU PRO ALA LEU ALA LYS ALA
SEQRES 11 B 261 ALA ARG PRO MET MET ARG GLY ARG ASN SER ALA ILE VAL
SEQRES 12 B 261 ALA LEU SER TYR LEU GLY ALA VAL ARG ALA ILE PRO ASN
SEQRES 13 B 261 TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU GLU ALA
SEQRES 14 B 261 GLY ILE ARG PHE THR ALA ALA CYS LEU GLY LYS GLU GLY
SEQRES 15 B 261 ILE ARG CYS ASN GLY ILE SER ALA GLY PRO ILE LYS THR
SEQRES 16 B 261 LEU ALA ALA SER GLY ILE ALA ASP PHE GLY LYS LEU LEU
SEQRES 17 B 261 GLY HIS VAL ALA ALA HIS ASN PRO LEU ARG ARG ASN VAL
SEQRES 18 B 261 THR ILE GLU GLU VAL GLY ASN THR ALA ALA PHE LEU LEU
SEQRES 19 B 261 SER ASP LEU SER SER GLY ILE THR GLY GLU ILE THR TYR
SEQRES 20 B 261 VAL ASP GLY GLY TYR SER ILE ASN ALA LEU SER THR GLU
SEQRES 21 B 261 GLY
HET NAD A 301 44
HET NAD B 301 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 5 HOH *260(H2 O)
HELIX 1 1 SER A 19 GLN A 31 1 13
HELIX 2 2 VAL A 41 LYS A 43 5 3
HELIX 3 3 LEU A 44 LEU A 55 1 12
HELIX 4 4 SER A 67 GLY A 79 1 13
HELIX 5 5 PRO A 96 SER A 101 5 6
HELIX 6 6 ASP A 103 ILE A 108 1 6
HELIX 7 7 SER A 109 ALA A 121 1 13
HELIX 8 8 TYR A 122 ARG A 136 1 15
HELIX 9 9 TYR A 147 VAL A 151 5 5
HELIX 10 10 ASN A 158 GLY A 179 1 22
HELIX 11 11 ALA A 197 ILE A 201 5 5
HELIX 12 12 ASP A 203 ASN A 215 1 13
HELIX 13 13 THR A 222 SER A 235 1 14
HELIX 14 14 ASP A 236 SER A 239 5 4
HELIX 15 15 GLY A 251 ASN A 255 5 5
HELIX 16 16 SER B 19 GLN B 31 1 13
HELIX 17 17 VAL B 41 LYS B 43 5 3
HELIX 18 18 LEU B 44 LEU B 55 1 12
HELIX 19 19 SER B 67 GLY B 79 1 13
HELIX 20 20 PRO B 96 SER B 101 5 6
HELIX 21 21 ASP B 103 ILE B 108 1 6
HELIX 22 22 SER B 109 ALA B 121 1 13
HELIX 23 23 TYR B 122 ARG B 136 1 15
HELIX 24 24 TYR B 147 VAL B 151 5 5
HELIX 25 25 ASN B 158 GLY B 179 1 22
HELIX 26 26 LYS B 206 ASN B 215 1 10
HELIX 27 27 THR B 222 SER B 235 1 14
HELIX 28 28 ASP B 236 SER B 239 5 4
HELIX 29 29 GLY B 251 ASN B 255 5 5
SHEET 1 A 7 VAL A 60 ARG A 62 0
SHEET 2 A 7 GLU A 34 TYR A 39 1 N PHE A 37 O PHE A 61
SHEET 3 A 7 LYS A 8 ILE A 11 1 N ILE A 11 O ALA A 36
SHEET 4 A 7 GLY A 87 HIS A 90 1 O GLY A 87 N LEU A 10
SHEET 5 A 7 SER A 140 SER A 146 1 O VAL A 143 N HIS A 90
SHEET 6 A 7 ILE A 183 ALA A 190 1 O ILE A 188 N SER A 146
SHEET 7 A 7 ILE A 245 VAL A 248 1 O THR A 246 N GLY A 187
SHEET 1 B 7 VAL B 60 ARG B 62 0
SHEET 2 B 7 GLU B 34 TYR B 39 1 N PHE B 37 O PHE B 61
SHEET 3 B 7 LYS B 8 ILE B 11 1 N ILE B 11 O ALA B 36
SHEET 4 B 7 GLY B 87 HIS B 90 1 O GLY B 87 N LEU B 10
SHEET 5 B 7 SER B 140 SER B 146 1 O VAL B 143 N HIS B 90
SHEET 6 B 7 ILE B 183 ALA B 190 1 O ILE B 188 N SER B 146
SHEET 7 B 7 ILE B 245 VAL B 248 1 O THR B 246 N GLY B 187
SITE 1 AC1 30 GLY A 13 ILE A 15 SER A 19 ILE A 20
SITE 2 AC1 30 VAL A 40 CYS A 63 ASP A 64 VAL A 65
SITE 3 AC1 30 SER A 91 ILE A 92 GLY A 93 ILE A 119
SITE 4 AC1 30 LEU A 145 SER A 146 LYS A 164 ALA A 190
SITE 5 AC1 30 GLY A 191 PRO A 192 ILE A 193 THR A 195
SITE 6 AC1 30 LEU A 196 ALA A 197 HOH A 401 HOH A 404
SITE 7 AC1 30 HOH A 413 HOH A 426 HOH A 433 HOH A 434
SITE 8 AC1 30 HOH A 504 HOH A 533
SITE 1 AC2 26 GLY B 13 ILE B 15 SER B 19 ILE B 20
SITE 2 AC2 26 VAL B 40 CYS B 63 ASP B 64 VAL B 65
SITE 3 AC2 26 SER B 91 ILE B 92 GLY B 93 ILE B 119
SITE 4 AC2 26 LEU B 145 SER B 146 TYR B 147 LYS B 164
SITE 5 AC2 26 ALA B 190 GLY B 191 PRO B 192 ILE B 193
SITE 6 AC2 26 HOH B 411 HOH B 418 HOH B 422 HOH B 460
SITE 7 AC2 26 HOH B 475 HOH B 514
CRYST1 91.100 91.100 240.840 90.00 90.00 120.00 P 61 2 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 0.010977 0.006338 0.000000 0.00000
SCALE2 0.000000 0.012675 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
