HEADER OXIDOREDUCTASE 12-SEP-13 4MP6
TITLE STAPHYLOFERRIN B PRECURSOR BIOSYNTHETIC ENZYME SBNB BOUND TO CITRATE
TITLE 2 AND NAD+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ORNITHINE CYCLODEAMINASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE 3 ORGANISM_TAXID: 196620;
SOURCE 4 STRAIN: NEWMAN;
SOURCE 5 GENE: SBNB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS SIDEROPHORE, L-DAP SYNTHESIS, ACEGA DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.GRIGG,M.J.KOBYLARZ,D.K.RAI,M.E.P.MURPHY
REVDAT 4 28-FEB-24 4MP6 1 REMARK SEQADV
REVDAT 3 15-NOV-17 4MP6 1 REMARK
REVDAT 2 09-APR-14 4MP6 1 JRNL
REVDAT 1 05-MAR-14 4MP6 0
JRNL AUTH M.J.KOBYLARZ,J.C.GRIGG,S.J.TAKAYAMA,D.K.RAI,D.E.HEINRICHS,
JRNL AUTH 2 M.E.MURPHY
JRNL TITL SYNTHESIS OF L-2,3-DIAMINOPROPIONIC ACID, A SIDEROPHORE AND
JRNL TITL 2 ANTIBIOTIC PRECURSOR.
JRNL REF CHEM.BIOL. V. 21 379 2014
JRNL REFN ISSN 1074-5521
JRNL PMID 24485762
JRNL DOI 10.1016/J.CHEMBIOL.2013.12.011
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 58.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19067
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 981
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) : 1289
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2637
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 129
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : 1.05000
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): 0.264
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.844
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2802 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3811 ; 1.468 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 344 ; 6.496 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;40.247 ;25.290
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 482 ;16.609 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;20.323 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 419 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2150 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1364 ; 0.800 ; 0.978
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1712 ; 1.440 ; 1.464
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1438 ; 0.826 ; 1.178
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
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 3 A 45
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1204 4.5618 -11.1264
REMARK 3 T TENSOR
REMARK 3 T11: 0.2396 T22: 0.2104
REMARK 3 T33: 0.2230 T12: -0.0226
REMARK 3 T13: 0.0045 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.8872 L22: 0.4626
REMARK 3 L33: 0.5128 L12: -0.1754
REMARK 3 L13: 0.4548 L23: 0.0738
REMARK 3 S TENSOR
REMARK 3 S11: -0.0434 S12: 0.2202 S13: 0.2699
REMARK 3 S21: -0.0269 S22: 0.0086 S23: -0.0130
REMARK 3 S31: 0.0771 S32: 0.0351 S33: 0.0348
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 : A 46 A 97
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6797 -0.6829 4.6248
REMARK 3 T TENSOR
REMARK 3 T11: 0.2101 T22: 0.3109
REMARK 3 T33: 0.2469 T12: 0.0654
REMARK 3 T13: 0.0261 T23: -0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 0.3326 L22: 1.3163
REMARK 3 L33: 2.7244 L12: 0.5357
REMARK 3 L13: -0.0207 L23: 1.0391
REMARK 3 S TENSOR
REMARK 3 S11: -0.0080 S12: -0.0059 S13: 0.1143
REMARK 3 S21: -0.0601 S22: -0.0920 S23: 0.2493
REMARK 3 S31: -0.0066 S32: -0.3334 S33: 0.1001
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 98 A 168
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9408 9.5846 -8.4410
REMARK 3 T TENSOR
REMARK 3 T11: 0.2723 T22: 0.2496
REMARK 3 T33: 0.2494 T12: -0.0224
REMARK 3 T13: -0.0515 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 3.0770 L22: 0.5636
REMARK 3 L33: 0.2197 L12: -1.1848
REMARK 3 L13: -0.2237 L23: 0.0022
REMARK 3 S TENSOR
REMARK 3 S11: -0.2632 S12: 0.0453 S13: 0.3409
REMARK 3 S21: 0.0522 S22: 0.1392 S23: -0.1721
REMARK 3 S31: 0.0782 S32: -0.0641 S33: 0.1240
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 169 A 258
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4723 10.9383 -0.8285
REMARK 3 T TENSOR
REMARK 3 T11: 0.2640 T22: 0.2880
REMARK 3 T33: 0.2175 T12: 0.0483
REMARK 3 T13: -0.0072 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 2.7075 L22: 1.3182
REMARK 3 L33: 0.5480 L12: -1.2455
REMARK 3 L13: -0.0082 L23: 0.4591
REMARK 3 S TENSOR
REMARK 3 S11: -0.6096 S12: -0.1918 S13: 0.0264
REMARK 3 S21: 0.2822 S22: 0.3919 S23: 0.1537
REMARK 3 S31: 0.0475 S32: -0.0085 S33: 0.2177
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 259 A 274
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6425 -11.5748 -0.9167
REMARK 3 T TENSOR
REMARK 3 T11: 0.2935 T22: 0.0471
REMARK 3 T33: 0.9416 T12: 0.0929
REMARK 3 T13: 0.4321 T23: 0.1810
REMARK 3 L TENSOR
REMARK 3 L11: 0.3281 L22: 23.7804
REMARK 3 L33: 0.0013 L12: -2.7690
REMARK 3 L13: 0.0191 L23: -0.1525
REMARK 3 S TENSOR
REMARK 3 S11: -0.2126 S12: -0.0439 S13: -0.0519
REMARK 3 S21: 1.3602 S22: 0.2482 S23: -0.1696
REMARK 3 S31: -0.0167 S32: -0.0052 S33: -0.0356
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 275 A 336
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4381 1.7208 -12.9418
REMARK 3 T TENSOR
REMARK 3 T11: 0.2541 T22: 0.2311
REMARK 3 T33: 0.2288 T12: -0.0331
REMARK 3 T13: 0.0065 T23: -0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 2.9774 L22: 0.3031
REMARK 3 L33: 0.1440 L12: -0.4651
REMARK 3 L13: 0.2495 L23: -0.0072
REMARK 3 S TENSOR
REMARK 3 S11: -0.1772 S12: 0.2467 S13: -0.3053
REMARK 3 S21: -0.0644 S22: 0.0537 S23: 0.0611
REMARK 3 S31: -0.0052 S32: 0.0352 S33: 0.1235
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4MP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082191.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 1.00000
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL; ASYMMETRIC CUT
REMARK 200 4.9650 DEG.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19090
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 58.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM CITRATE TRIBASIC, PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 78.53950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.33000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.33000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.26975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.33000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.33000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 117.80925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.33000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.33000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.26975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.33000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.33000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.80925
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 78.53950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
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 NH2 ARG A 10 OG SER A 116 2.07
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 GLN A 42 86.55 -154.13
REMARK 500 ASN A 234 59.87 -92.73
REMARK 500 ILE A 237 -56.39 73.21
REMARK 500 ASN A 260 31.40 -88.46
REMARK 500 LYS A 263 47.50 -87.95
REMARK 500 GLU A 272 -167.21 -73.17
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 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M54 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH N-(1-AMINO-1-CARBOXYL-2-ETHYL)-
REMARK 900 GLUTAMIC ACID AND NADH
REMARK 900 RELATED ID: 4MP3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN APO SELENOMETHIONINE
REMARK 900 RELATED ID: 4MP8 RELATED DB: PDB
REMARK 900 RELATED ID: 4MPD RELATED DB: PDB
DBREF 4MP6 A 1 336 UNP Q8NYS7 Q8NYS7_STAAW 1 336
SEQADV 4MP6 GLY A -2 UNP Q8NYS7 EXPRESSION TAG
SEQADV 4MP6 SER A -1 UNP Q8NYS7 EXPRESSION TAG
SEQADV 4MP6 HIS A 0 UNP Q8NYS7 EXPRESSION TAG
SEQRES 1 A 339 GLY SER HIS MET ASN ARG GLU MET LEU TYR LEU ASN ARG
SEQRES 2 A 339 SER ASP ILE GLU GLN ALA GLY GLY ASN HIS SER GLN VAL
SEQRES 3 A 339 TYR VAL ASP ALA LEU THR GLU ALA LEU THR ALA HIS ALA
SEQRES 4 A 339 HIS ASN ASP PHE VAL GLN PRO LEU LYS PRO TYR LEU ARG
SEQRES 5 A 339 GLN ASP PRO GLU ASN GLY HIS ILE ALA ASP ARG ILE ILE
SEQRES 6 A 339 ALA MET PRO SER HIS ILE GLY GLY GLU HIS ALA ILE SER
SEQRES 7 A 339 GLY ILE LYS TRP ILE GLY SER LYS HIS ASP ASN PRO SER
SEQRES 8 A 339 LYS ARG ASN MET GLU ARG ALA SER GLY VAL ILE ILE LEU
SEQRES 9 A 339 ASN ASP PRO GLU THR ASN TYR PRO ILE ALA VAL MET GLU
SEQRES 10 A 339 ALA SER LEU ILE SER SER MET ARG THR ALA ALA VAL SER
SEQRES 11 A 339 VAL ILE ALA ALA LYS HIS LEU ALA LYS LYS GLY PHE LYS
SEQRES 12 A 339 ASP LEU THR ILE ILE GLY CYS GLY LEU ILE GLY ASP LYS
SEQRES 13 A 339 GLN LEU GLN SER MET LEU GLU GLN PHE ASP HIS ILE GLU
SEQRES 14 A 339 ARG VAL PHE VAL TYR ASP GLN PHE SER GLU ALA CYS ALA
SEQRES 15 A 339 ARG PHE VAL ASP ARG TRP GLN GLN GLN ARG PRO GLU ILE
SEQRES 16 A 339 ASN PHE ILE ALA THR GLU ASN ALA LYS GLU ALA VAL SER
SEQRES 17 A 339 ASN GLY GLU VAL VAL ILE THR CYS THR VAL THR ASP GLN
SEQRES 18 A 339 PRO TYR ILE GLU TYR ASP TRP LEU GLN LYS GLY ALA PHE
SEQRES 19 A 339 ILE SER ASN ILE SER ILE MET ASP VAL HIS LYS GLU VAL
SEQRES 20 A 339 PHE ILE LYS ALA ASP LYS VAL VAL VAL ASP ASP TRP SER
SEQRES 21 A 339 GLN CYS ASN ARG GLU LYS LYS THR ILE ASN GLN LEU VAL
SEQRES 22 A 339 LEU GLU GLY LYS PHE SER LYS GLU ALA LEU HIS ALA GLU
SEQRES 23 A 339 LEU GLY GLN LEU VAL THR GLY ASP ILE PRO GLY ARG GLU
SEQRES 24 A 339 ASP ASP ASP GLU ILE ILE LEU LEU ASN PRO MET GLY MET
SEQRES 25 A 339 ALA ILE GLU ASP ILE SER SER ALA TYR PHE ILE TYR GLN
SEQRES 26 A 339 GLN ALA GLN GLN GLN ASN ILE GLY THR THR LEU ASN LEU
SEQRES 27 A 339 TYR
HET NAD A 400 44
HET CIT A 401 13
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM CIT CITRIC ACID
FORMUL 2 NAD C21 H27 N7 O14 P2
FORMUL 3 CIT C6 H8 O7
FORMUL 4 HOH *129(H2 O)
HELIX 1 1 ASN A 9 ALA A 16 1 8
HELIX 2 2 SER A 21 HIS A 37 1 17
HELIX 3 3 ASP A 85 ASN A 91 1 7
HELIX 4 4 ALA A 115 ALA A 135 1 21
HELIX 5 5 GLY A 148 PHE A 162 1 15
HELIX 6 6 PHE A 174 ARG A 189 1 16
HELIX 7 7 ASN A 199 ASN A 206 1 8
HELIX 8 8 GLU A 222 LEU A 226 5 5
HELIX 9 9 HIS A 241 ALA A 248 1 8
HELIX 10 10 LYS A 264 GLU A 272 1 9
HELIX 11 11 LEU A 284 THR A 289 1 6
HELIX 12 12 MET A 309 GLN A 327 1 19
SHEET 1 A 3 PHE A 40 VAL A 41 0
SHEET 2 A 3 ARG A 60 ILE A 68 -1 O HIS A 67 N VAL A 41
SHEET 3 A 3 TYR A 47 LEU A 48 -1 N LEU A 48 O ILE A 61
SHEET 1 B 7 PHE A 40 VAL A 41 0
SHEET 2 B 7 ARG A 60 ILE A 68 -1 O HIS A 67 N VAL A 41
SHEET 3 B 7 ILE A 74 SER A 82 -1 O GLY A 76 N SER A 66
SHEET 4 B 7 ALA A 95 ASN A 102 -1 O VAL A 98 N TRP A 79
SHEET 5 B 7 PRO A 109 GLU A 114 -1 O ILE A 110 N LEU A 101
SHEET 6 B 7 GLU A 4 LEU A 8 1 N LEU A 8 O GLU A 114
SHEET 7 B 7 THR A 331 ASN A 334 -1 O THR A 331 N TYR A 7
SHEET 1 C 8 ASN A 193 ALA A 196 0
SHEET 2 C 8 ARG A 167 TYR A 171 1 N VAL A 170 O ILE A 195
SHEET 3 C 8 ASP A 141 ILE A 145 1 N LEU A 142 O PHE A 169
SHEET 4 C 8 VAL A 209 THR A 212 1 O VAL A 209 N THR A 143
SHEET 5 C 8 PHE A 231 SER A 233 1 O SER A 233 N VAL A 210
SHEET 6 C 8 ILE A 302 ASN A 305 1 O LEU A 304 N ILE A 232
SHEET 7 C 8 LYS A 250 VAL A 253 1 N VAL A 252 O LEU A 303
SHEET 8 C 8 ALA A 282 GLU A 283 1 O ALA A 282 N VAL A 253
SITE 1 AC1 25 HIS A 37 ARG A 94 ARG A 122 THR A 123
SITE 2 AC1 25 GLY A 146 GLY A 148 LEU A 149 ILE A 150
SITE 3 AC1 25 ASP A 172 GLN A 173 CYS A 213 THR A 214
SITE 4 AC1 25 VAL A 215 ILE A 235 PRO A 306 GLY A 308
SITE 5 AC1 25 CIT A 401 HOH A 505 HOH A 529 HOH A 535
SITE 6 AC1 25 HOH A 540 HOH A 549 HOH A 572 HOH A 597
SITE 7 AC1 25 HOH A 618
SITE 1 AC2 11 LYS A 45 ARG A 60 ILE A 62 MET A 64
SITE 2 AC2 11 LYS A 78 ARG A 94 ARG A 122 GLY A 308
SITE 3 AC2 11 NAD A 400 HOH A 603 HOH A 628
CRYST1 62.660 62.660 157.079 90.00 90.00 90.00 P 41 21 2 8
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 0.015959 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006366 0.00000
(ATOM LINES ARE NOT SHOWN.)
END