HEADER TRANSFERASE 31-JUL-11 3T7V
TITLE CRYSTAL STRUCTURE OF METHYLORNITHINE SYNTHASE (PYLB)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLORNITHINE SYNTHASE PYLB;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.8.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOSARCINA BARKERI;
SOURCE 3 ORGANISM_TAXID: 269797;
SOURCE 4 STRAIN: FUSARO / DSM 804;
SOURCE 5 GENE: MBAR_A0838;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SOLUBL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B:SUMO
KEYWDS TIM-BARREL FOLD, MUTASE, [4FE-4S]-CLUSTER, SAM, LYSINE, 3-
KEYWDS 2 METHYLORNITHINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.QUITTERER,A.LIST,W.EISENREICH,A.BACHER,M.GROLL
REVDAT 3 28-FEB-24 3T7V 1 REMARK LINK
REVDAT 2 18-APR-12 3T7V 1 JRNL
REVDAT 1 30-NOV-11 3T7V 0
JRNL AUTH F.QUITTERER,A.LIST,W.EISENREICH,A.BACHER,M.GROLL
JRNL TITL CRYSTAL STRUCTURE OF METHYLORNITHINE SYNTHASE (PYLB):
JRNL TITL 2 INSIGHTS INTO THE PYRROLYSINE BIOSYNTHESIS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 51 1339 2012
JRNL REFN ISSN 1433-7851
JRNL PMID 22095926
JRNL DOI 10.1002/ANIE.201106765
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 55170
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) : 0.130
REMARK 3 R VALUE (WORKING SET) : 0.129
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2904
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3718
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.1610
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.2210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2699
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.01000
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): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.977
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2804 ; 0.029 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3828 ; 2.576 ; 2.016
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 336 ; 5.960 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;35.165 ;23.676
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 510 ;12.872 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;15.308 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 420 ; 0.289 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2096 ; 0.013 ; 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): 1683 ; 1.418 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2713 ; 2.529 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1115 ; 3.188 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1055 ; 4.963 ; 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): 2802 ; 8.312 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 101 ;36.259 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2963 ;14.847 ; 5.000
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 : 8
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 12 A 29
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2078 45.9911 28.9195
REMARK 3 T TENSOR
REMARK 3 T11: 0.1772 T22: 0.1565
REMARK 3 T33: 0.0916 T12: -0.1108
REMARK 3 T13: 0.0424 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 2.1219 L22: 1.0135
REMARK 3 L33: 1.7544 L12: 1.4642
REMARK 3 L13: -1.9274 L23: -1.3329
REMARK 3 S TENSOR
REMARK 3 S11: 0.3563 S12: -0.3783 S13: -0.0018
REMARK 3 S21: 0.2763 S22: -0.3039 S23: 0.0149
REMARK 3 S31: -0.3578 S32: 0.3388 S33: -0.0524
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 30 A 80
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2500 45.5562 9.4658
REMARK 3 T TENSOR
REMARK 3 T11: 0.1022 T22: 0.0972
REMARK 3 T33: 0.1020 T12: 0.0061
REMARK 3 T13: 0.0194 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.2413 L22: 0.3478
REMARK 3 L33: 0.4797 L12: 0.1358
REMARK 3 L13: -0.2493 L23: 0.0998
REMARK 3 S TENSOR
REMARK 3 S11: 0.0454 S12: 0.0453 S13: 0.0781
REMARK 3 S21: 0.0105 S22: 0.0326 S23: 0.0632
REMARK 3 S31: -0.0460 S32: -0.0186 S33: -0.0780
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 81 A 188
REMARK 3 ORIGIN FOR THE GROUP (A): 57.8270 33.5713 -1.0695
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.1080
REMARK 3 T33: 0.0936 T12: -0.0135
REMARK 3 T13: -0.0001 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.2894 L22: 0.2517
REMARK 3 L33: 0.1410 L12: 0.1652
REMARK 3 L13: -0.1340 L23: -0.0352
REMARK 3 S TENSOR
REMARK 3 S11: -0.0193 S12: 0.0281 S13: -0.0202
REMARK 3 S21: 0.0213 S22: 0.0291 S23: -0.0326
REMARK 3 S31: 0.0010 S32: -0.0075 S33: -0.0098
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 189 A 195
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8764 27.1283 12.5373
REMARK 3 T TENSOR
REMARK 3 T11: 0.1211 T22: 0.1454
REMARK 3 T33: 0.1075 T12: -0.0006
REMARK 3 T13: -0.0155 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.3160 L22: 2.2931
REMARK 3 L33: 0.3403 L12: 0.8319
REMARK 3 L13: -0.3168 L23: -0.8818
REMARK 3 S TENSOR
REMARK 3 S11: 0.0243 S12: -0.0515 S13: -0.0659
REMARK 3 S21: 0.1032 S22: -0.0557 S23: -0.1013
REMARK 3 S31: -0.0436 S32: 0.0066 S33: 0.0315
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 196 A 232
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6308 34.4005 15.3123
REMARK 3 T TENSOR
REMARK 3 T11: 0.1247 T22: 0.1179
REMARK 3 T33: 0.1001 T12: -0.0067
REMARK 3 T13: 0.0024 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.7979 L22: 0.0567
REMARK 3 L33: 0.1480 L12: 0.0300
REMARK 3 L13: -0.2879 L23: -0.0491
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: -0.0104 S13: 0.0183
REMARK 3 S21: 0.0615 S22: 0.0028 S23: 0.0015
REMARK 3 S31: -0.0140 S32: -0.0016 S33: -0.0128
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 233 A 247
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8590 37.0055 2.2791
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.1310
REMARK 3 T33: 0.0976 T12: -0.0103
REMARK 3 T13: 0.0044 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.3317 L22: 0.0848
REMARK 3 L33: 1.0723 L12: 0.1046
REMARK 3 L13: 0.3705 L23: 0.2767
REMARK 3 S TENSOR
REMARK 3 S11: -0.0260 S12: 0.0297 S13: 0.0900
REMARK 3 S21: 0.0216 S22: -0.0059 S23: 0.0257
REMARK 3 S31: -0.0233 S32: -0.0843 S33: 0.0319
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 248 A 295
REMARK 3 ORIGIN FOR THE GROUP (A): 42.8931 46.0338 10.5190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.1015
REMARK 3 T33: 0.1081 T12: 0.0070
REMARK 3 T13: 0.0254 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.4370 L22: 0.4133
REMARK 3 L33: 0.3436 L12: 0.2351
REMARK 3 L13: -0.3016 L23: 0.0340
REMARK 3 S TENSOR
REMARK 3 S11: 0.1033 S12: 0.0393 S13: 0.1311
REMARK 3 S21: 0.0870 S22: -0.0113 S23: 0.0809
REMARK 3 S31: -0.0461 S32: -0.0462 S33: -0.0921
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 296 A 348
REMARK 3 RESIDUE RANGE : A 991 A 993
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7392 50.0544 -0.5622
REMARK 3 T TENSOR
REMARK 3 T11: 0.1087 T22: 0.0961
REMARK 3 T33: 0.1130 T12: 0.0101
REMARK 3 T13: 0.0091 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 0.3860 L22: 0.6400
REMARK 3 L33: 0.0974 L12: 0.3218
REMARK 3 L13: -0.1349 L23: 0.0226
REMARK 3 S TENSOR
REMARK 3 S11: 0.0377 S12: 0.0694 S13: 0.0879
REMARK 3 S21: 0.0136 S22: 0.0142 S23: 0.0516
REMARK 3 S31: -0.0208 S32: -0.0400 S33: -0.0519
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
REMARK 4
REMARK 4 3T7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : FIXED EXIT DOUBLE, CHANNEL DCM
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58074
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : 0.52500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HYDROCHLORIDE, 200 MM
REMARK 280 MGCL2, 25% PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 69.96667
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 34.98333
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 34.98333
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 69.96667
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ILE A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 4
REMARK 465 MET A 5
REMARK 465 ALA A 6
REMARK 465 LEU A 7
REMARK 465 ASP A 8
REMARK 465 GLU A 9
REMARK 465 PHE A 10
REMARK 465 ASP A 11
REMARK 465 GLY A 349
REMARK 465 CYS A 350
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 O HOH A 431 O HOH A 650 1.61
REMARK 500 O HOH A 595 O HOH A 650 2.13
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 650 O HOH A 660 5565 2.04
REMARK 500 O HOH A 650 O HOH A 661 5565 2.08
REMARK 500 OE1 GLN A 306 O HOH A 551 6764 2.17
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 LEU A 23 CB - CG - CD1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 MET A 150 CB - CG - SD ANGL. DEV. = -20.1 DEGREES
REMARK 500 LYS A 180 CD - CE - NZ ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 MET A 226 CG - SD - CE ANGL. DEV. = -16.2 DEGREES
REMARK 500 MET A 237 CG - SD - CE ANGL. DEV. = 11.2 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 GLU A 171 -49.54 76.62
REMARK 500 LEU A 181 -67.25 -98.45
REMARK 500 LYS A 253 52.68 -103.06
REMARK 500 GLU A 281 10.59 -150.66
REMARK 500 ASP A 304 -106.53 73.58
REMARK 500 SER A 305 124.79 60.74
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 SF4 A 991 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 71 SG
REMARK 620 2 SF4 A 991 S1 119.1
REMARK 620 3 SF4 A 991 S3 104.8 103.5
REMARK 620 4 SF4 A 991 S4 115.7 104.9 107.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 991 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 75 SG
REMARK 620 2 SF4 A 991 S1 107.1
REMARK 620 3 SF4 A 991 S2 114.1 107.3
REMARK 620 4 SF4 A 991 S3 118.0 104.6 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 991 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 78 SG
REMARK 620 2 SF4 A 991 S1 108.6
REMARK 620 3 SF4 A 991 S2 109.5 106.9
REMARK 620 4 SF4 A 991 S4 121.5 104.3 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 991 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SAM A 992 O
REMARK 620 2 SF4 A 991 S2 92.1
REMARK 620 3 SF4 A 991 S3 90.0 100.2
REMARK 620 4 SF4 A 991 S4 161.4 98.2 103.3
REMARK 620 5 SAM A 992 N 76.0 157.9 98.4 89.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 991
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 992
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MD0 A 993
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R30 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN SYNTHASE
REMARK 900 RELATED ID: 3CIW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYDE
DBREF 3T7V A 1 350 UNP Q46E78 Q46E78_METBF 1 350
SEQRES 1 A 350 MET ILE GLN LYS MET ALA LEU ASP GLU PHE ASP SER LEU
SEQRES 2 A 350 GLY ASP LYS VAL ILE GLU GLY TYR GLN LEU THR ASP ASN
SEQRES 3 A 350 ASP LEU ARG THR LEU LEU SER LEU GLU SER LYS GLU GLY
SEQRES 4 A 350 LEU GLU ARG LEU TYR SER ALA ALA ARG LYS VAL ARG ASP
SEQRES 5 A 350 HIS TYR PHE GLY ASN ARG VAL PHE LEU ASN CYS PHE ILE
SEQRES 6 A 350 TYR PHE SER THR TYR CYS LYS ASN GLN CYS SER PHE CYS
SEQRES 7 A 350 TYR TYR ASN CYS ARG ASN GLU ILE ASN ARG TYR ARG LEU
SEQRES 8 A 350 THR MET GLU GLU ILE LYS GLU THR CYS LYS THR LEU LYS
SEQRES 9 A 350 GLY ALA GLY PHE HIS MET VAL ASP LEU THR MET GLY GLU
SEQRES 10 A 350 ASP PRO TYR TYR TYR GLU ASP PRO ASN ARG PHE VAL GLU
SEQRES 11 A 350 LEU VAL GLN ILE VAL LYS GLU GLU LEU GLY LEU PRO ILE
SEQRES 12 A 350 MET ILE SER PRO GLY LEU MET ASP ASN ALA THR LEU LEU
SEQRES 13 A 350 LYS ALA ARG GLU LYS GLY ALA ASN PHE LEU ALA LEU TYR
SEQRES 14 A 350 GLN GLU THR TYR ASP THR GLU LEU TYR ARG LYS LEU ARG
SEQRES 15 A 350 VAL GLY GLN SER PHE ASP GLY ARG VAL ASN ALA ARG ARG
SEQRES 16 A 350 PHE ALA LYS GLN GLN GLY TYR CYS VAL GLU ASP GLY ILE
SEQRES 17 A 350 LEU THR GLY VAL GLY ASN ASP ILE GLU SER THR ILE LEU
SEQRES 18 A 350 SER LEU ARG GLY MET SER THR ASN ASP PRO ASP MET VAL
SEQRES 19 A 350 ARG VAL MET THR PHE LEU PRO GLN GLU GLY THR PRO LEU
SEQRES 20 A 350 GLU GLY PHE ARG ASP LYS SER ASN LEU SER GLU LEU LYS
SEQRES 21 A 350 ILE ILE SER VAL LEU ARG LEU MET PHE PRO LYS ARG LEU
SEQRES 22 A 350 ILE PRO ALA SER LEU ASP LEU GLU GLY ILE ASP GLY MET
SEQRES 23 A 350 VAL LEU ARG LEU ASN ALA GLY ALA ASN ILE VAL THR SER
SEQRES 24 A 350 ILE LEU PRO PRO ASP SER GLN LEU GLU GLY VAL ALA ASN
SEQRES 25 A 350 TYR ASP ARG ASP LEU GLU GLU ARG ASP ARG ASP ILE LYS
SEQRES 26 A 350 SER VAL VAL ARG ARG LEU GLU ILE MET GLY MET LYS PRO
SEQRES 27 A 350 ALA ARG GLN ALA ASP PHE GLU ALA VAL LEU GLY CYS
HET SF4 A 991 8
HET SAM A 992 31
HET MD0 A 993 10
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM SAM S-ADENOSYLMETHIONINE
HETNAM MD0 5-AMINO-D-ISOLEUCINE
FORMUL 2 SF4 FE4 S4
FORMUL 3 SAM C15 H22 N6 O5 S
FORMUL 4 MD0 C6 H14 N2 O2
FORMUL 5 HOH *315(H2 O)
HELIX 1 1 SER A 12 GLU A 19 1 8
HELIX 2 2 THR A 24 SER A 33 1 10
HELIX 3 3 SER A 36 GLY A 56 1 21
HELIX 4 4 THR A 92 LYS A 104 1 13
HELIX 5 5 ASP A 118 ASP A 124 1 7
HELIX 6 6 PRO A 125 GLY A 140 1 16
HELIX 7 7 ASP A 151 LYS A 161 1 11
HELIX 8 8 ASP A 174 ARG A 182 1 9
HELIX 9 9 SER A 186 GLN A 200 1 15
HELIX 10 10 ASP A 215 ASN A 229 1 15
HELIX 11 11 SER A 257 PHE A 269 1 13
HELIX 12 12 LEU A 278 ALA A 292 1 15
HELIX 13 13 ASP A 323 GLY A 335 1 13
HELIX 14 14 ARG A 340 ALA A 346 1 7
SHEET 1 A 8 MET A 233 THR A 238 0
SHEET 2 A 8 CYS A 203 THR A 210 1 N THR A 210 O MET A 237
SHEET 3 A 8 ALA A 163 ALA A 167 1 N ASN A 164 O CYS A 203
SHEET 4 A 8 ILE A 143 SER A 146 1 N ILE A 145 O ALA A 167
SHEET 5 A 8 MET A 110 MET A 115 1 N VAL A 111 O MET A 144
SHEET 6 A 8 ARG A 58 SER A 68 1 N CYS A 63 O ASP A 112
SHEET 7 A 8 ILE A 296 ILE A 300 1 O ILE A 300 N PHE A 64
SHEET 8 A 8 PRO A 275 SER A 277 1 N ALA A 276 O ILE A 296
SHEET 1 B 7 MET A 233 THR A 238 0
SHEET 2 B 7 CYS A 203 THR A 210 1 N THR A 210 O MET A 237
SHEET 3 B 7 ALA A 163 ALA A 167 1 N ASN A 164 O CYS A 203
SHEET 4 B 7 ILE A 143 SER A 146 1 N ILE A 145 O ALA A 167
SHEET 5 B 7 MET A 110 MET A 115 1 N VAL A 111 O MET A 144
SHEET 6 B 7 ARG A 58 SER A 68 1 N CYS A 63 O ASP A 112
SHEET 7 B 7 LYS A 337 PRO A 338 1 O LYS A 337 N VAL A 59
LINK SG CYS A 71 FE2 SF4 A 991 1555 1555 2.29
LINK SG CYS A 75 FE4 SF4 A 991 1555 1555 2.34
LINK SG CYS A 78 FE3 SF4 A 991 1555 1555 2.33
LINK FE1 SF4 A 991 O SAM A 992 1555 1555 2.18
LINK FE1 SF4 A 991 N SAM A 992 1555 1555 2.18
SITE 1 AC1 7 CYS A 71 ASN A 73 CYS A 75 CYS A 78
SITE 2 AC1 7 ASN A 81 ARG A 182 SAM A 992
SITE 1 AC2 19 PHE A 77 THR A 114 MET A 115 TYR A 169
SITE 2 AC2 19 GLU A 171 ARG A 182 ARG A 190 LEU A 209
SITE 3 AC2 19 MET A 237 THR A 238 PHE A 239 LEU A 240
SITE 4 AC2 19 GLN A 242 VAL A 310 HOH A 354 HOH A 359
SITE 5 AC2 19 HOH A 363 SF4 A 991 MD0 A 993
SITE 1 AC3 12 PHE A 64 ASP A 112 SER A 146 TYR A 169
SITE 2 AC3 12 ARG A 235 SER A 277 ASP A 279 THR A 298
SITE 3 AC3 12 SER A 299 HOH A 357 HOH A 362 SAM A 992
CRYST1 77.020 77.020 104.950 90.00 90.00 120.00 P 32 2 1 6
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 0.012984 0.007496 0.000000 0.00000
SCALE2 0.000000 0.014992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009528 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
