HEADER OXIDOREDUCTASE 15-JUL-12 4G3T
TITLE MYCOBACTERIUM SMEGMATIS DPRE1 - HEXAGONAL CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDOREDUCTASE DPRE1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 66-468;
COMPND 5 EC: 1.-.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 1772;
SOURCE 4 STRAIN: ATCC607;
SOURCE 5 GENE: MSMEG_6382;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS VAO SUPERFAMILY, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,G.JOGL
REVDAT 3 28-FEB-24 4G3T 1 REMARK
REVDAT 2 28-AUG-13 4G3T 1 JRNL
REVDAT 1 05-DEC-12 4G3T 0
JRNL AUTH H.LI,G.JOGL
JRNL TITL CRYSTAL STRUCTURE OF DECAPRENYLPHOSPHORYL-BETA- D-RIBOSE
JRNL TITL 2 2'-EPIMERASE FROM MYCOBACTERIUM SMEGMATIS.
JRNL REF PROTEINS V. 81 538 2013
JRNL REFN ISSN 0887-3585
JRNL PMID 23184707
JRNL DOI 10.1002/PROT.24220
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1000
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 28559
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.510
REMARK 3 FREE R VALUE TEST SET COUNT : 1288
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.2459 - 4.8787 0.98 3201 175 0.2025 0.2395
REMARK 3 2 4.8787 - 3.8731 1.00 3096 154 0.1812 0.1885
REMARK 3 3 3.8731 - 3.3838 1.00 3007 156 0.2299 0.2458
REMARK 3 4 3.3838 - 3.0745 1.00 3013 150 0.2669 0.3148
REMARK 3 5 3.0745 - 2.8542 1.00 3002 160 0.2494 0.3420
REMARK 3 6 2.8542 - 2.6859 1.00 2961 146 0.2775 0.3109
REMARK 3 7 2.6859 - 2.5514 1.00 2980 147 0.2768 0.3267
REMARK 3 8 2.5514 - 2.4404 1.00 3011 109 0.3135 0.3478
REMARK 3 9 2.4404 - 2.3460 0.99 3000 91 0.3239 0.3397
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 47.21
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.49550
REMARK 3 B22 (A**2) : 11.49550
REMARK 3 B33 (A**2) : -25.59660
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 2683
REMARK 3 ANGLE : 0.724 3641
REMARK 3 CHIRALITY : 0.052 400
REMARK 3 PLANARITY : 0.002 474
REMARK 3 DIHEDRAL : 10.999 964
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 85 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2571 -14.6232 14.0386
REMARK 3 T TENSOR
REMARK 3 T11: 0.5451 T22: 0.8608
REMARK 3 T33: 0.4729 T12: 0.1846
REMARK 3 T13: 0.0054 T23: -0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 0.3989 L22: 0.0562
REMARK 3 L33: 0.5898 L12: -0.1457
REMARK 3 L13: 0.0928 L23: -0.0747
REMARK 3 S TENSOR
REMARK 3 S11: 0.1020 S12: -0.4651 S13: 0.1229
REMARK 3 S21: -0.0098 S22: 0.1376 S23: -0.0139
REMARK 3 S31: -0.8355 S32: -0.4296 S33: 0.0077
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 130 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0570 -21.0770 18.4974
REMARK 3 T TENSOR
REMARK 3 T11: 0.3328 T22: 0.8081
REMARK 3 T33: 0.4879 T12: 0.0403
REMARK 3 T13: 0.0322 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.0023 L22: 0.2431
REMARK 3 L33: 0.6557 L12: 0.0976
REMARK 3 L13: 0.2364 L23: -0.0745
REMARK 3 S TENSOR
REMARK 3 S11: 0.0732 S12: -0.0736 S13: -0.0370
REMARK 3 S21: -0.1282 S22: -0.0068 S23: -0.1025
REMARK 3 S31: -0.3602 S32: -0.1308 S33: -0.0065
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 224 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0652 -24.5171 37.6700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2568 T22: 1.0336
REMARK 3 T33: 0.5914 T12: -0.0296
REMARK 3 T13: 0.0028 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.4108 L22: 0.6466
REMARK 3 L33: 0.0857 L12: -0.0011
REMARK 3 L13: -0.1955 L23: -0.0637
REMARK 3 S TENSOR
REMARK 3 S11: 0.0808 S12: -0.0094 S13: 0.1273
REMARK 3 S21: 0.1121 S22: 0.0218 S23: 0.0137
REMARK 3 S31: 0.0180 S32: -0.5832 S33: 0.1560
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 269 THROUGH 389 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5831 -20.3564 35.7082
REMARK 3 T TENSOR
REMARK 3 T11: 0.2649 T22: 0.8267
REMARK 3 T33: 0.5422 T12: 0.0871
REMARK 3 T13: 0.0148 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.4030 L22: 0.3720
REMARK 3 L33: 0.2975 L12: 0.4244
REMARK 3 L13: -0.1184 L23: -0.3348
REMARK 3 S TENSOR
REMARK 3 S11: 0.0840 S12: -0.0216 S13: 0.0441
REMARK 3 S21: 0.0341 S22: 0.0328 S23: 0.1047
REMARK 3 S31: -0.2073 S32: -0.2590 S33: 0.1267
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 390 THROUGH 416 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0190 -15.2531 40.3840
REMARK 3 T TENSOR
REMARK 3 T11: 0.4427 T22: 0.8712
REMARK 3 T33: 0.6017 T12: -0.1050
REMARK 3 T13: -0.0192 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.0621 L22: 0.0341
REMARK 3 L33: 0.5678 L12: -0.0477
REMARK 3 L13: 0.1860 L23: -0.1374
REMARK 3 S TENSOR
REMARK 3 S11: 0.1524 S12: -0.2285 S13: 0.0244
REMARK 3 S21: 0.2597 S22: -0.2701 S23: -0.0240
REMARK 3 S31: -0.5922 S32: -0.0933 S33: 0.0017
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 417 THROUGH 468 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9941 -15.4912 21.1760
REMARK 3 T TENSOR
REMARK 3 T11: -0.0688 T22: 1.3097
REMARK 3 T33: 0.5612 T12: -0.1843
REMARK 3 T13: 0.1051 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 0.8275 L22: 0.9598
REMARK 3 L33: 0.6632 L12: -0.0776
REMARK 3 L13: -0.4979 L23: -0.4468
REMARK 3 S TENSOR
REMARK 3 S11: -0.1906 S12: 0.0336 S13: -0.0687
REMARK 3 S21: 0.2915 S22: 0.1399 S23: -0.3631
REMARK 3 S31: -0.4290 S32: 0.9674 S33: -0.0454
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000073702.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28628
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.346
REMARK 200 RESOLUTION RANGE LOW (A) : 47.531
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.01200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.010
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% ISOPROPANOL, 0.2 M SODIUM
REMARK 280 CITRATE, 0.5% N,N-DIMETHYLDODECYLAMINE-N-OXIDE, PH 6.8, SITTING
REMARK 280 DROP, TEMPERATURE 277K
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 183.64133
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 91.82067
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 91.82067
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 183.64133
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 SER A 66
REMARK 465 TYR A 67
REMARK 465 GLY A 68
REMARK 465 ASP A 69
REMARK 465 ASN A 70
REMARK 465 ALA A 71
REMARK 465 GLN A 72
REMARK 465 ASN A 73
REMARK 465 GLY A 74
REMARK 465 GLY A 75
REMARK 465 GLY A 76
REMARK 465 LEU A 77
REMARK 465 VAL A 78
REMARK 465 ILE A 79
REMARK 465 ASP A 80
REMARK 465 MET A 81
REMARK 465 PRO A 82
REMARK 465 ALA A 83
REMARK 465 LEU A 84
REMARK 465 ASP A 275
REMARK 465 ALA A 276
REMARK 465 PRO A 277
REMARK 465 GLN A 278
REMARK 465 LEU A 279
REMARK 465 LEU A 280
REMARK 465 THR A 281
REMARK 465 LEU A 282
REMARK 465 PRO A 283
REMARK 465 ASP A 284
REMARK 465 ILE A 285
REMARK 465 PHE A 286
REMARK 465 PRO A 287
REMARK 465 ASN A 288
REMARK 465 GLY A 289
REMARK 465 LEU A 290
REMARK 465 ALA A 291
REMARK 465 ASN A 292
REMARK 465 LYS A 293
REMARK 465 PHE A 294
REMARK 465 THR A 295
REMARK 465 PHE A 296
REMARK 465 MET A 297
REMARK 465 PRO A 298
REMARK 465 ILE A 299
REMARK 465 GLY A 300
REMARK 465 GLU A 301
REMARK 465 LEU A 302
REMARK 465 TRP A 303
REMARK 465 TYR A 304
REMARK 465 ARG A 305
REMARK 465 LYS A 306
REMARK 465 SER A 307
REMARK 465 PRO A 323
REMARK 465 LEU A 324
REMARK 465 ASP A 325
REMARK 465 MET A 326
REMARK 465 PHE A 327
REMARK 465 GLY A 328
REMARK 465 GLU A 329
REMARK 465 TRP A 330
REMARK 465 ASN A 331
REMARK 465 ARG A 332
REMARK 465 ALA A 333
REMARK 465 TYR A 334
REMARK 465 GLY A 335
REMARK 465 SER A 336
REMARK 465 ALA A 337
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 559 O HOH A 563 1.83
REMARK 500 O HOH A 553 O HOH A 554 1.91
REMARK 500 O HOH A 550 O HOH A 552 2.17
REMARK 500 O HOH A 558 O HOH A 560 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 185 45.46 -105.23
REMARK 500 ALA A 424 -163.26 -107.41
REMARK 500 THR A 429 116.18 -165.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G3U RELATED DB: PDB
DBREF 4G3T A 66 468 UNP A0R607 A0R607_MYCS2 66 468
SEQRES 1 A 403 SER TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL
SEQRES 2 A 403 ILE ASP MET PRO ALA LEU ASN ARG ILE HIS SER ILE ASP
SEQRES 3 A 403 SER GLY THR ARG LEU VAL ASP VAL ASP ALA GLY VAL SER
SEQRES 4 A 403 LEU ASP GLN LEU MET LYS ALA ALA LEU PRO HIS GLY LEU
SEQRES 5 A 403 TRP VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL
SEQRES 6 A 403 GLY GLY ALA ILE GLY CYS ASP ILE HIS GLY LYS ASN HIS
SEQRES 7 A 403 HIS SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET
SEQRES 8 A 403 GLU LEU LEU THR ALA ASN GLY GLU VAL ARG HIS LEU THR
SEQRES 9 A 403 PRO ALA GLY PRO ASP SER ASP LEU PHE TRP ALA THR VAL
SEQRES 10 A 403 GLY GLY ASN GLY LEU THR GLY ILE ILE LEU ARG ALA THR
SEQRES 11 A 403 ILE GLU MET THR PRO THR GLU THR ALA TYR PHE ILE ALA
SEQRES 12 A 403 ASP GLY ASP VAL THR GLY SER LEU ASP GLU THR ILE ALA
SEQRES 13 A 403 PHE HIS SER ASP GLY SER GLU ALA ASN TYR THR TYR SER
SEQRES 14 A 403 SER ALA TRP PHE ASP ALA ILE SER LYS PRO PRO LYS LEU
SEQRES 15 A 403 GLY ARG ALA ALA ILE SER ARG GLY SER LEU ALA LYS LEU
SEQRES 16 A 403 ASP GLN LEU PRO SER LYS LEU GLN LYS ASP PRO LEU LYS
SEQRES 17 A 403 PHE ASP ALA PRO GLN LEU LEU THR LEU PRO ASP ILE PHE
SEQRES 18 A 403 PRO ASN GLY LEU ALA ASN LYS PHE THR PHE MET PRO ILE
SEQRES 19 A 403 GLY GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG ASN
SEQRES 20 A 403 LYS VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP
SEQRES 21 A 403 MET PHE GLY GLU TRP ASN ARG ALA TYR GLY SER ALA GLY
SEQRES 22 A 403 PHE LEU GLN TYR GLN PHE VAL VAL PRO THR GLU ALA VAL
SEQRES 23 A 403 GLU GLU PHE LYS SER ILE ILE VAL ASP ILE GLN ARG SER
SEQRES 24 A 403 GLY HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY
SEQRES 25 A 403 PRO GLY ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY
SEQRES 26 A 403 TRP ASN VAL CYS VAL ASP PHE PRO ILE LYS ALA GLY LEU
SEQRES 27 A 403 HIS GLU PHE VAL THR GLU LEU ASP ARG ARG VAL LEU GLU
SEQRES 28 A 403 PHE GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR
SEQRES 29 A 403 THR ALA GLU THR PHE HIS ALA MET TYR PRO ARG ILE ASP
SEQRES 30 A 403 GLU TRP ILE ARG ILE ARG ARG SER VAL ASP PRO ASP GLY
SEQRES 31 A 403 VAL PHE ALA SER ASP MET ALA ARG ARG LEU GLN LEU LEU
FORMUL 2 HOH *77(H2 O)
HELIX 1 1 SER A 104 LEU A 113 1 10
HELIX 2 2 THR A 129 CYS A 136 1 8
HELIX 3 3 ASN A 142 GLY A 147 1 6
HELIX 4 4 SER A 148 ASN A 151 5 4
HELIX 5 5 ASP A 174 GLY A 184 1 11
HELIX 6 6 SER A 215 HIS A 223 1 9
HELIX 7 7 GLY A 226 TYR A 231 5 6
HELIX 8 8 LYS A 259 LEU A 263 5 5
HELIX 9 9 PRO A 264 LYS A 269 1 6
HELIX 10 10 ASN A 316 TYR A 321 1 6
HELIX 11 11 ALA A 350 GLY A 365 1 16
HELIX 12 12 GLY A 402 PHE A 417 1 16
HELIX 13 13 THR A 430 TYR A 438 1 9
HELIX 14 14 ARG A 440 ASP A 452 1 13
HELIX 15 15 SER A 459 LEU A 465 1 7
SHEET 1 A 5 ILE A 87 ASP A 91 0
SHEET 2 A 5 LEU A 96 ASP A 100 -1 O ASP A 98 N SER A 89
SHEET 3 A 5 ILE A 190 GLU A 197 -1 O ALA A 194 N VAL A 99
SHEET 4 A 5 VAL A 153 LEU A 159 -1 N SER A 155 O THR A 195
SHEET 5 A 5 VAL A 165 LEU A 168 -1 O LEU A 168 N MET A 156
SHEET 1 B 2 LEU A 117 TRP A 118 0
SHEET 2 B 2 THR A 199 PRO A 200 -1 O THR A 199 N TRP A 118
SHEET 1 C 8 TYR A 310 GLN A 315 0
SHEET 2 C 8 PHE A 206 VAL A 212 -1 N PHE A 206 O GLN A 315
SHEET 3 C 8 ALA A 250 LEU A 257 -1 O ILE A 252 N ASP A 211
SHEET 4 C 8 TYR A 233 PHE A 238 -1 N TYR A 233 O GLY A 255
SHEET 5 C 8 ASN A 371 PHE A 376 -1 O PHE A 373 N ALA A 236
SHEET 6 C 8 GLY A 390 PRO A 398 -1 O ASN A 392 N LYS A 374
SHEET 7 C 8 PHE A 339 PRO A 347 -1 N TYR A 342 O VAL A 395
SHEET 8 C 8 ARG A 420 LEU A 421 -1 O ARG A 420 N VAL A 345
CISPEP 1 PRO A 244 PRO A 245 0 5.91
CISPEP 2 SER A 427 ARG A 428 0 3.63
CRYST1 64.148 64.148 275.462 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 0.015589 0.009000 0.000000 0.00000
SCALE2 0.000000 0.018001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003630 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
