HEADER OXIDOREDUCTASE 15-JUL-12 4G3U
TITLE MYCOBACTERIUM SMEGMATIS DPRE1 - MONOCLINIC CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDOREDUCTASE DPRE1;
COMPND 3 CHAIN: A, B;
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 4G3U 1 REMARK
REVDAT 2 28-AUG-13 4G3U 1 JRNL
REVDAT 1 05-DEC-12 4G3U 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. 2.69 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) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 36552
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1838
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 34.1992 - 6.3107 0.88 2598 160 0.2041 0.2297
REMARK 3 2 6.3107 - 5.0141 0.90 2615 129 0.1962 0.2231
REMARK 3 3 5.0141 - 4.3817 0.92 2636 149 0.1592 0.1580
REMARK 3 4 4.3817 - 3.9818 0.92 2686 127 0.1702 0.1930
REMARK 3 5 3.9818 - 3.6967 0.93 2656 142 0.2139 0.2498
REMARK 3 6 3.6967 - 3.4790 0.93 2685 131 0.2669 0.3077
REMARK 3 7 3.4790 - 3.3049 0.94 2681 156 0.2355 0.2978
REMARK 3 8 3.3049 - 3.1612 0.95 2705 139 0.2297 0.3012
REMARK 3 9 3.1612 - 3.0395 0.95 2728 142 0.2440 0.2908
REMARK 3 10 3.0395 - 2.9347 0.95 2715 163 0.2586 0.2874
REMARK 3 11 2.9347 - 2.8430 0.95 2703 133 0.2686 0.3084
REMARK 3 12 2.8430 - 2.7618 0.96 2719 131 0.2819 0.3729
REMARK 3 13 2.7618 - 2.6890 0.89 2587 136 0.3208 0.3660
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 25.98
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.67290
REMARK 3 B22 (A**2) : -6.12840
REMARK 3 B33 (A**2) : 7.61370
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 7.28740
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 5502
REMARK 3 ANGLE : 0.715 7468
REMARK 3 CHIRALITY : 0.049 824
REMARK 3 PLANARITY : 0.003 972
REMARK 3 DIHEDRAL : 12.247 1978
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 75 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9657 -7.4717 -5.4227
REMARK 3 T TENSOR
REMARK 3 T11: 0.1245 T22: 0.1308
REMARK 3 T33: 0.0764 T12: -0.0457
REMARK 3 T13: -0.0396 T23: -0.0895
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0067
REMARK 3 L33: 0.0048 L12: 0.0021
REMARK 3 L13: 0.0028 L23: 0.0071
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: 0.0421 S13: 0.0089
REMARK 3 S21: -0.0033 S22: -0.0085 S23: 0.0111
REMARK 3 S31: -0.0330 S32: -0.0103 S33: -0.0051
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 116 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6859 -3.3772 -2.6647
REMARK 3 T TENSOR
REMARK 3 T11: -0.0424 T22: 0.1408
REMARK 3 T33: 0.2056 T12: -0.0100
REMARK 3 T13: -0.0948 T23: -0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 0.0032 L22: 0.0024
REMARK 3 L33: -0.0010 L12: 0.0011
REMARK 3 L13: 0.0020 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0020 S12: 0.0157 S13: -0.0079
REMARK 3 S21: -0.0185 S22: -0.0107 S23: 0.0206
REMARK 3 S31: -0.0090 S32: -0.0184 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 149 THROUGH 389 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.1237 -1.9111 -0.7804
REMARK 3 T TENSOR
REMARK 3 T11: -0.3906 T22: 0.0913
REMARK 3 T33: 0.3581 T12: 0.1083
REMARK 3 T13: -0.0605 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.0174 L22: 0.0162
REMARK 3 L33: 0.0356 L12: -0.0119
REMARK 3 L13: -0.0150 L23: -0.0062
REMARK 3 S TENSOR
REMARK 3 S11: 0.0289 S12: 0.0071 S13: 0.0201
REMARK 3 S21: -0.0158 S22: -0.0022 S23: 0.1227
REMARK 3 S31: -0.0814 S32: 0.1051 S33: 0.0259
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 390 THROUGH 417 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.9915 14.6432 -9.3889
REMARK 3 T TENSOR
REMARK 3 T11: 0.1580 T22: 0.1865
REMARK 3 T33: 0.3899 T12: -0.0015
REMARK 3 T13: -0.0560 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.0033 L22: 0.0003
REMARK 3 L33: 0.0013 L12: 0.0004
REMARK 3 L13: 0.0012 L23: -0.0024
REMARK 3 S TENSOR
REMARK 3 S11: 0.0410 S12: 0.0075 S13: 0.0126
REMARK 3 S21: -0.0447 S22: 0.0283 S23: 0.0010
REMARK 3 S31: -0.0169 S32: 0.0035 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 418 THROUGH 468 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7087 18.4019 -3.6258
REMARK 3 T TENSOR
REMARK 3 T11: 0.0838 T22: 0.1764
REMARK 3 T33: 0.2293 T12: -0.0083
REMARK 3 T13: -0.0482 T23: 0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 0.0013 L22: 0.0100
REMARK 3 L33: 0.0032 L12: -0.0032
REMARK 3 L13: -0.0020 L23: 0.0049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0324 S12: -0.0069 S13: 0.0201
REMARK 3 S21: -0.0014 S22: -0.0471 S23: 0.0485
REMARK 3 S31: -0.0404 S32: 0.0464 S33: -0.0143
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND ( RESID 75 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0028 -11.8893 16.6156
REMARK 3 T TENSOR
REMARK 3 T11: 0.1609 T22: 0.1578
REMARK 3 T33: 0.0524 T12: 0.0194
REMARK 3 T13: -0.0100 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.0034 L22: 0.0165
REMARK 3 L33: 0.0027 L12: 0.0030
REMARK 3 L13: 0.0035 L23: -0.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: -0.0215 S13: -0.0162
REMARK 3 S21: 0.0127 S22: 0.0125 S23: -0.0256
REMARK 3 S31: -0.0199 S32: 0.0277 S33: 0.0067
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND ( RESID 116 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6713 -16.2307 27.7042
REMARK 3 T TENSOR
REMARK 3 T11: 0.4334 T22: 0.2387
REMARK 3 T33: 0.0566 T12: -0.0061
REMARK 3 T13: 0.0455 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.0022 L22: 0.0126
REMARK 3 L33: 0.0074 L12: 0.0053
REMARK 3 L13: -0.0049 L23: -0.0088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0229 S12: -0.0287 S13: 0.0075
REMARK 3 S21: 0.0283 S22: 0.0320 S23: -0.0156
REMARK 3 S31: 0.0028 S32: -0.0153 S33: 0.0043
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND ( RESID 149 THROUGH 389 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1493 -17.8858 35.0608
REMARK 3 T TENSOR
REMARK 3 T11: 0.2944 T22: 0.1066
REMARK 3 T33: -0.5011 T12: -0.0073
REMARK 3 T13: 0.2667 T23: 0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 0.0880 L22: 0.0145
REMARK 3 L33: 0.0312 L12: -0.0127
REMARK 3 L13: -0.0067 L23: 0.0349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0103 S12: -0.0387 S13: 0.0334
REMARK 3 S21: 0.4004 S22: -0.0017 S23: -0.0127
REMARK 3 S31: -0.1203 S32: -0.0305 S33: -0.0258
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND ( RESID 390 THROUGH 417 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9086 -35.0165 44.5014
REMARK 3 T TENSOR
REMARK 3 T11: 0.5967 T22: 0.3338
REMARK 3 T33: 0.3111 T12: 0.0226
REMARK 3 T13: 0.1371 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: 0.0004
REMARK 3 L33: 0.0056 L12: -0.0015
REMARK 3 L13: -0.0012 L23: 0.0005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.0088 S13: -0.0417
REMARK 3 S21: 0.0203 S22: -0.0228 S23: -0.0390
REMARK 3 S31: 0.0000 S32: 0.0004 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND ( RESID 418 THROUGH 468 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4459 -37.9206 24.2371
REMARK 3 T TENSOR
REMARK 3 T11: 0.2830 T22: 0.1428
REMARK 3 T33: 0.0273 T12: 0.0530
REMARK 3 T13: 0.0295 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 0.0054 L22: 0.0024
REMARK 3 L33: 0.0088 L12: -0.0013
REMARK 3 L13: -0.0052 L23: 0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0068 S12: -0.0016 S13: -0.0124
REMARK 3 S21: 0.0569 S22: -0.0214 S23: 0.0166
REMARK 3 S31: 0.0285 S32: -0.0159 S33: -0.0046
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 86:274 OR RESSEQ
REMARK 3 308:322 OR RESSEQ 338:468 )
REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 86:274 OR RESSEQ
REMARK 3 308:322 OR RESSEQ 338:468 )
REMARK 3 ATOM PAIRS NUMBER : 2610
REMARK 3 RMSD : 0.011
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G3U 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_1000073703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-10
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 : NSLS
REMARK 200 BEAMLINE : X4A
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 : KOHZU DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36583
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.689
REMARK 200 RESOLUTION RANGE LOW (A) : 102.589
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.62500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.340
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 (%): 69.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% BUTANOL, 0.2 M SODIUM CHLORIDE,
REMARK 280 0.1 M TRIS, 0.5% N,N-DIMETHYLDODECYLAMINE-N-OXIDE, PH 7.5,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.90400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 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 465 SER B 66
REMARK 465 TYR B 67
REMARK 465 GLY B 68
REMARK 465 ASP B 69
REMARK 465 ASN B 70
REMARK 465 ALA B 71
REMARK 465 GLN B 72
REMARK 465 ASN B 73
REMARK 465 GLY B 74
REMARK 465 ASP B 275
REMARK 465 ALA B 276
REMARK 465 PRO B 277
REMARK 465 GLN B 278
REMARK 465 LEU B 279
REMARK 465 LEU B 280
REMARK 465 THR B 281
REMARK 465 LEU B 282
REMARK 465 PRO B 283
REMARK 465 ASP B 284
REMARK 465 ILE B 285
REMARK 465 PHE B 286
REMARK 465 PRO B 287
REMARK 465 ASN B 288
REMARK 465 GLY B 289
REMARK 465 LEU B 290
REMARK 465 ALA B 291
REMARK 465 ASN B 292
REMARK 465 LYS B 293
REMARK 465 PHE B 294
REMARK 465 THR B 295
REMARK 465 PHE B 296
REMARK 465 MET B 297
REMARK 465 PRO B 298
REMARK 465 ILE B 299
REMARK 465 GLY B 300
REMARK 465 GLU B 301
REMARK 465 LEU B 302
REMARK 465 TRP B 303
REMARK 465 TYR B 304
REMARK 465 ARG B 305
REMARK 465 LYS B 306
REMARK 465 SER B 307
REMARK 465 PRO B 323
REMARK 465 LEU B 324
REMARK 465 ASP B 325
REMARK 465 MET B 326
REMARK 465 PHE B 327
REMARK 465 GLY B 328
REMARK 465 GLU B 329
REMARK 465 TRP B 330
REMARK 465 ASN B 331
REMARK 465 ARG B 332
REMARK 465 ALA B 333
REMARK 465 TYR B 334
REMARK 465 GLY B 335
REMARK 465 SER B 336
REMARK 465 ALA B 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 528 O HOH A 529 1.82
REMARK 500 N GLY A 308 O HOH A 635 1.84
REMARK 500 O HOH A 620 O HOH A 630 1.88
REMARK 500 O HOH A 619 O HOH A 621 1.89
REMARK 500 O HOH A 535 O HOH A 643 1.95
REMARK 500 O HOH B 566 O HOH B 570 1.95
REMARK 500 O ALA A 204 O HOH A 516 1.97
REMARK 500 O HOH A 569 O HOH A 571 1.98
REMARK 500 O PRO B 173 O HOH B 504 2.00
REMARK 500 O HOH A 570 O HOH A 587 2.02
REMARK 500 OG SER A 256 O HOH A 573 2.04
REMARK 500 O HOH B 584 O HOH B 587 2.04
REMARK 500 OH TYR A 321 O HOH A 521 2.05
REMARK 500 OD1 ASP B 91 O HOH B 507 2.05
REMARK 500 O HOH A 537 O HOH A 598 2.06
REMARK 500 O HOH A 637 O HOH A 672 2.06
REMARK 500 O GLU A 409 O HOH A 610 2.07
REMARK 500 O HOH B 537 O HOH B 541 2.07
REMARK 500 OD2 ASP A 452 O HOH A 501 2.09
REMARK 500 O PHE B 274 O HOH B 531 2.09
REMARK 500 N ARG A 413 O HOH A 610 2.11
REMARK 500 O HOH A 632 O HOH A 652 2.11
REMARK 500 O HOH B 516 O HOH B 526 2.12
REMARK 500 OE1 GLU B 432 O HOH B 613 2.12
REMARK 500 OG SER B 242 O HOH B 571 2.12
REMARK 500 O HOH A 626 O HOH A 631 2.13
REMARK 500 O LEU B 272 O HOH B 522 2.14
REMARK 500 O HOH A 622 O HOH A 639 2.14
REMARK 500 O HOH B 536 O HOH B 539 2.14
REMARK 500 O ARG B 428 O HOH B 606 2.15
REMARK 500 OD1 ASN A 312 O HOH A 548 2.15
REMARK 500 O HOH A 551 O HOH A 567 2.15
REMARK 500 O GLY B 418 O HOH B 553 2.15
REMARK 500 O HOH B 556 O HOH B 591 2.16
REMARK 500 ND1 HIS B 322 O HOH B 581 2.16
REMARK 500 O LEU A 272 O HOH A 566 2.17
REMARK 500 O HOH A 647 O HOH A 651 2.17
REMARK 500 O HOH A 665 O HOH A 670 2.18
REMARK 500 OH TYR A 233 O HOH A 536 2.19
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 MET A 81 79.10 -119.86
REMARK 500 LEU A 84 47.29 -84.79
REMARK 500 PRO A 123 -158.99 -77.83
REMARK 500 ILE A 399 86.06 -69.37
REMARK 500 ALA A 424 -167.30 -102.03
REMARK 500 ASN B 85 39.18 -142.92
REMARK 500 PRO B 123 -158.94 -77.80
REMARK 500 ALA B 424 -167.19 -101.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G3T RELATED DB: PDB
DBREF 4G3U A 66 468 UNP A0R607 A0R607_MYCS2 66 468
DBREF 4G3U B 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
SEQRES 1 B 403 SER TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL
SEQRES 2 B 403 ILE ASP MET PRO ALA LEU ASN ARG ILE HIS SER ILE ASP
SEQRES 3 B 403 SER GLY THR ARG LEU VAL ASP VAL ASP ALA GLY VAL SER
SEQRES 4 B 403 LEU ASP GLN LEU MET LYS ALA ALA LEU PRO HIS GLY LEU
SEQRES 5 B 403 TRP VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL
SEQRES 6 B 403 GLY GLY ALA ILE GLY CYS ASP ILE HIS GLY LYS ASN HIS
SEQRES 7 B 403 HIS SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET
SEQRES 8 B 403 GLU LEU LEU THR ALA ASN GLY GLU VAL ARG HIS LEU THR
SEQRES 9 B 403 PRO ALA GLY PRO ASP SER ASP LEU PHE TRP ALA THR VAL
SEQRES 10 B 403 GLY GLY ASN GLY LEU THR GLY ILE ILE LEU ARG ALA THR
SEQRES 11 B 403 ILE GLU MET THR PRO THR GLU THR ALA TYR PHE ILE ALA
SEQRES 12 B 403 ASP GLY ASP VAL THR GLY SER LEU ASP GLU THR ILE ALA
SEQRES 13 B 403 PHE HIS SER ASP GLY SER GLU ALA ASN TYR THR TYR SER
SEQRES 14 B 403 SER ALA TRP PHE ASP ALA ILE SER LYS PRO PRO LYS LEU
SEQRES 15 B 403 GLY ARG ALA ALA ILE SER ARG GLY SER LEU ALA LYS LEU
SEQRES 16 B 403 ASP GLN LEU PRO SER LYS LEU GLN LYS ASP PRO LEU LYS
SEQRES 17 B 403 PHE ASP ALA PRO GLN LEU LEU THR LEU PRO ASP ILE PHE
SEQRES 18 B 403 PRO ASN GLY LEU ALA ASN LYS PHE THR PHE MET PRO ILE
SEQRES 19 B 403 GLY GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG ASN
SEQRES 20 B 403 LYS VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP
SEQRES 21 B 403 MET PHE GLY GLU TRP ASN ARG ALA TYR GLY SER ALA GLY
SEQRES 22 B 403 PHE LEU GLN TYR GLN PHE VAL VAL PRO THR GLU ALA VAL
SEQRES 23 B 403 GLU GLU PHE LYS SER ILE ILE VAL ASP ILE GLN ARG SER
SEQRES 24 B 403 GLY HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY
SEQRES 25 B 403 PRO GLY ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY
SEQRES 26 B 403 TRP ASN VAL CYS VAL ASP PHE PRO ILE LYS ALA GLY LEU
SEQRES 27 B 403 HIS GLU PHE VAL THR GLU LEU ASP ARG ARG VAL LEU GLU
SEQRES 28 B 403 PHE GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR
SEQRES 29 B 403 THR ALA GLU THR PHE HIS ALA MET TYR PRO ARG ILE ASP
SEQRES 30 B 403 GLU TRP ILE ARG ILE ARG ARG SER VAL ASP PRO ASP GLY
SEQRES 31 B 403 VAL PHE ALA SER ASP MET ALA ARG ARG LEU GLN LEU LEU
FORMUL 3 HOH *287(H2 O)
HELIX 1 1 SER A 104 LEU A 113 1 10
HELIX 2 2 THR A 129 ASP A 137 1 9
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 ASN A 316 TYR A 321 1 6
HELIX 10 10 ALA A 350 GLY A 365 1 16
HELIX 11 11 GLY A 402 PHE A 417 1 16
HELIX 12 12 THR A 430 TYR A 438 1 9
HELIX 13 13 ARG A 440 ASP A 452 1 13
HELIX 14 14 SER A 459 LEU A 465 1 7
HELIX 15 15 SER B 104 LEU B 113 1 10
HELIX 16 16 THR B 129 ASP B 137 1 9
HELIX 17 17 ASN B 142 GLY B 147 1 6
HELIX 18 18 SER B 148 ASN B 151 5 4
HELIX 19 19 ASP B 174 GLY B 184 1 11
HELIX 20 20 SER B 215 HIS B 223 1 9
HELIX 21 21 GLY B 226 TYR B 231 5 6
HELIX 22 22 LYS B 259 LEU B 263 5 5
HELIX 23 23 ASN B 316 TYR B 321 1 6
HELIX 24 24 ALA B 350 GLY B 365 1 16
HELIX 25 25 GLY B 402 PHE B 417 1 16
HELIX 26 26 THR B 430 TYR B 438 1 9
HELIX 27 27 ARG B 440 ASP B 452 1 13
HELIX 28 28 SER B 459 LEU B 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 LEU A 96 N ASP A 91
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 LEU A 159 O ILE A 190
SHEET 5 A 5 VAL A 165 LEU A 168 -1 O ARG A 166 N LEU A 158
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 ARG A 254 N ASP A 209
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 VAL A 346 O TRP A 391
SHEET 8 C 8 ARG A 420 LEU A 421 -1 O ARG A 420 N VAL A 345
SHEET 1 D 5 ILE B 87 ASP B 91 0
SHEET 2 D 5 LEU B 96 ASP B 100 -1 O LEU B 96 N ASP B 91
SHEET 3 D 5 ILE B 190 GLU B 197 -1 O ALA B 194 N VAL B 99
SHEET 4 D 5 VAL B 153 LEU B 159 -1 N LEU B 159 O ILE B 190
SHEET 5 D 5 VAL B 165 LEU B 168 -1 O ARG B 166 N LEU B 158
SHEET 1 E 2 LEU B 117 TRP B 118 0
SHEET 2 E 2 THR B 199 PRO B 200 -1 O THR B 199 N TRP B 118
SHEET 1 F 8 TYR B 310 GLN B 315 0
SHEET 2 F 8 PHE B 206 VAL B 212 -1 N PHE B 206 O GLN B 315
SHEET 3 F 8 ALA B 250 LEU B 257 -1 O ARG B 254 N ASP B 209
SHEET 4 F 8 TYR B 233 PHE B 238 -1 N SER B 235 O SER B 253
SHEET 5 F 8 ASN B 371 PHE B 376 -1 O PHE B 373 N ALA B 236
SHEET 6 F 8 GLY B 390 PRO B 398 -1 O ASN B 392 N LYS B 374
SHEET 7 F 8 PHE B 339 PRO B 347 -1 N VAL B 346 O TRP B 391
SHEET 8 F 8 ARG B 420 LEU B 421 -1 O ARG B 420 N VAL B 345
CISPEP 1 PRO A 244 PRO A 245 0 5.19
CISPEP 2 SER A 427 ARG A 428 0 9.60
CISPEP 3 PRO B 244 PRO B 245 0 5.06
CISPEP 4 SER B 427 ARG B 428 0 9.30
CRYST1 105.152 65.808 108.504 90.00 109.00 90.00 P 1 21 1 4
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 0.009510 0.000000 0.003275 0.00000
SCALE2 0.000000 0.015196 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009748 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
