HEADER TRANSFERASE/TRANSCRIPTION 23-APR-13 4KBM
TITLE STRUCTURE OF THE MTB CARD/RNAP BETA SUBUNIT B1-B2 DOMAINS COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: B1 AND B2 DOMAINS OF MTB RNAP;
COMPND 5 SYNONYM: RNAP SUBUNIT BETA, RNA POLYMERASE SUBUNIT BETA,
COMPND 6 TRANSCRIPTASE SUBUNIT BETA;
COMPND 7 EC: 2.7.7.6;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RNA POLYMERASE-BINDING TRANSCRIPTION FACTOR CARD;
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: MT0695, MTCI376.08C, RPOB, RV0667;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 13 ORGANISM_TAXID: 1773;
SOURCE 14 STRAIN: H37RV;
SOURCE 15 GENE: CARD, MT3689, RV3583C;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET30B
KEYWDS STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC, TUDOR,
KEYWDS 2 DNA-DEPENDENT RNA POLYMERASE, TRANSCRIPTION REGULATOR, PROTEIN-
KEYWDS 3 PROTEIN COMPLEX, CARD, DNA, SIGMA FACTOR, TRANSFERASE-TRANSCRIPTION
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.GULTEN,J.C.SACCHETTINI,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 4 20-SEP-23 4KBM 1 SEQADV
REVDAT 3 30-OCT-13 4KBM 1 JRNL
REVDAT 2 09-OCT-13 4KBM 1 JRNL
REVDAT 1 02-OCT-13 4KBM 0
JRNL AUTH G.GULTEN,J.C.SACCHETTINI
JRNL TITL STRUCTURE OF THE MTB CARD/RNAP BETA-LOBES COMPLEX REVEALS
JRNL TITL 2 THE MOLECULAR BASIS OF INTERACTION AND PRESENTS A DISTINCT
JRNL TITL 3 DNA-BINDING DOMAIN FOR MTB CARD.
JRNL REF STRUCTURE V. 21 1859 2013
JRNL REFN ISSN 0969-2126
JRNL PMID 24055315
JRNL DOI 10.1016/J.STR.2013.08.014
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 40748
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2055
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 37.5936 - 5.2108 0.97 2724 168 0.2058 0.2209
REMARK 3 2 5.2108 - 4.1377 0.96 2566 156 0.1619 0.1893
REMARK 3 3 4.1377 - 3.6151 0.97 2579 136 0.1862 0.2074
REMARK 3 4 3.6151 - 3.2848 0.98 2585 140 0.2001 0.2288
REMARK 3 5 3.2848 - 3.0495 0.99 2652 115 0.2130 0.2402
REMARK 3 6 3.0495 - 2.8698 1.00 2588 141 0.2237 0.2792
REMARK 3 7 2.8698 - 2.7261 1.00 2623 133 0.2287 0.3025
REMARK 3 8 2.7261 - 2.6074 1.00 2650 120 0.2318 0.2845
REMARK 3 9 2.6074 - 2.5071 1.00 2573 140 0.2260 0.2868
REMARK 3 10 2.5071 - 2.4206 1.00 2623 143 0.2207 0.2710
REMARK 3 11 2.4206 - 2.3449 1.00 2555 143 0.2304 0.2521
REMARK 3 12 2.3449 - 2.2779 1.00 2600 139 0.2328 0.2733
REMARK 3 13 2.2779 - 2.2179 1.00 2573 131 0.2420 0.2927
REMARK 3 14 2.2179 - 2.1638 0.99 2587 130 0.2534 0.2932
REMARK 3 15 2.1638 - 2.1146 0.85 2215 120 0.2718 0.3119
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 : 0.32
REMARK 3 B_SOL : 33.56
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60120
REMARK 3 B22 (A**2) : -3.44050
REMARK 3 B33 (A**2) : 4.04170
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 : 0.005 4268
REMARK 3 ANGLE : 0.872 5770
REMARK 3 CHIRALITY : 0.059 663
REMARK 3 PLANARITY : 0.004 751
REMARK 3 DIHEDRAL : 14.276 1617
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ -5:128)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1388 -4.4684 39.7123
REMARK 3 T TENSOR
REMARK 3 T11: 0.0777 T22: 0.1676
REMARK 3 T33: 0.0997 T12: 0.0179
REMARK 3 T13: -0.0230 T23: -0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 2.1422 L22: 1.4838
REMARK 3 L33: 1.6877 L12: -0.7196
REMARK 3 L13: 1.0097 L23: -0.0016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0423 S12: -0.1203 S13: 0.0235
REMARK 3 S21: -0.1048 S22: -0.0237 S23: -0.0311
REMARK 3 S31: -0.0685 S32: 0.0427 S33: 0.0198
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 129:325)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5773 -28.8381 33.3990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: 0.1463
REMARK 3 T33: 0.1579 T12: -0.0105
REMARK 3 T13: -0.0188 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.4729 L22: 1.7015
REMARK 3 L33: 0.2404 L12: -0.6321
REMARK 3 L13: -0.2135 L23: 0.3638
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: -0.1019 S13: -0.0939
REMARK 3 S21: -0.0446 S22: -0.0687 S23: 0.0390
REMARK 3 S31: 0.0766 S32: -0.0606 S33: 0.0339
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 328:379)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8151 -34.2653 34.3786
REMARK 3 T TENSOR
REMARK 3 T11: 0.1316 T22: 0.1841
REMARK 3 T33: 0.3629 T12: 0.0124
REMARK 3 T13: 0.0031 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.3749 L22: 3.0781
REMARK 3 L33: 0.1514 L12: -1.4717
REMARK 3 L13: -0.3877 L23: 0.1526
REMARK 3 S TENSOR
REMARK 3 S11: 0.0283 S12: -0.2125 S13: 0.1265
REMARK 3 S21: 0.0860 S22: 0.1574 S23: -0.7984
REMARK 3 S31: 0.0955 S32: 0.0301 S33: -0.1870
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 2:58)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0711 1.6310 17.1702
REMARK 3 T TENSOR
REMARK 3 T11: 0.1485 T22: 0.1245
REMARK 3 T33: 0.2051 T12: -0.0033
REMARK 3 T13: -0.0140 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 5.2176 L22: 5.5468
REMARK 3 L33: 4.8240 L12: -0.8542
REMARK 3 L13: 0.6193 L23: -0.2701
REMARK 3 S TENSOR
REMARK 3 S11: -0.0539 S12: 0.2741 S13: 0.0690
REMARK 3 S21: -0.4823 S22: 0.0562 S23: -0.2875
REMARK 3 S31: -0.2722 S32: 0.1617 S33: -0.0163
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 63:145)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.9212 16.4987 -2.2026
REMARK 3 T TENSOR
REMARK 3 T11: 0.3847 T22: 0.2848
REMARK 3 T33: 0.2496 T12: 0.1267
REMARK 3 T13: 0.1086 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 3.7968 L22: 2.6988
REMARK 3 L33: 7.2488 L12: 0.0086
REMARK 3 L13: 0.7590 L23: -0.5650
REMARK 3 S TENSOR
REMARK 3 S11: -0.2978 S12: 0.0605 S13: 0.0230
REMARK 3 S21: 0.2880 S22: -0.0765 S23: 0.0438
REMARK 3 S31: -0.1083 S32: 0.3854 S33: 0.3858
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 4KBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079134.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
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 300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40844
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110
REMARK 200 RESOLUTION RANGE LOW (A) : 37.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
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) : 2.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
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 : 2.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4KBJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 3350, 2% TACSIMATE PH 5.0, 0.1
REMARK 280 M SODIUM CITRATE TRIBASIC DIHYDRATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K, PH 5.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.76300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.76300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.57600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.44450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.57600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.44450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 112.76300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.57600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.44450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.76300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.57600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 64.44450
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 LEU A -8
REMARK 465 VAL A -7
REMARK 465 PRO A -6
REMARK 465 THR A 427
REMARK 465 SER A 428
REMARK 465 GLN A 429
REMARK 465 LEU A 430
REMARK 465 SER A 431
REMARK 465 GLN A 432
REMARK 465 PHE A 433
REMARK 465 MET B 1
REMARK 465 THR B 26
REMARK 465 ILE B 27
REMARK 465 LYS B 28
REMARK 465 GLY B 29
REMARK 465 HIS B 78
REMARK 465 THR B 79
REMARK 465 GLU B 80
REMARK 465 GLU B 81
REMARK 465 PRO B 82
REMARK 465 THR B 83
REMARK 465 ASN B 84
REMARK 465 ALA B 161
REMARK 465 SER B 162
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A -5 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 364 CG1 CG2 CD1
REMARK 470 ASP A 365 CG OD1 OD2
REMARK 470 HIS A 366 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 367 CG CD1 CD2 CE1 CE2 CZ
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 75 71.77 49.79
REMARK 500 PHE A 93 -61.99 -27.81
REMARK 500 ASP A 190 1.71 81.25
REMARK 500 ALA A 303 166.71 63.20
REMARK 500 THR A 323 -73.28 -105.71
REMARK 500 HIS B 13 -4.12 74.81
REMARK 500 GLU B 117 -105.23 -116.14
REMARK 500 ALA B 148 -38.13 -156.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KBJ RELATED DB: PDB
REMARK 900 STRUCTURE OF MTB RNAP BETA SUBUNIT B1 AND B2 DOMAINS
DBREF 4KBM A 47 433 UNP P0A680 RPOB_MYCTU 53 439
DBREF 4KBM B 1 162 UNP O53568 CARD_MYCTU 1 162
SEQADV 4KBM MET A -21 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM GLY A -20 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM SER A -19 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM SER A -18 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM HIS A -17 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM HIS A -16 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM HIS A -15 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM HIS A -14 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM HIS A -13 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM HIS A -12 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM SER A -11 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM SER A -10 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM GLY A -9 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM LEU A -8 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM VAL A -7 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM PRO A -6 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM ARG A -5 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM GLY A -4 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM SER A -3 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM HIS A -2 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM MET A -1 UNP P0A680 EXPRESSION TAG
SEQADV 4KBM MET A 0 UNP P0A680 EXPRESSION TAG
SEQRES 1 A 409 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 409 LEU VAL PRO ARG GLY SER HIS MET MET LEU LEU ASP VAL
SEQRES 3 A 409 GLN THR ASP SER PHE GLU TRP LEU ILE GLY SER PRO ARG
SEQRES 4 A 409 TRP ARG GLU SER ALA ALA GLU ARG GLY ASP VAL ASN PRO
SEQRES 5 A 409 VAL GLY GLY LEU GLU GLU VAL LEU TYR GLU LEU SER PRO
SEQRES 6 A 409 ILE GLU ASP PHE SER GLY SER MET SER LEU SER PHE SER
SEQRES 7 A 409 ASP PRO ARG PHE ASP ASP VAL LYS ALA PRO VAL ASP GLU
SEQRES 8 A 409 CYS LYS ASP LYS ASP MET THR TYR ALA ALA PRO LEU PHE
SEQRES 9 A 409 VAL THR ALA GLU PHE ILE ASN ASN ASN THR GLY GLU ILE
SEQRES 10 A 409 LYS SER GLN THR VAL PHE MET GLY ASP PHE PRO MET MET
SEQRES 11 A 409 THR GLU LYS GLY THR PHE ILE ILE ASN GLY THR GLU ARG
SEQRES 12 A 409 VAL VAL VAL SER GLN LEU VAL ARG SER PRO GLY VAL TYR
SEQRES 13 A 409 PHE ASP GLU THR ILE ASP LYS SER THR ASP LYS THR LEU
SEQRES 14 A 409 HIS SER VAL LYS VAL ILE PRO SER ARG GLY ALA TRP LEU
SEQRES 15 A 409 GLU PHE ASP VAL ASP LYS ARG ASP THR VAL GLY VAL ARG
SEQRES 16 A 409 ILE ASP ARG LYS ARG ARG GLN PRO VAL THR VAL LEU LEU
SEQRES 17 A 409 LYS ALA LEU GLY TRP THR SER GLU GLN ILE VAL GLU ARG
SEQRES 18 A 409 PHE GLY PHE SER GLU ILE MET ARG SER THR LEU GLU LYS
SEQRES 19 A 409 ASP ASN THR VAL GLY THR ASP GLU ALA LEU LEU ASP ILE
SEQRES 20 A 409 TYR ARG LYS LEU ARG PRO GLY GLU PRO PRO THR LYS GLU
SEQRES 21 A 409 SER ALA GLN THR LEU LEU GLU ASN LEU PHE PHE LYS GLU
SEQRES 22 A 409 LYS ARG TYR ASP LEU ALA ARG VAL GLY ARG TYR LYS VAL
SEQRES 23 A 409 ASN LYS LYS LEU GLY LEU HIS VAL GLY GLU PRO ILE THR
SEQRES 24 A 409 SER SER THR LEU THR GLU GLU ASP VAL VAL ALA THR ILE
SEQRES 25 A 409 GLU TYR LEU VAL ARG LEU HIS GLU GLY GLN THR THR MET
SEQRES 26 A 409 THR VAL PRO GLY GLY VAL GLU VAL PRO VAL GLU THR ASP
SEQRES 27 A 409 ASP ILE ASP HIS PHE GLY ASN ARG ARG LEU ARG THR VAL
SEQRES 28 A 409 GLY GLU LEU ILE GLN ASN GLN ILE ARG VAL GLY MET SER
SEQRES 29 A 409 ARG MET GLU ARG VAL VAL ARG GLU ARG MET THR THR GLN
SEQRES 30 A 409 ASP VAL GLU ALA ILE THR PRO GLN THR LEU ILE ASN ILE
SEQRES 31 A 409 ARG PRO VAL VAL ALA ALA ILE LYS GLU PHE PHE GLY THR
SEQRES 32 A 409 SER GLN LEU SER GLN PHE
SEQRES 1 B 162 MET ILE PHE LYS VAL GLY ASP THR VAL VAL TYR PRO HIS
SEQRES 2 B 162 HIS GLY ALA ALA LEU VAL GLU ALA ILE GLU THR ARG THR
SEQRES 3 B 162 ILE LYS GLY GLU GLN LYS GLU TYR LEU VAL LEU LYS VAL
SEQRES 4 B 162 ALA GLN GLY ASP LEU THR VAL ARG VAL PRO ALA GLU ASN
SEQRES 5 B 162 ALA GLU TYR VAL GLY VAL ARG ASP VAL VAL GLY GLN GLU
SEQRES 6 B 162 GLY LEU ASP LYS VAL PHE GLN VAL LEU ARG ALA PRO HIS
SEQRES 7 B 162 THR GLU GLU PRO THR ASN TRP SER ARG ARG TYR LYS ALA
SEQRES 8 B 162 ASN LEU GLU LYS LEU ALA SER GLY ASP VAL ASN LYS VAL
SEQRES 9 B 162 ALA GLU VAL VAL ARG ASP LEU TRP ARG ARG ASP GLN GLU
SEQRES 10 B 162 ARG GLY LEU SER ALA GLY GLU LYS ARG MET LEU ALA LYS
SEQRES 11 B 162 ALA ARG GLN ILE LEU VAL GLY GLU LEU ALA LEU ALA GLU
SEQRES 12 B 162 SER THR ASP ASP ALA LYS ALA GLU THR ILE LEU ASP GLU
SEQRES 13 B 162 VAL LEU ALA ALA ALA SER
FORMUL 3 HOH *305(H2 O)
HELIX 1 1 LEU A 47 ILE A 59 1 13
HELIX 2 2 SER A 61 GLY A 72 1 12
HELIX 3 3 GLY A 78 SER A 88 1 11
HELIX 4 4 PRO A 112 LYS A 119 1 8
HELIX 5 5 VAL A 228 LEU A 235 1 8
HELIX 6 6 THR A 238 GLY A 247 1 10
HELIX 7 7 SER A 249 ASP A 259 1 11
HELIX 8 8 VAL A 262 ARG A 276 1 15
HELIX 9 9 THR A 282 PHE A 295 1 14
HELIX 10 10 LEU A 302 GLY A 315 1 14
HELIX 11 11 THR A 328 GLU A 344 1 17
HELIX 12 12 THR A 374 GLN A 401 1 28
HELIX 13 13 THR A 407 ILE A 412 1 6
HELIX 14 14 ILE A 414 PHE A 425 1 12
HELIX 15 15 GLU B 51 ALA B 53 5 3
HELIX 16 16 GLY B 63 ALA B 76 1 14
HELIX 17 17 SER B 86 SER B 98 1 13
HELIX 18 18 ASP B 100 GLN B 116 1 17
HELIX 19 19 SER B 121 GLU B 143 1 23
HELIX 20 20 LYS B 149 ALA B 160 1 12
SHEET 1 A 8 ILE A 90 GLU A 91 0
SHEET 2 A 8 MET A 97 PHE A 106 -1 O LEU A 99 N ILE A 90
SHEET 3 A 8 ALA A 124 ASN A 135 -1 O PHE A 128 N ARG A 105
SHEET 4 A 8 GLU A 140 PRO A 152 -1 O LYS A 142 N PHE A 133
SHEET 5 A 8 LEU B 44 PRO B 49 -1 O THR B 45 N SER A 143
SHEET 6 A 8 LYS B 32 VAL B 39 -1 N LEU B 35 O VAL B 48
SHEET 7 A 8 GLY B 15 ARG B 25 -1 N LEU B 18 O LYS B 38
SHEET 8 A 8 THR B 8 TYR B 11 -1 N VAL B 9 O ALA B 17
SHEET 1 B 2 PHE A 160 ILE A 162 0
SHEET 2 B 2 THR A 165 ARG A 167 -1 O ARG A 167 N PHE A 160
SHEET 1 C 2 GLN A 172 ARG A 175 0
SHEET 2 C 2 ARG A 370 ARG A 373 -1 O ARG A 371 N VAL A 174
SHEET 1 D 5 GLY A 178 ILE A 185 0
SHEET 2 D 5 THR A 192 ILE A 199 -1 O LEU A 193 N THR A 184
SHEET 3 D 5 LEU A 206 VAL A 210 -1 O VAL A 210 N HIS A 194
SHEET 4 D 5 VAL A 216 ILE A 220 -1 O GLY A 217 N ASP A 209
SHEET 5 D 5 GLN A 226 PRO A 227 -1 O GLN A 226 N VAL A 218
SHEET 1 E 2 THR A 348 MET A 349 0
SHEET 2 E 2 VAL A 357 PRO A 358 -1 O VAL A 357 N MET A 349
CISPEP 1 SER A 88 PRO A 89 0 -0.22
CISPEP 2 LYS A 187 SER A 188 0 -9.63
CRYST1 49.152 128.889 225.526 90.00 90.00 90.00 C 2 2 21 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 0.020345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007759 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004434 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
