HEADER TRANSCRIPTION 03-JUN-14 4QJF
TITLE X-RAY CRYSTAL STRUCTURE OF THERMOCUCCUS KODAKARENSIS RNA POLYMERASE
TITLE 2 RPP4/RPO7 (RPOF/RPOE) COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE, SUBUNIT E';
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA-DIRECTED RNA POLYMERASE, SUBUNIT F;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS;
SOURCE 3 ORGANISM_TAXID: 69014;
SOURCE 4 STRAIN: ATCC BAA-918 / JCM 12380 / KOD1;
SOURCE 5 GENE: RPO7, TK1699;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS;
SOURCE 10 ORGANISM_TAXID: 69014;
SOURCE 11 STRAIN: ATCC BAA-918 / JCM 12380 / KOD1;
SOURCE 12 GENE: RPO4, TK0901;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.MURAKAMI
REVDAT 2 28-FEB-24 4QJF 1 SEQADV
REVDAT 1 15-OCT-14 4QJF 0
JRNL AUTH K.S.MURAKAMI
JRNL TITL CRYSTAL STRUCTURE OF EURYARCHAEAL RNA POLYMERASE AND INSIGHT
JRNL TITL 2 INTO THE EVOLUTION OF RNA POLYMERASE II STRUCTURE
JRNL REF NAT.COMMUN. 2014
JRNL REFN ESSN 2041-1723
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1626)
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) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 3 NUMBER OF REFLECTIONS : 12575
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 673
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 25.7958 - 3.9489 0.99 2833 145 0.1526 0.1886
REMARK 3 2 3.9489 - 3.1361 0.90 1655 91 0.2100 0.3045
REMARK 3 3 3.1361 - 2.7402 1.00 2858 169 0.2123 0.3048
REMARK 3 4 2.7402 - 2.4899 0.99 2837 133 0.2204 0.2909
REMARK 3 5 2.4899 - 2.3115 0.84 2391 135 0.2485 0.3443
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.510
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 2573
REMARK 3 ANGLE : 1.212 3462
REMARK 3 CHIRALITY : 0.044 376
REMARK 3 PLANARITY : 0.006 449
REMARK 3 DIHEDRAL : 17.264 1019
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9209 7.2343 -42.8383
REMARK 3 T TENSOR
REMARK 3 T11: 0.1573 T22: 0.1195
REMARK 3 T33: 0.0843 T12: 0.0139
REMARK 3 T13: -0.0058 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.4785 L22: 0.1363
REMARK 3 L33: 1.1019 L12: -0.0474
REMARK 3 L13: -0.4933 L23: 0.5205
REMARK 3 S TENSOR
REMARK 3 S11: 0.0420 S12: 0.0754 S13: -0.0168
REMARK 3 S21: -0.0752 S22: -0.0000 S23: -0.0533
REMARK 3 S31: -0.3278 S32: -0.1676 S33: 0.0175
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 94 THROUGH 140 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1436 -1.6345 -9.7129
REMARK 3 T TENSOR
REMARK 3 T11: 0.1913 T22: 0.2339
REMARK 3 T33: 0.1843 T12: 0.0055
REMARK 3 T13: -0.0260 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: -0.0154 L22: 0.1088
REMARK 3 L33: 0.2102 L12: -0.0389
REMARK 3 L13: 0.3416 L23: -0.2222
REMARK 3 S TENSOR
REMARK 3 S11: 0.0598 S12: -0.1146 S13: -0.0952
REMARK 3 S21: 0.0294 S22: -0.1031 S23: 0.0320
REMARK 3 S31: 0.1891 S32: 0.0963 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 141 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2427 5.4715 -24.8502
REMARK 3 T TENSOR
REMARK 3 T11: 0.1462 T22: 0.2297
REMARK 3 T33: 0.2037 T12: 0.0001
REMARK 3 T13: 0.0020 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.0312 L22: 0.1301
REMARK 3 L33: 0.2233 L12: -0.1757
REMARK 3 L13: 0.0317 L23: -0.0847
REMARK 3 S TENSOR
REMARK 3 S11: 0.0800 S12: 0.0840 S13: 0.0106
REMARK 3 S21: -0.0672 S22: -0.1002 S23: -0.0599
REMARK 3 S31: 0.0926 S32: 0.1163 S33: -0.0020
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5649 10.0426 -2.7188
REMARK 3 T TENSOR
REMARK 3 T11: 0.2093 T22: 0.3609
REMARK 3 T33: 0.2097 T12: -0.1029
REMARK 3 T13: 0.0125 T23: -0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 0.0131 L22: 0.1479
REMARK 3 L33: 0.0375 L12: -0.0196
REMARK 3 L13: -0.0490 L23: -0.1057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: -0.3661 S13: 0.1999
REMARK 3 S21: 0.2061 S22: -0.0546 S23: 0.0948
REMARK 3 S31: -0.2577 S32: -0.0463 S33: 0.0002
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7792 10.8168 -35.1162
REMARK 3 T TENSOR
REMARK 3 T11: 0.2776 T22: 0.1576
REMARK 3 T33: 0.1692 T12: -0.0503
REMARK 3 T13: -0.0594 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.1817 L22: 0.7237
REMARK 3 L33: 0.7341 L12: -0.4325
REMARK 3 L13: 0.0317 L23: 0.4196
REMARK 3 S TENSOR
REMARK 3 S11: -0.0689 S12: 0.0331 S13: 0.0826
REMARK 3 S21: -0.7709 S22: -0.1570 S23: 0.7448
REMARK 3 S31: -0.2941 S32: -0.1132 S33: -0.0397
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 27 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8396 -5.1268 -42.1997
REMARK 3 T TENSOR
REMARK 3 T11: 0.4162 T22: 0.0781
REMARK 3 T33: 0.3092 T12: -0.0038
REMARK 3 T13: -0.1676 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.3789 L22: 0.3346
REMARK 3 L33: 0.6225 L12: 0.2351
REMARK 3 L13: 0.3319 L23: 0.0365
REMARK 3 S TENSOR
REMARK 3 S11: 0.2499 S12: 0.4104 S13: -0.1393
REMARK 3 S21: -0.7790 S22: -0.1163 S23: 0.1763
REMARK 3 S31: 0.2803 S32: 0.5234 S33: -0.0397
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 39 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5790 17.0277 -17.8647
REMARK 3 T TENSOR
REMARK 3 T11: 0.1409 T22: 0.1090
REMARK 3 T33: 0.1761 T12: 0.0220
REMARK 3 T13: -0.0016 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: -0.1423 L22: 1.2240
REMARK 3 L33: 0.2804 L12: -0.4097
REMARK 3 L13: -0.1402 L23: -0.5606
REMARK 3 S TENSOR
REMARK 3 S11: -0.1140 S12: 0.0511 S13: 0.0277
REMARK 3 S21: 0.1118 S22: 0.1520 S23: 0.1478
REMARK 3 S31: -0.0806 S32: -0.0780 S33: 0.0054
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 117 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8917 11.8984 -12.4735
REMARK 3 T TENSOR
REMARK 3 T11: 0.2463 T22: 0.4076
REMARK 3 T33: 0.4631 T12: 0.0006
REMARK 3 T13: 0.0216 T23: 0.1400
REMARK 3 L TENSOR
REMARK 3 L11: 0.0509 L22: 0.0208
REMARK 3 L33: 0.5745 L12: 0.0106
REMARK 3 L13: -0.1088 L23: 0.0363
REMARK 3 S TENSOR
REMARK 3 S11: 0.3278 S12: -0.1145 S13: -0.2601
REMARK 3 S21: -0.3929 S22: 0.3674 S23: 0.3304
REMARK 3 S31: -0.4404 S32: 0.3666 S33: 0.0043
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 4QJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086130.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9714
REMARK 200 MONOCHROMATOR : NA
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12575
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.6
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAACETATE AND 30 % GLYCEROL, PH
REMARK 280 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 21.23250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.70650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.47100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.70650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.23250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.47100
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 SER A 187
REMARK 465 LYS A 188
REMARK 465 GLY A 189
REMARK 465 GLU A 190
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 ALA A 183 O HOH A 257 1.92
REMARK 500 OE1 GLU A 174 O HOH A 223 2.10
REMARK 500 N LEU B 54 O HOH B 261 2.15
REMARK 500 OE2 GLU A 88 O HOH A 217 2.15
REMARK 500 NH1 ARG B 23 O HOH B 241 2.16
REMARK 500 OE2 GLU A 158 O HOH A 246 2.16
REMARK 500 O HOH B 242 O HOH B 266 2.17
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 B 210 O HOH B 240 3544 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 ASN A 133 33.88 -77.63
REMARK 500 LYS A 152 -86.24 -93.94
REMARK 500 ARG A 166 46.84 -84.63
REMARK 500 LYS A 180 -146.75 -73.17
REMARK 500 LYS A 181 11.11 -64.30
REMARK 500 GLU A 185 74.75 -68.68
REMARK 500 LEU B 29 57.94 25.92
REMARK 500 GLU B 31 -91.11 60.13
REMARK 500 GLU B 34 -62.05 57.72
REMARK 500 GLU B 35 73.55 68.18
REMARK 500 GLU B 117 -169.09 -75.61
REMARK 500 TYR B 118 -34.80 58.67
REMARK 500 LEU B 121 -20.58 65.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QIW RELATED DB: PDB
DBREF 4QJF A 1 190 UNP Q5JIY4 Q5JIY4_THEKO 1 190
DBREF 4QJF B 1 114 UNP Q5JI52 Q5JI52_THEKO 1 114
SEQADV 4QJF ILE B 115 UNP Q5JI52 EXPRESSION TAG
SEQADV 4QJF ASP B 116 UNP Q5JI52 EXPRESSION TAG
SEQADV 4QJF GLU B 117 UNP Q5JI52 EXPRESSION TAG
SEQADV 4QJF TYR B 118 UNP Q5JI52 EXPRESSION TAG
SEQADV 4QJF ARG B 119 UNP Q5JI52 EXPRESSION TAG
SEQADV 4QJF PRO B 120 UNP Q5JI52 EXPRESSION TAG
SEQADV 4QJF LEU B 121 UNP Q5JI52 EXPRESSION TAG
SEQADV 4QJF GLU B 122 UNP Q5JI52 EXPRESSION TAG
SEQRES 1 A 190 MET TYR LYS LEU LEU LYS VAL LYS ASP VAL VAL ARG ILE
SEQRES 2 A 190 PRO PRO ARG MET PHE THR MET ASP PRO LYS GLU ALA ALA
SEQRES 3 A 190 LYS ILE VAL LEU ARG GLU THR TYR GLU GLY ILE TYR ASP
SEQRES 4 A 190 ARG ASP GLU GLY VAL VAL LEU ALA ILE LEU ASP VAL GLU
SEQRES 5 A 190 GLU ILE SER GLU GLY VAL ILE VAL PRO GLY ASP GLY ALA
SEQRES 6 A 190 THR TYR HIS GLU ALA ILE PHE ASN VAL LEU VAL TRP GLU
SEQRES 7 A 190 PRO ARG ASN GLN GLU VAL VAL GLU GLY GLU VAL VAL GLU
SEQRES 8 A 190 MET MET PRO TYR GLY ALA PHE ILE ARG ILE GLY PRO MET
SEQRES 9 A 190 ASP GLY LEU VAL HIS ILE SER GLN LEU MET ASP ASP TYR
SEQRES 10 A 190 VAL VAL PHE ASP GLU LYS ASN ARG GLN PHE ILE GLY LYS
SEQRES 11 A 190 GLU THR ASN ARG VAL LEU LYS LEU GLY ASP TYR VAL ARG
SEQRES 12 A 190 ALA ARG ILE ILE GLY VAL SER VAL LYS SER ARG VAL ILE
SEQRES 13 A 190 ARG GLU ASN LYS ILE ASN MET THR MET ARG GLN PRO GLY
SEQRES 14 A 190 LEU GLY LYS PHE GLU TRP ILE GLU LYS GLU LYS LYS LYS
SEQRES 15 A 190 ALA LYS GLU GLU SER LYS GLY GLU
SEQRES 1 B 122 MET ILE GLY ARG LYS LYS LEU GLU GLU HIS TYR ILE THR
SEQRES 2 B 122 ILE ALA GLU ALA LYS GLU LEU LEU GLU ARG ARG HIS ALA
SEQRES 3 B 122 GLU GLY LEU ALA GLU ASN PRO GLU GLU PRO MET PHE TYR
SEQRES 4 B 122 GLU ALA ARG VAL SER LEU GLU HIS ALA GLU ARG PHE ALA
SEQRES 5 B 122 LYS LEU LYS PRO GLU GLN ALA ARG GLU LEU LYS GLU LYS
SEQRES 6 B 122 LEU MET GLY LEU PHE ASP TRP ILE ASN GLU ARG ILE ALA
SEQRES 7 B 122 ALA LYS LEU VAL ASP ILE LEU PRO GLU ASP TYR LEU ASP
SEQRES 8 B 122 ILE ARG VAL ILE PHE ALA LYS GLU GLU TYR MET PRO THR
SEQRES 9 B 122 PRO GLU GLU ALA GLU GLU ILE ILE LYS VAL ILE ASP GLU
SEQRES 10 B 122 TYR ARG PRO LEU GLU
FORMUL 3 HOH *137(H2 O)
HELIX 1 1 PRO A 14 PHE A 18 5 5
HELIX 2 2 ASP A 21 GLU A 35 1 15
HELIX 3 3 SER A 111 LEU A 113 5 3
HELIX 4 4 VAL A 155 ASN A 159 5 5
HELIX 5 5 PHE A 173 LYS A 180 1 8
HELIX 6 6 THR B 13 GLU B 27 1 15
HELIX 7 7 PHE B 38 ALA B 52 1 15
HELIX 8 8 LYS B 55 GLY B 68 1 14
HELIX 9 9 ASN B 74 LEU B 85 1 12
HELIX 10 10 ASP B 88 ALA B 97 1 10
HELIX 11 11 THR B 104 GLU B 117 1 14
SHEET 1 A 5 TYR A 38 ASP A 39 0
SHEET 2 A 5 GLY A 43 ILE A 54 -1 O GLY A 43 N ASP A 39
SHEET 3 A 5 THR A 66 TRP A 77 -1 O ASN A 73 N LEU A 49
SHEET 4 A 5 TYR A 2 ILE A 13 -1 N ASP A 9 O ALA A 70
SHEET 5 A 5 LYS B 5 ILE B 12 -1 O GLU B 8 N LYS A 6
SHEET 1 B 7 GLY A 171 LYS A 172 0
SHEET 2 B 7 TYR A 141 SER A 150 -1 N ARG A 143 O GLY A 171
SHEET 3 B 7 LYS A 160 THR A 164 -1 O ASN A 162 N ILE A 147
SHEET 4 B 7 ASP A 105 HIS A 109 1 N LEU A 107 O MET A 163
SHEET 5 B 7 GLY A 96 ARG A 100 -1 N ILE A 99 O GLY A 106
SHEET 6 B 7 VAL A 84 MET A 93 -1 N GLU A 88 O ARG A 100
SHEET 7 B 7 TYR A 141 SER A 150 -1 O ALA A 144 N VAL A 85
SHEET 1 C 3 VAL A 118 ASP A 121 0
SHEET 2 C 3 GLN A 126 GLY A 129 -1 O GLN A 126 N ASP A 121
SHEET 3 C 3 VAL A 135 LYS A 137 -1 O LEU A 136 N PHE A 127
CISPEP 1 ILE A 101 GLY A 102 0 12.49
CISPEP 2 GLY B 28 LEU B 29 0 -13.53
CRYST1 42.465 80.942 97.413 90.00 90.00 90.00 P 21 21 21 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 0.023549 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012355 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010266 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
