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HEADER TRANSFERASE 20-MAR-17 5V7O
TITLE CRYSTAL STRUCTURE OF NOSK FROM STREPTOMYCES ACTUOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOSK;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES ACTUOSUS;
SOURCE 3 ORGANISM_TAXID: 1885;
SOURCE 4 GENE: NOSK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA/BETA HYDROLASE FOLD, NOSIHEPTIDE, ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.BOOKER,A.KBOAL,T.L.GROVE,E.D.BADDING
REVDAT 1 12-APR-17 5V7O 0
JRNL AUTH E.BADDING,T.L.GROVE,L.GADSBY,J.LAMATTINA,A.K.BOAL,S.J.BOOKER
JRNL TITL REROUTING THE PATHWAY FOR THE BIOSYNTHESIS OF THE SIDE RING
JRNL TITL 2 SYSTEM OF NOSIHEPTIDE: THE ROLES OF NOSI, NOSJ, AND NOSK.
JRNL REF J. AM. CHEM. SOC. 2017
JRNL REFN ESSN 1520-5126
JRNL PMID 28343381
JRNL DOI 10.1021/JACS.7B01497
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 16451
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1649
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 28.0549 - 5.2561 1.00 1344 146 0.1698 0.1973
REMARK 3 2 5.2561 - 4.1764 1.00 1253 143 0.1538 0.1830
REMARK 3 3 4.1764 - 3.6497 1.00 1256 147 0.2185 0.2646
REMARK 3 4 3.6497 - 3.3166 0.99 1238 134 0.2442 0.2946
REMARK 3 5 3.3166 - 3.0792 1.00 1225 138 0.2317 0.2927
REMARK 3 6 3.0792 - 2.8979 1.00 1214 140 0.2283 0.2517
REMARK 3 7 2.8979 - 2.7529 1.00 1233 138 0.2297 0.2810
REMARK 3 8 2.7529 - 2.6331 0.97 1199 124 0.3484 0.3886
REMARK 3 9 2.6331 - 2.5318 1.00 1221 128 0.2548 0.2874
REMARK 3 10 2.5318 - 2.4445 1.00 1226 122 0.2607 0.3563
REMARK 3 11 2.4445 - 2.3681 1.00 1213 129 0.2591 0.3286
REMARK 3 12 2.3681 - 2.3004 1.00 1180 160 0.2550 0.3295
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.89
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 : 0.007 1810
REMARK 3 ANGLE : 0.863 2464
REMARK 3 CHIRALITY : 0.049 268
REMARK 3 PLANARITY : 0.006 327
REMARK 3 DIHEDRAL : 14.082 1051
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 28 THROUGH 46 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9460 44.2079 35.1932
REMARK 3 T TENSOR
REMARK 3 T11: 0.2886 T22: 0.2866
REMARK 3 T33: 0.2725 T12: 0.0172
REMARK 3 T13: -0.0394 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.5861 L22: 0.3266
REMARK 3 L33: 2.7793 L12: 0.5123
REMARK 3 L13: -0.3814 L23: 0.2213
REMARK 3 S TENSOR
REMARK 3 S11: -0.1772 S12: 0.1935 S13: 0.0298
REMARK 3 S21: 0.0479 S22: 0.0651 S23: -0.0164
REMARK 3 S31: -0.4093 S32: 0.6453 S33: 0.2569
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 47 THROUGH 62 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9020 47.5879 28.8059
REMARK 3 T TENSOR
REMARK 3 T11: 0.3992 T22: 0.3329
REMARK 3 T33: 0.3522 T12: -0.0256
REMARK 3 T13: 0.0385 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 3.5789 L22: 2.5268
REMARK 3 L33: 6.0499 L12: -0.8475
REMARK 3 L13: -0.6071 L23: -0.8682
REMARK 3 S TENSOR
REMARK 3 S11: 0.0966 S12: -0.1347 S13: 0.7061
REMARK 3 S21: -0.5370 S22: 0.1784 S23: -0.2136
REMARK 3 S31: -0.3110 S32: 0.2671 S33: -0.3999
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 95 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8398 43.5983 40.9537
REMARK 3 T TENSOR
REMARK 3 T11: 0.2830 T22: 0.3452
REMARK 3 T33: 0.2201 T12: 0.0631
REMARK 3 T13: -0.0008 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 1.8992 L22: 0.8321
REMARK 3 L33: 3.7433 L12: -0.2308
REMARK 3 L13: 0.6927 L23: 1.6745
REMARK 3 S TENSOR
REMARK 3 S11: -0.1055 S12: -0.0972 S13: 0.0695
REMARK 3 S21: -0.0891 S22: -0.0897 S23: 0.1393
REMARK 3 S31: -0.2983 S32: -0.7648 S33: 0.1672
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 96 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1341 34.0932 34.0231
REMARK 3 T TENSOR
REMARK 3 T11: 0.2157 T22: 0.3102
REMARK 3 T33: 0.2554 T12: 0.0236
REMARK 3 T13: 0.0108 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.7702 L22: 1.2272
REMARK 3 L33: 1.2952 L12: 0.5418
REMARK 3 L13: -0.8616 L23: 0.7628
REMARK 3 S TENSOR
REMARK 3 S11: -0.0520 S12: 0.0258 S13: -0.0813
REMARK 3 S21: 0.2180 S22: -0.0135 S23: 0.0674
REMARK 3 S31: 0.0930 S32: -0.2876 S33: 0.0911
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2635 28.0107 50.5250
REMARK 3 T TENSOR
REMARK 3 T11: 0.4347 T22: 0.3796
REMARK 3 T33: 0.5325 T12: -0.0059
REMARK 3 T13: -0.0057 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 2.2452 L22: 4.3205
REMARK 3 L33: 1.9540 L12: 0.8730
REMARK 3 L13: 0.8191 L23: 2.5583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0282 S12: 0.4275 S13: 0.6646
REMARK 3 S21: 0.8021 S22: 0.2534 S23: 0.3620
REMARK 3 S31: 0.7509 S32: 0.1439 S33: -0.2403
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0875 44.2811 55.0283
REMARK 3 T TENSOR
REMARK 3 T11: 0.3147 T22: 0.3358
REMARK 3 T33: 0.2539 T12: 0.0782
REMARK 3 T13: 0.0330 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 1.3263 L22: 2.0437
REMARK 3 L33: 2.0219 L12: 0.7686
REMARK 3 L13: 0.3523 L23: 0.7531
REMARK 3 S TENSOR
REMARK 3 S11: -0.2179 S12: -0.0916 S13: -0.1156
REMARK 3 S21: -0.0195 S22: 0.2265 S23: -0.1912
REMARK 3 S31: -0.2227 S32: -0.0317 S33: -0.0223
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 180 THROUGH 197 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2982 25.0129 39.9945
REMARK 3 T TENSOR
REMARK 3 T11: 0.4448 T22: 0.3193
REMARK 3 T33: 0.3255 T12: 0.0468
REMARK 3 T13: 0.0003 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 0.3150 L22: 0.7357
REMARK 3 L33: 3.5065 L12: -0.0436
REMARK 3 L13: 0.9228 L23: 0.6990
REMARK 3 S TENSOR
REMARK 3 S11: 0.2719 S12: -0.0169 S13: -0.2944
REMARK 3 S21: 0.2056 S22: -0.0544 S23: 0.2366
REMARK 3 S31: 0.3875 S32: -1.0507 S33: -0.3104
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1763 28.6527 35.7697
REMARK 3 T TENSOR
REMARK 3 T11: 0.3897 T22: 0.4331
REMARK 3 T33: 0.3420 T12: 0.0913
REMARK 3 T13: -0.0198 T23: -0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 2.5755 L22: 1.8783
REMARK 3 L33: 3.1348 L12: 0.0012
REMARK 3 L13: 0.9778 L23: -0.1305
REMARK 3 S TENSOR
REMARK 3 S11: -0.1419 S12: 0.1356 S13: -0.4000
REMARK 3 S21: -0.0340 S22: 0.1891 S23: -0.2047
REMARK 3 S31: 0.0018 S32: 0.7889 S33: 0.0259
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 257 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7005 36.5159 25.5030
REMARK 3 T TENSOR
REMARK 3 T11: 0.3315 T22: 0.5198
REMARK 3 T33: 0.3357 T12: 0.0310
REMARK 3 T13: 0.0448 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 3.5007 L22: 4.0405
REMARK 3 L33: 4.3332 L12: 0.3534
REMARK 3 L13: 1.7131 L23: 0.6568
REMARK 3 S TENSOR
REMARK 3 S11: -0.0631 S12: 0.4496 S13: 0.2187
REMARK 3 S21: -0.6746 S22: -0.1289 S23: -0.6044
REMARK 3 S31: -0.3647 S32: 0.4841 S33: 0.1391
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 5V7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227000.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16566
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 28.053
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 1.15500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 53.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M (NH4)2SO4, 0.1 M NACL, 0.1 M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 36.70700
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 73.41400
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 73.41400
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 36.70700
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 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 ALA A 3
REMARK 465 GLU A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 MET A 7
REMARK 465 ASP A 8
REMARK 465 THR A 9
REMARK 465 GLU A 10
REMARK 465 THR A 11
REMARK 465 PRO A 12
REMARK 465 ARG A 13
REMARK 465 ASP A 14
REMARK 465 THR A 15
REMARK 465 GLU A 16
REMARK 465 THR A 17
REMARK 465 PRO A 18
REMARK 465 MET A 19
REMARK 465 HIS A 20
REMARK 465 THR A 21
REMARK 465 GLY A 22
REMARK 465 MET A 23
REMARK 465 SER A 24
REMARK 465 THR A 25
REMARK 465 GLY A 26
REMARK 465 PRO A 27
REMARK 465 ALA A 258
REMARK 465 PRO A 259
REMARK 465 ALA A 260
REMARK 465 GLY A 261
REMARK 465 PRO A 262
REMARK 465 ARG A 263
REMARK 465 THR A 264
REMARK 465 THR A 265
REMARK 465 GLN A 266
REMARK 465 LYS A 267
REMARK 465 GLY A 268
REMARK 465 ASP A 269
REMARK 465 THR A 270
REMARK 465 GLU A 271
REMARK 465 PHE A 272
REMARK 465 GLU A 273
REMARK 465 LEU A 274
REMARK 465 ARG A 275
REMARK 465 ARG A 276
REMARK 465 GLN A 277
REMARK 465 ALA A 278
REMARK 465 CYS A 279
REMARK 465 GLY A 280
REMARK 465 ARG A 281
REMARK 465 THR A 282
REMARK 465 ARG A 283
REMARK 465 ALA A 284
REMARK 465 PRO A 285
REMARK 465 PRO A 286
REMARK 465 PRO A 287
REMARK 465 PRO A 288
REMARK 465 PRO A 289
REMARK 465 LEU A 290
REMARK 465 ARG A 291
REMARK 465 SER A 292
REMARK 465 GLY A 293
REMARK 465 CYS A 294
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 ASP A 257 CG OD1 OD2
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 479 O HOH A 480 2.06
REMARK 500 N ARG A 223 O HOH A 401 2.12
REMARK 500 O SER A 205 NH1 ARG A 211 2.12
REMARK 500 NH2 ARG A 58 O PHE A 93 2.18
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 449 O HOH A 476 2665 2.18
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 SER A 102 -168.01 61.83
REMARK 500 ASP A 180 62.58 -157.34
REMARK 500 THR A 184 -72.55 -128.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
DBREF 5V7O A 1 270 UNP C6FX50 C6FX50_STRAS 1 270
SEQADV 5V7O MET A -19 UNP C6FX50 INITIATING METHIONINE
SEQADV 5V7O GLY A -18 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O SER A -17 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O SER A -16 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O HIS A -15 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O HIS A -14 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O HIS A -13 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O HIS A -12 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O HIS A -11 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O HIS A -10 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O SER A -9 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O SER A -8 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O GLY A -7 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O LEU A -6 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O VAL A -5 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O PRO A -4 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ARG A -3 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O GLY A -2 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O SER A -1 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O HIS A 0 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O GLU A 271 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O PHE A 272 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O GLU A 273 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O LEU A 274 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ARG A 275 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ARG A 276 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O GLN A 277 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ALA A 278 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O CYS A 279 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O GLY A 280 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ARG A 281 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O THR A 282 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ARG A 283 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ALA A 284 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O PRO A 285 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O PRO A 286 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O PRO A 287 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O PRO A 288 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O PRO A 289 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O LEU A 290 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O ARG A 291 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O SER A 292 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O GLY A 293 UNP C6FX50 EXPRESSION TAG
SEQADV 5V7O CYS A 294 UNP C6FX50 EXPRESSION TAG
SEQRES 1 A 314 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 314 LEU VAL PRO ARG GLY SER HIS MET ASP ALA GLU THR PRO
SEQRES 3 A 314 MET ASP THR GLU THR PRO ARG ASP THR GLU THR PRO MET
SEQRES 4 A 314 HIS THR GLY MET SER THR GLY PRO GLU THR PRO THR VAL
SEQRES 5 A 314 TYR LEU VAL HIS GLY LEU LEU GLY THR GLY HIS GLY HIS
SEQRES 6 A 314 PHE ALA ALA GLN ILE ARG ALA TRP HIS GLY ARG LEU ARG
SEQRES 7 A 314 THR VAL PRO VAL ASP LEU PRO GLY HIS GLY ARG CYS ARG
SEQRES 8 A 314 ARG ASP ALA ALA GLU ASP TYR PHE ASP ASP ALA LEU ARG
SEQRES 9 A 314 TYR LEU VAL ALA VAL LEU GLU ARG PHE GLY PRO GLY ARG
SEQRES 10 A 314 LEU ILE GLY ALA SER TYR LEU GLY GLY PRO LEU ALA HIS
SEQRES 11 A 314 ARG CYS ALA ALA THR ARG PRO ASP LEU VAL SER SER LEU
SEQRES 12 A 314 VAL LEU THR GLY PHE ALA PRO ASP VAL SER ARG ASP ALA
SEQRES 13 A 314 PHE LEU SER LEU ILE ALA GLY PHE GLU GLY LEU ALA ALA
SEQRES 14 A 314 GLN GLN PRO ALA LEU ALA ALA GLU TYR GLU GLN LEU HIS
SEQRES 15 A 314 GLY THR ARG TRP LYS ARG THR LEU ASP ALA VAL THR GLY
SEQRES 16 A 314 HIS VAL GLU ARG ASP PHE GLU ARG THR ALA LEU VAL ARG
SEQRES 17 A 314 ALA ALA ASP VAL ALA ALA LEU THR VAL PRO THR LEU VAL
SEQRES 18 A 314 LEU ASN GLY SER LEU LYS SER VAL GLU ARG ALA ALA ALA
SEQRES 19 A 314 GLU GLN ALA PRO GLY TRP GLY GLY ARG VAL ARG GLY ARG
SEQRES 20 A 314 VAL VAL PRO GLY ALA GLY HIS LEU VAL GLY HIS ASP ARG
SEQRES 21 A 314 PRO ARG GLU PHE ASN GLU ALA VAL GLU ASP PHE TRP ARG
SEQRES 22 A 314 THR ALA HIS ASP ALA PRO ALA GLY PRO ARG THR THR GLN
SEQRES 23 A 314 LYS GLY ASP THR GLU PHE GLU LEU ARG ARG GLN ALA CYS
SEQRES 24 A 314 GLY ARG THR ARG ALA PRO PRO PRO PRO PRO LEU ARG SER
SEQRES 25 A 314 GLY CYS
HET SO4 A 301 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *91(H2 O)
HELIX 1 AA1 THR A 41 PHE A 46 1 6
HELIX 2 AA2 PHE A 46 HIS A 54 1 9
HELIX 3 AA3 ASP A 77 GLY A 94 1 18
HELIX 4 AA4 SER A 102 ARG A 116 1 15
HELIX 5 AA5 SER A 133 GLY A 143 1 11
HELIX 6 AA6 GLY A 146 GLN A 151 1 6
HELIX 7 AA7 GLN A 151 GLY A 163 1 13
HELIX 8 AA8 ARG A 165 ASP A 180 1 16
HELIX 9 AA9 ARG A 188 ALA A 194 1 7
HELIX 10 AB1 LYS A 207 ALA A 217 1 11
HELIX 11 AB2 PRO A 218 GLY A 221 5 4
HELIX 12 AB3 LEU A 235 ARG A 240 1 6
HELIX 13 AB4 ARG A 240 HIS A 256 1 17
SHEET 1 AA1 6 ARG A 58 VAL A 62 0
SHEET 2 AA1 6 THR A 31 VAL A 35 1 N VAL A 32 O ARG A 58
SHEET 3 AA1 6 GLY A 96 ALA A 101 1 O ARG A 97 N TYR A 33
SHEET 4 AA1 6 VAL A 120 THR A 126 1 O SER A 121 N GLY A 96
SHEET 5 AA1 6 THR A 199 GLY A 204 1 O LEU A 200 N LEU A 125
SHEET 6 AA1 6 ARG A 225 VAL A 229 1 O ARG A 225 N VAL A 201
SITE 1 AC1 9 ARG A 97 SER A 121 THR A 164 ARG A 165
SITE 2 AC1 9 ARG A 168 HIS A 256 HOH A 408 HOH A 420
SITE 3 AC1 9 HOH A 440
CRYST1 75.290 75.290 110.121 90.00 90.00 120.00 P 31 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 0.013282 0.007668 0.000000 0.00000
SCALE2 0.000000 0.015337 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009081 0.00000
TER 1763 ASP A 257
MASTER 501 0 1 13 6 0 3 6 1858 1 5 25
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