HEADER LIGASE 09-SEP-11 3TQT
TITLE STRUCTURE OF THE D-ALANINE-D-ALANINE LIGASE FROM COXIELLA BURNETII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;
COMPND 5 EC: 6.3.2.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COXIELLA BURNETII;
SOURCE 3 ORGANISM_TAXID: 227377;
SOURCE 4 STRAIN: RSA493;
SOURCE 5 GENE: DDL, CBU_1338;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS CELL ENVELOPE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RUDOLPH,J.CHEUNG,M.FRANKLIN,M.CASSIDY,E.GARY,F.BURSHTEYN,J.LOVE
REVDAT 1 28-SEP-11 3TQT 0
JRNL AUTH M.RUDOLPH,J.CHEUNG,M.FRANKLIN,M.CASSIDY,E.GARY,F.BURSHTEYN,
JRNL AUTH 2 J.LOVE
JRNL TITL STRUCTURE OF THE D-ALANINE-D-ALANINE LIGASE FROM COXIELLA
JRNL TITL 2 BURNETII
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 56794
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2875
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 39.6603 - 4.0441 0.97 5668 282 0.1712 0.1859
REMARK 3 2 4.0441 - 3.2104 0.99 5593 311 0.1681 0.2116
REMARK 3 3 3.2104 - 2.8047 0.99 5559 283 0.1873 0.2371
REMARK 3 4 2.8047 - 2.5483 0.99 5524 291 0.1981 0.2338
REMARK 3 5 2.5483 - 2.3657 0.99 5453 315 0.1898 0.2488
REMARK 3 6 2.3657 - 2.2262 0.99 5469 280 0.1825 0.2480
REMARK 3 7 2.2262 - 2.1148 0.98 5404 298 0.1798 0.2465
REMARK 3 8 2.1148 - 2.0227 0.97 5348 291 0.1834 0.2473
REMARK 3 9 2.0227 - 1.9448 0.96 5306 283 0.1900 0.2526
REMARK 3 10 1.9448 - 1.8800 0.83 4595 241 0.2186 0.2892
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 : 0.83
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 41.04
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.83710
REMARK 3 B22 (A**2) : -6.02470
REMARK 3 B33 (A**2) : 3.18760
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 : 0.006 5442
REMARK 3 ANGLE : 1.055 7379
REMARK 3 CHIRALITY : 0.068 856
REMARK 3 PLANARITY : 0.005 942
REMARK 3 DIHEDRAL : 14.269 2011
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 2:132)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.1891 62.5449 -8.4817
REMARK 3 T TENSOR
REMARK 3 T11: 0.2503 T22: 0.1562
REMARK 3 T33: 0.1986 T12: -0.0587
REMARK 3 T13: -0.0792 T23: 0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 1.0631 L22: 0.7483
REMARK 3 L33: 1.6763 L12: -0.5555
REMARK 3 L13: -0.0945 L23: -0.0181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0997 S12: -0.0943 S13: -0.1230
REMARK 3 S21: 0.2549 S22: -0.0389 S23: 0.0340
REMARK 3 S31: 0.0270 S32: -0.0780 S33: -0.0436
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 133:172)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.6017 43.6705 -32.7004
REMARK 3 T TENSOR
REMARK 3 T11: 0.1875 T22: 0.1735
REMARK 3 T33: 0.1847 T12: 0.0038
REMARK 3 T13: -0.0279 T23: -0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 1.6804 L22: 0.5175
REMARK 3 L33: 0.1403 L12: -0.0493
REMARK 3 L13: 0.0089 L23: -0.2758
REMARK 3 S TENSOR
REMARK 3 S11: 0.0644 S12: 0.0549 S13: -0.2601
REMARK 3 S21: -0.0566 S22: -0.1508 S23: 0.0093
REMARK 3 S31: 0.0211 S32: -0.0469 S33: 0.0293
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 173:224)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.0146 34.2665 -26.0960
REMARK 3 T TENSOR
REMARK 3 T11: 0.2226 T22: 0.1736
REMARK 3 T33: 0.3568 T12: -0.0150
REMARK 3 T13: -0.0294 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 1.8636 L22: 0.5701
REMARK 3 L33: 0.8777 L12: -0.0519
REMARK 3 L13: -0.1077 L23: 0.1131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0198 S12: -0.0347 S13: -0.5365
REMARK 3 S21: 0.1841 S22: -0.1693 S23: -0.1399
REMARK 3 S31: 0.0936 S32: -0.0097 S33: 0.0471
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 225:355)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3767 50.2066 -27.9039
REMARK 3 T TENSOR
REMARK 3 T11: 0.1660 T22: 0.1773
REMARK 3 T33: 0.2667 T12: 0.0061
REMARK 3 T13: -0.0305 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.7125 L22: 1.6164
REMARK 3 L33: 0.9713 L12: -0.2843
REMARK 3 L13: -0.1439 L23: 0.3612
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 0.0206 S13: -0.1178
REMARK 3 S21: -0.0377 S22: 0.0021 S23: -0.4185
REMARK 3 S31: 0.0500 S32: 0.1131 S33: 0.0172
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 356:371)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.6854 79.2236 -30.7631
REMARK 3 T TENSOR
REMARK 3 T11: 0.2640 T22: 0.1982
REMARK 3 T33: 0.2737 T12: 0.0181
REMARK 3 T13: -0.0306 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 1.0132 L22: 0.7925
REMARK 3 L33: 0.4658 L12: -0.2803
REMARK 3 L13: 0.1258 L23: -0.1514
REMARK 3 S TENSOR
REMARK 3 S11: 0.0247 S12: -0.2827 S13: 0.6469
REMARK 3 S21: 0.2101 S22: -0.0068 S23: -0.2437
REMARK 3 S31: -0.2061 S32: -0.1300 S33: 0.0363
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain B and resid 4:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5108 73.6549 -13.5424
REMARK 3 T TENSOR
REMARK 3 T11: 0.1890 T22: 0.2089
REMARK 3 T33: 0.1867 T12: 0.0265
REMARK 3 T13: 0.0436 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.0151 L22: 2.5041
REMARK 3 L33: 1.2722 L12: -0.8335
REMARK 3 L13: 0.0651 L23: 0.2884
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: -0.0995 S13: 0.0973
REMARK 3 S21: 0.1734 S22: -0.0030 S23: 0.0371
REMARK 3 S31: -0.2094 S32: -0.0514 S33: -0.0181
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain B and resid 100:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7626 60.2825 -28.2720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1701 T22: 0.1928
REMARK 3 T33: 0.1599 T12: 0.0361
REMARK 3 T13: -0.0382 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.8619 L22: 1.1208
REMARK 3 L33: 0.9233 L12: 0.0637
REMARK 3 L13: -0.3660 L23: 0.3961
REMARK 3 S TENSOR
REMARK 3 S11: 0.1066 S12: 0.0102 S13: -0.0251
REMARK 3 S21: -0.1817 S22: -0.0273 S23: 0.1130
REMARK 3 S31: -0.3040 S32: 0.0967 S33: -0.1130
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain B and resid 159:224)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4284 70.1618 -47.4729
REMARK 3 T TENSOR
REMARK 3 T11: 0.3374 T22: 0.3315
REMARK 3 T33: 0.1439 T12: -0.0165
REMARK 3 T13: 0.0095 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 1.3925 L22: 1.6706
REMARK 3 L33: 0.6043 L12: 0.3384
REMARK 3 L13: 0.1016 L23: -0.0549
REMARK 3 S TENSOR
REMARK 3 S11: -0.0621 S12: 0.5062 S13: 0.0532
REMARK 3 S21: -0.5391 S22: 0.1263 S23: -0.0833
REMARK 3 S31: -0.1171 S32: 0.1184 S33: -0.0620
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain B and resid 225:320)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8602 58.4658 -40.6552
REMARK 3 T TENSOR
REMARK 3 T11: 0.3002 T22: 0.2648
REMARK 3 T33: 0.2322 T12: 0.0417
REMARK 3 T13: -0.1419 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 1.3238 L22: 1.5266
REMARK 3 L33: 0.8477 L12: -0.0380
REMARK 3 L13: 0.5922 L23: 0.1612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0940 S12: 0.1942 S13: -0.0863
REMARK 3 S21: -0.3415 S22: 0.0437 S23: 0.3494
REMARK 3 S31: 0.0272 S32: 0.0457 S33: -0.0214
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain B and resid 321:368)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0048 56.5621 -22.2608
REMARK 3 T TENSOR
REMARK 3 T11: 0.1803 T22: 0.2024
REMARK 3 T33: 0.2432 T12: -0.0132
REMARK 3 T13: -0.0108 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.5399 L22: 1.7522
REMARK 3 L33: 1.3267 L12: 0.2538
REMARK 3 L13: -0.1824 L23: 0.1161
REMARK 3 S TENSOR
REMARK 3 S11: 0.1103 S12: 0.0061 S13: -0.1938
REMARK 3 S21: 0.0059 S22: -0.0698 S23: 0.5438
REMARK 3 S31: 0.1663 S32: -0.1844 S33: -0.0225
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 3TQT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB067807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56853
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37900
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: 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 (%): 42.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 5% PEG 3350, 30%
REMARK 280 PEG 200, SITTING DROP, TEMPERATURE 293K
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 34.11900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.28150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.72100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.28150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.11900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.72100
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: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 MET A 1
REMARK 465 ASN A 91
REMARK 465 GLY A 92
REMARK 465 ASP A 93
REMARK 465 GLY A 94
REMARK 465 GLY A 179
REMARK 465 THR A 180
REMARK 465 SER A 181
REMARK 465 HIS A 252
REMARK 465 ASP A 253
REMARK 465 TYR A 254
REMARK 465 TYR A 255
REMARK 465 SER A 256
REMARK 465 TYR A 257
REMARK 465 ASP A 258
REMARK 465 ALA A 259
REMARK 465 LYS A 260
REMARK 465 TYR A 261
REMARK 465 LEU A 262
REMARK 465 ASP A 263
REMARK 465 PRO A 264
REMARK 465 ASN A 265
REMARK 465 GLY A 266
REMARK 465 LEU A 372
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLY B 81
REMARK 465 ASP B 82
REMARK 465 ALA B 83
REMARK 465 ALA B 84
REMARK 465 ASN B 91
REMARK 465 GLY B 92
REMARK 465 PRO B 250
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 ASP B 253
REMARK 465 TYR B 254
REMARK 465 TYR B 255
REMARK 465 SER B 256
REMARK 465 TYR B 257
REMARK 465 ASP B 258
REMARK 465 ALA B 259
REMARK 465 LYS B 260
REMARK 465 TYR B 261
REMARK 465 LEU B 262
REMARK 465 ASP B 263
REMARK 465 PRO B 264
REMARK 465 ASN B 265
REMARK 465 GLY B 266
REMARK 465 ALA B 267
REMARK 465 SER B 272
REMARK 465 VAL B 273
REMARK 465 ASP B 274
REMARK 465 LEU B 275
REMARK 465 ALA B 369
REMARK 465 ARG B 370
REMARK 465 SER B 371
REMARK 465 LEU B 372
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 THR A 77 -163.95 -125.83
REMARK 500 GLN A 110 -43.42 74.94
REMARK 500 ASN A 237 -93.25 -109.58
REMARK 500 ALA A 239 73.58 -115.89
REMARK 500 ASP A 274 69.17 -101.07
REMARK 500 THR B 77 -167.37 -128.18
REMARK 500 GLN B 110 -20.26 69.18
REMARK 500 ASN B 237 -98.67 -110.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 534 DISTANCE = 5.68 ANGSTROMS
DBREF 3TQT A 1 372 UNP Q83BZ9 DDL_COXBU 1 372
DBREF 3TQT B 1 372 UNP Q83BZ9 DDL_COXBU 1 372
SEQRES 1 A 372 MET ALA GLU LYS LEU HIS ILE SER VAL LEU CYS GLY GLY
SEQRES 2 A 372 GLN SER THR GLU HIS GLU ILE SER ILE GLN SER ALA LYS
SEQRES 3 A 372 ASN ILE VAL ASN THR LEU ASP ALA ALA LYS TYR LEU ILE
SEQRES 4 A 372 SER VAL ILE PHE ILE ASP HIS VAL GLY ARG TRP TYR LEU
SEQRES 5 A 372 ILE ASP GLN PRO GLU MET PHE LEU ALA HIS SER PRO ASP
SEQRES 6 A 372 HIS LEU VAL LYS GLU GLY SER ALA ARG PRO ILE THR ILE
SEQRES 7 A 372 ALA PHE GLY ASP ALA ALA LYS PRO TRP GLN SER LEU ASN
SEQRES 8 A 372 GLY ASP GLY ARG ARG TYR SER ALA ASP CYS VAL PHE PRO
SEQRES 9 A 372 MET VAL HIS GLY THR GLN GLY GLU ASP GLY ALA LEU GLN
SEQRES 10 A 372 GLY LEU LEU GLU LEU LEU ASN LEU PRO TYR VAL GLY ALA
SEQRES 11 A 372 ASN VAL GLN SER SER ALA VAL CYS MET GLU LYS ASP LEU
SEQRES 12 A 372 THR LYS THR VAL LEU ARG ALA GLY GLY ILE PRO VAL VAL
SEQRES 13 A 372 ASP TRP HIS THR LEU SER PRO ARG ASP ALA THR GLU GLY
SEQRES 14 A 372 VAL TYR GLN ARG LEU LEU ASP ARG TRP GLY THR SER GLU
SEQRES 15 A 372 LEU PHE VAL LYS ALA VAL SER LEU GLY SER SER VAL ALA
SEQRES 16 A 372 THR LEU PRO VAL LYS THR GLU THR GLU PHE THR LYS ALA
SEQRES 17 A 372 VAL LYS GLU VAL PHE ARG TYR ASP ASP ARG LEU MET VAL
SEQRES 18 A 372 GLU PRO ARG ILE ARG GLY ARG GLU ILE GLU CYS ALA VAL
SEQRES 19 A 372 LEU GLY ASN GLY ALA PRO LYS ALA SER LEU PRO GLY GLU
SEQRES 20 A 372 ILE ILE PRO HIS HIS ASP TYR TYR SER TYR ASP ALA LYS
SEQRES 21 A 372 TYR LEU ASP PRO ASN GLY ALA THR THR THR THR SER VAL
SEQRES 22 A 372 ASP LEU SER GLU SER VAL THR LYS GLN ILE GLN GLN ILE
SEQRES 23 A 372 ALA ILE ASP ALA PHE LYS MET VAL HIS CYS SER GLY MET
SEQRES 24 A 372 ALA ARG VAL ASP PHE PHE VAL THR PRO ASN ASN LYS VAL
SEQRES 25 A 372 LEU VAL ASN GLU ILE ASN THR ILE PRO GLY PHE THR ASN
SEQRES 26 A 372 ILE SER MET TYR PRO LYS MET TRP GLU ALA SER GLY LEU
SEQRES 27 A 372 PRO CYS PRO ASN LEU LEU ASP GLN LEU ILE GLU LEU ALA
SEQRES 28 A 372 ILE ASP ARG HIS GLN GLU GLN GLN LYS LEU ILE ARG CYS
SEQRES 29 A 372 TYR GLU VAL LYS ALA ARG SER LEU
SEQRES 1 B 372 MET ALA GLU LYS LEU HIS ILE SER VAL LEU CYS GLY GLY
SEQRES 2 B 372 GLN SER THR GLU HIS GLU ILE SER ILE GLN SER ALA LYS
SEQRES 3 B 372 ASN ILE VAL ASN THR LEU ASP ALA ALA LYS TYR LEU ILE
SEQRES 4 B 372 SER VAL ILE PHE ILE ASP HIS VAL GLY ARG TRP TYR LEU
SEQRES 5 B 372 ILE ASP GLN PRO GLU MET PHE LEU ALA HIS SER PRO ASP
SEQRES 6 B 372 HIS LEU VAL LYS GLU GLY SER ALA ARG PRO ILE THR ILE
SEQRES 7 B 372 ALA PHE GLY ASP ALA ALA LYS PRO TRP GLN SER LEU ASN
SEQRES 8 B 372 GLY ASP GLY ARG ARG TYR SER ALA ASP CYS VAL PHE PRO
SEQRES 9 B 372 MET VAL HIS GLY THR GLN GLY GLU ASP GLY ALA LEU GLN
SEQRES 10 B 372 GLY LEU LEU GLU LEU LEU ASN LEU PRO TYR VAL GLY ALA
SEQRES 11 B 372 ASN VAL GLN SER SER ALA VAL CYS MET GLU LYS ASP LEU
SEQRES 12 B 372 THR LYS THR VAL LEU ARG ALA GLY GLY ILE PRO VAL VAL
SEQRES 13 B 372 ASP TRP HIS THR LEU SER PRO ARG ASP ALA THR GLU GLY
SEQRES 14 B 372 VAL TYR GLN ARG LEU LEU ASP ARG TRP GLY THR SER GLU
SEQRES 15 B 372 LEU PHE VAL LYS ALA VAL SER LEU GLY SER SER VAL ALA
SEQRES 16 B 372 THR LEU PRO VAL LYS THR GLU THR GLU PHE THR LYS ALA
SEQRES 17 B 372 VAL LYS GLU VAL PHE ARG TYR ASP ASP ARG LEU MET VAL
SEQRES 18 B 372 GLU PRO ARG ILE ARG GLY ARG GLU ILE GLU CYS ALA VAL
SEQRES 19 B 372 LEU GLY ASN GLY ALA PRO LYS ALA SER LEU PRO GLY GLU
SEQRES 20 B 372 ILE ILE PRO HIS HIS ASP TYR TYR SER TYR ASP ALA LYS
SEQRES 21 B 372 TYR LEU ASP PRO ASN GLY ALA THR THR THR THR SER VAL
SEQRES 22 B 372 ASP LEU SER GLU SER VAL THR LYS GLN ILE GLN GLN ILE
SEQRES 23 B 372 ALA ILE ASP ALA PHE LYS MET VAL HIS CYS SER GLY MET
SEQRES 24 B 372 ALA ARG VAL ASP PHE PHE VAL THR PRO ASN ASN LYS VAL
SEQRES 25 B 372 LEU VAL ASN GLU ILE ASN THR ILE PRO GLY PHE THR ASN
SEQRES 26 B 372 ILE SER MET TYR PRO LYS MET TRP GLU ALA SER GLY LEU
SEQRES 27 B 372 PRO CYS PRO ASN LEU LEU ASP GLN LEU ILE GLU LEU ALA
SEQRES 28 B 372 ILE ASP ARG HIS GLN GLU GLN GLN LYS LEU ILE ARG CYS
SEQRES 29 B 372 TYR GLU VAL LYS ALA ARG SER LEU
FORMUL 3 HOH *490(H2 O)
HELIX 1 1 GLU A 17 LEU A 32 1 16
HELIX 2 2 GLN A 55 HIS A 62 1 8
HELIX 3 3 SER A 63 GLY A 71 1 9
HELIX 4 4 GLY A 114 LEU A 123 1 10
HELIX 5 5 ASN A 131 GLU A 140 1 10
HELIX 6 6 GLU A 140 GLY A 151 1 12
HELIX 7 7 GLY A 169 TRP A 178 1 10
HELIX 8 8 SER A 192 VAL A 194 5 3
HELIX 9 9 THR A 201 PHE A 213 1 13
HELIX 10 10 SER A 276 VAL A 294 1 19
HELIX 11 11 SER A 327 SER A 336 1 10
HELIX 12 12 PRO A 339 SER A 371 1 33
HELIX 13 13 GLU B 17 LEU B 32 1 16
HELIX 14 14 GLN B 55 HIS B 62 1 8
HELIX 15 15 SER B 63 GLY B 71 1 9
HELIX 16 16 GLY B 114 LEU B 123 1 10
HELIX 17 17 ASN B 131 GLU B 140 1 10
HELIX 18 18 GLU B 140 GLY B 151 1 12
HELIX 19 19 GLY B 169 GLY B 179 1 11
HELIX 20 20 SER B 192 VAL B 194 5 3
HELIX 21 21 THR B 201 PHE B 213 1 13
HELIX 22 22 GLU B 277 VAL B 294 1 18
HELIX 23 23 SER B 327 SER B 336 1 10
HELIX 24 24 PRO B 339 LYS B 368 1 30
SHEET 1 A 7 ARG A 96 TYR A 97 0
SHEET 2 A 7 TRP A 87 SER A 89 -1 N TRP A 87 O TYR A 97
SHEET 3 A 7 ARG A 74 ILE A 78 -1 N THR A 77 O GLN A 88
SHEET 4 A 7 TRP A 50 ILE A 53 -1 N LEU A 52 O ARG A 74
SHEET 5 A 7 TYR A 37 ILE A 44 -1 N VAL A 41 O ILE A 53
SHEET 6 A 7 LEU A 5 GLY A 12 1 N VAL A 9 O ILE A 42
SHEET 7 A 7 CYS A 101 PRO A 104 1 O PHE A 103 N SER A 8
SHEET 1 B 4 HIS A 159 LEU A 161 0
SHEET 2 B 4 LEU A 219 PRO A 223 -1 O VAL A 221 N HIS A 159
SHEET 3 B 4 LEU A 183 ALA A 187 -1 N PHE A 184 O GLU A 222
SHEET 4 B 4 THR A 196 VAL A 199 -1 O LEU A 197 N VAL A 185
SHEET 1 C 4 LYS A 241 ALA A 242 0
SHEET 2 C 4 ARG A 228 GLY A 236 -1 N LEU A 235 O LYS A 241
SHEET 3 C 4 GLY A 246 ILE A 249 -1 O GLY A 246 N GLU A 231
SHEET 4 C 4 THR A 268 THR A 270 -1 O THR A 268 N ILE A 249
SHEET 1 D 4 LYS A 241 ALA A 242 0
SHEET 2 D 4 ARG A 228 GLY A 236 -1 N LEU A 235 O LYS A 241
SHEET 3 D 4 GLY A 298 VAL A 306 -1 O PHE A 304 N ILE A 230
SHEET 4 D 4 VAL A 312 ASN A 318 -1 O ASN A 315 N ASP A 303
SHEET 1 E 7 ARG B 96 TYR B 97 0
SHEET 2 E 7 TRP B 87 SER B 89 -1 N TRP B 87 O TYR B 97
SHEET 3 E 7 ARG B 74 ILE B 78 -1 N THR B 77 O GLN B 88
SHEET 4 E 7 TRP B 50 ILE B 53 -1 N LEU B 52 O ARG B 74
SHEET 5 E 7 TYR B 37 ILE B 44 -1 N VAL B 41 O ILE B 53
SHEET 6 E 7 LEU B 5 GLY B 12 1 N VAL B 9 O ILE B 42
SHEET 7 E 7 CYS B 101 PRO B 104 1 O PHE B 103 N SER B 8
SHEET 1 F 4 HIS B 159 LEU B 161 0
SHEET 2 F 4 LEU B 219 PRO B 223 -1 O VAL B 221 N HIS B 159
SHEET 3 F 4 LEU B 183 ALA B 187 -1 N LYS B 186 O MET B 220
SHEET 4 F 4 THR B 196 VAL B 199 -1 O VAL B 199 N LEU B 183
SHEET 1 G 3 LYS B 241 ALA B 242 0
SHEET 2 G 3 ARG B 228 GLY B 236 -1 N LEU B 235 O LYS B 241
SHEET 3 G 3 GLY B 246 ILE B 248 -1 O GLY B 246 N GLU B 231
SHEET 1 H 4 LYS B 241 ALA B 242 0
SHEET 2 H 4 ARG B 228 GLY B 236 -1 N LEU B 235 O LYS B 241
SHEET 3 H 4 GLY B 298 VAL B 306 -1 O PHE B 304 N ILE B 230
SHEET 4 H 4 VAL B 312 ASN B 318 -1 O ASN B 315 N ASP B 303
CRYST1 68.238 97.442 106.563 90.00 90.00 90.00 P 21 21 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 0.014655 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009384 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
