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HEADER HYDROLASE 02-OCT-09 2WUD
TITLE CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE
COMPND 3 HYDROLASE BPHD;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: HSAD, 2-HYDROXY-6-PHENYLHEXA-2\,4-DIENOIC ACID
COMPND 6 HYDROLASE;
COMPND 7 EC: 3.7.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.LACK,K.C.YAM,E.D.LOWE,G.P.HORSMAN,R.OWEN,E.SIM,
AUTHOR 2 L.D.ELTIS
REVDAT 2 10-NOV-09 2WUD 1 JRNL REMARK
REVDAT 1 20-OCT-09 2WUD 0
JRNL AUTH N.A.LACK,K.C.YAM,E.D.LOWE,G.P.HORSMAN,R.OWEN,E.SIM,
JRNL AUTH 2 L.D.ELTIS
JRNL TITL CHARACTERIZATION OF A C-C HYDROLASE FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS INVOLVED IN CHOLESTEROL
JRNL TITL 3 METABOLISM
JRNL REF J.BIOL.CHEM. 2009
JRNL REFN ESSN 1083-351X
JRNL PMID 19875455
JRNL DOI 10.1074/JBC.M109.058081
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.1
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.8
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 35439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1779
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 49.7929 - 4.9363 0.97 2663 133 0.1776 0.1930
REMARK 3 2 4.9363 - 3.9186 1.00 2659 112 0.1408 0.1440
REMARK 3 3 3.9186 - 3.4234 1.00 2616 136 0.1572 0.1929
REMARK 3 4 3.4234 - 3.1105 1.00 2590 147 0.1758 0.2349
REMARK 3 5 3.1105 - 2.8875 1.00 2574 159 0.1808 0.2658
REMARK 3 6 2.8875 - 2.7173 0.99 2569 135 0.2064 0.2288
REMARK 3 7 2.7173 - 2.5812 0.99 2582 142 0.2118 0.2529
REMARK 3 8 2.5812 - 2.4689 1.00 2568 140 0.2065 0.2841
REMARK 3 9 2.4689 - 2.3738 1.00 2576 133 0.2127 0.2658
REMARK 3 10 2.3738 - 2.2919 1.00 2580 141 0.2184 0.2846
REMARK 3 11 2.2919 - 2.2203 1.00 2573 137 0.2296 0.2909
REMARK 3 12 2.2203 - 2.1568 1.00 2568 138 0.2346 0.2719
REMARK 3 13 2.1568 - 2.1000 0.99 2542 126 0.2358 0.2936
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 : 0.347
REMARK 3 B_SOL : 44.943
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.30
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.86
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 : 0.009 NULL
REMARK 3 ANGLE : 0.746 NULL
REMARK 3 CHIRALITY : 0.066 NULL
REMARK 3 PLANARITY : 0.003 NULL
REMARK 3 DIHEDRAL : 10.285 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 7:36)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9639 -7.4300 17.2730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0808 T22: 0.1583
REMARK 3 T33: 0.0980 T12: -0.0589
REMARK 3 T13: 0.0037 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.9263 L22: 1.6073
REMARK 3 L33: 1.1858 L12: 0.2766
REMARK 3 L13: -0.4568 L23: 0.1103
REMARK 3 S TENSOR
REMARK 3 S11: -0.1008 S22: 0.2160 S33: -0.0693
REMARK 3 S12: 0.3360 S13: 0.0994 S21: -0.1915
REMARK 3 S23: -0.3042 S31: -0.1946 S32: 0.0388
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 37:84)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8419 -14.9273 22.1954
REMARK 3 T TENSOR
REMARK 3 T11: 0.0930 T22: 0.0964
REMARK 3 T33: 0.1026 T12: -0.0363
REMARK 3 T13: 0.0055 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 1.0499 L22: 1.0539
REMARK 3 L33: 0.1931 L12: 0.6237
REMARK 3 L13: -0.3586 L23: -0.3350
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S22: -0.0155 S33: 0.0383
REMARK 3 S12: -0.0954 S13: -0.0747 S21: -0.1307
REMARK 3 S23: -0.2203 S31: 0.0837 S32: -0.0508
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 85:156)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.6005 -11.5292 31.8675
REMARK 3 T TENSOR
REMARK 3 T11: 0.0905 T22: 0.0727
REMARK 3 T33: 0.0908 T12: -0.0290
REMARK 3 T13: -0.0096 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.7669 L22: 0.2461
REMARK 3 L33: 0.8284 L12: -0.0857
REMARK 3 L13: -0.1578 L23: -0.2568
REMARK 3 S TENSOR
REMARK 3 S11: -0.0402 S22: -0.0054 S33: 0.0302
REMARK 3 S12: 0.1177 S13: 0.0430 S21: -0.0364
REMARK 3 S23: -0.0452 S31: -0.0008 S32: 0.0317
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 157:205)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5303 -23.9953 33.9934
REMARK 3 T TENSOR
REMARK 3 T11: 0.0823 T22: 0.1699
REMARK 3 T33: 0.1613 T12: -0.0203
REMARK 3 T13: 0.0154 T23: 0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.3740 L22: 0.7834
REMARK 3 L33: 0.1971 L12: -0.4941
REMARK 3 L13: -0.0836 L23: 0.0627
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S22: 0.0130 S33: 0.0129
REMARK 3 S12: 0.0593 S13: -0.0543 S21: 0.0212
REMARK 3 S23: -0.2452 S31: -0.0424 S32: 0.1795
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 206:213)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1638 -8.0560 42.2106
REMARK 3 T TENSOR
REMARK 3 T11: 0.1369 T22: 0.2515
REMARK 3 T33: 0.1554 T12: -0.0361
REMARK 3 T13: -0.0745 T23: 0.0889
REMARK 3 L TENSOR
REMARK 3 L11: 3.4174 L22: 0.0733
REMARK 3 L33: 5.6544 L12: 1.2881
REMARK 3 L13: -6.0632 L23: -1.3689
REMARK 3 S TENSOR
REMARK 3 S11: 0.2929 S22: -0.4827 S33: 0.2354
REMARK 3 S12: -0.8639 S13: -0.5219 S21: 0.0665
REMARK 3 S23: -0.0561 S31: -0.3362 S32: 0.7804
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 214:230)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.4819 -9.0986 40.8924
REMARK 3 T TENSOR
REMARK 3 T11: 0.1319 T22: 0.1232
REMARK 3 T33: 0.0700 T12: -0.0373
REMARK 3 T13: -0.0064 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 0.8272 L22: -0.0958
REMARK 3 L33: 1.8024 L12: 0.1924
REMARK 3 L13: 0.4337 L23: 0.9320
REMARK 3 S TENSOR
REMARK 3 S11: -0.1769 S22: 0.1102 S33: 0.0541
REMARK 3 S12: 0.2376 S13: 0.1284 S21: -0.1215
REMARK 3 S23: 0.0271 S31: -0.2975 S32: 0.3702
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 231:288)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2256 -25.8258 29.8621
REMARK 3 T TENSOR
REMARK 3 T11: 0.0693 T22: 0.0797
REMARK 3 T33: 0.0447 T12: -0.0234
REMARK 3 T13: 0.0065 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.0626 L22: 0.8472
REMARK 3 L33: 0.5343 L12: 0.1955
REMARK 3 L13: 0.2296 L23: -0.3635
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S22: 0.0540 S33: 0.0332
REMARK 3 S12: 0.0492 S13: -0.0209 S21: -0.0837
REMARK 3 S23: -0.0552 S31: 0.0222 S32: 0.0167
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 7:37)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7854 -41.5917 28.4007
REMARK 3 T TENSOR
REMARK 3 T11: 0.0796 T22: 0.2170
REMARK 3 T33: 0.1786 T12: 0.0047
REMARK 3 T13: -0.0834 T23: -0.1259
REMARK 3 L TENSOR
REMARK 3 L11: 2.2370 L22: 1.5032
REMARK 3 L33: 2.7800 L12: 0.0273
REMARK 3 L13: -0.3130 L23: 0.8893
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S22: -0.0019 S33: -0.0845
REMARK 3 S12: -0.8303 S13: 0.4981 S21: 0.1922
REMARK 3 S23: -0.3004 S31: 0.0087 S32: 0.2105
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 38:84)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3507 -42.2194 23.1758
REMARK 3 T TENSOR
REMARK 3 T11: 0.1071 T22: 0.1475
REMARK 3 T33: 0.2142 T12: -0.0002
REMARK 3 T13: -0.0344 T23: -0.0882
REMARK 3 L TENSOR
REMARK 3 L11: 1.6400 L22: -0.2205
REMARK 3 L33: 0.6699 L12: -0.0193
REMARK 3 L13: 0.8301 L23: 0.6570
REMARK 3 S TENSOR
REMARK 3 S11: -0.0980 S22: 0.0251 S33: 0.0946
REMARK 3 S12: -0.3460 S13: 0.4858 S21: 0.0150
REMARK 3 S23: -0.0617 S31: -0.1084 S32: -0.1601
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 85:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4273 -50.4119 13.7120
REMARK 3 T TENSOR
REMARK 3 T11: 0.0923 T22: 0.1325
REMARK 3 T33: 0.1388 T12: -0.0287
REMARK 3 T13: -0.0096 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.3930 L22: 0.1056
REMARK 3 L33: 0.5240 L12: -0.5296
REMARK 3 L13: 0.3973 L23: 0.2560
REMARK 3 S TENSOR
REMARK 3 S11: -0.0169 S22: 0.0052 S33: 0.0063
REMARK 3 S12: -0.1209 S13: 0.1877 S21: 0.0130
REMARK 3 S23: -0.1121 S31: 0.0073 S32: -0.0456
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 157:205)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5975 -30.9044 11.7318
REMARK 3 T TENSOR
REMARK 3 T11: 0.2031 T22: 0.0608
REMARK 3 T33: 0.2120 T12: -0.0333
REMARK 3 T13: -0.0196 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.6389 L22: -0.5165
REMARK 3 L33: 0.3617 L12: -0.0967
REMARK 3 L13: -0.1706 L23: 0.6580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S22: -0.0313 S33: 0.0395
REMARK 3 S12: -0.0532 S13: 0.0966 S21: 0.0259
REMARK 3 S23: 0.1646 S31: -0.0810 S32: 0.0572
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 206:213)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0426 -37.2878 3.2148
REMARK 3 T TENSOR
REMARK 3 T11: 0.6305 T22: 0.5010
REMARK 3 T33: 0.3512 T12: 0.0809
REMARK 3 T13: -0.1201 T23: -0.0677
REMARK 3 L TENSOR
REMARK 3 L11: 0.2036 L22: -1.9320
REMARK 3 L33: 1.3412 L12: -0.3548
REMARK 3 L13: -3.3200 L23: 9.3203
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S22: 0.2419 S33: -0.1642
REMARK 3 S12: 0.5554 S13: -0.0743 S21: -0.5491
REMARK 3 S23: 0.0281 S31: -0.6554 S32: -0.1243
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 214:230)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5649 -56.3454 4.6993
REMARK 3 T TENSOR
REMARK 3 T11: 0.1009 T22: 0.1799
REMARK 3 T33: 0.0857 T12: -0.0218
REMARK 3 T13: -0.0157 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.7108 L22: 0.9757
REMARK 3 L33: 0.6173 L12: 0.1535
REMARK 3 L13: -0.7379 L23: 0.0829
REMARK 3 S TENSOR
REMARK 3 S11: 0.1097 S22: -0.0342 S33: -0.0784
REMARK 3 S12: 0.0092 S13: -0.0456 S21: -0.0507
REMARK 3 S23: 0.0094 S31: -0.1512 S32: 0.2140
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 231:288)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0307 -53.5793 15.8107
REMARK 3 T TENSOR
REMARK 3 T11: 0.0580 T22: 0.0970
REMARK 3 T33: 0.0520 T12: -0.0239
REMARK 3 T13: -0.0124 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.0580 L22: 0.3670
REMARK 3 L33: 0.2278 L12: -0.0939
REMARK 3 L13: 0.2881 L23: 0.0649
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S22: -0.0159 S33: 0.0107
REMARK 3 S12: -0.2243 S13: 0.0230 S21: 0.0709
REMARK 3 S23: -0.0209 S31: 0.0070 S32: -0.0253
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)
REMARK 3 SELECTION : (CHAIN B)
REMARK 3 ATOM PAIRS NUMBER : 2185
REMARK 3 RMSD : 0.311
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2WUD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-09.
REMARK 100 THE PDBE ID CODE IS EBI-41325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 : BRUKER MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MONTEL 200 OPTICS
REMARK 200 OPTICS : MONTEL 200 OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35484
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 59.80
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.2
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : 0.32
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.80
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: PDB ENTRY 2VF2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.9
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM KSCN, 24% PEG 3350, 100MM
REMARK 280 BIS-TRIS PROPANE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.38250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 91.29600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.38250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 91.29600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.38250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 91.29600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.38250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 91.29600
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 91.29600
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 91.29600
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 91.29600
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 91.29600
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 59.38250
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 59.38250
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 59.38250
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 56.12700
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 59.38250
REMARK 290 SMTRY3 16 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 GENERATING THE BIOMOLECULE
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.96 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -56.12700
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 91.29600
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 -0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 -59.38250
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 91.29600
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -56.12700
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 -59.38250
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.48 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 -0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -118.76500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 -118.76500
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 114 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, SER 114 TO ALA
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 THR A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 GLU A 6
REMARK 465 GLY A 289
REMARK 465 GLY A 290
REMARK 465 ARG A 291
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 THR B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 GLY B 289
REMARK 465 GLY B 290
REMARK 465 ARG B 291
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 187 CD GLU A 187 OE1 -0.101
REMARK 500 GLU A 200 CD GLU A 200 OE2 -0.088
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 133 CD - NE - CZ ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 133 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG B 133 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG B 133 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
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 ALA A 114 -124.66 51.57
REMARK 500 VAL A 243 -61.52 -100.71
REMARK 500 LYS B 81 79.65 -117.54
REMARK 500 ALA B 114 -118.30 53.05
REMARK 500 VAL B 243 -62.63 -100.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 113 21.8 L L OUTSIDE RANGE
REMARK 500 ASN B 113 25.0 L L OUTSIDE RANGE
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B1289
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VF2 RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HSAD FROM
REMARK 900 MYCOBACTERIUM TUBERCULOSIS
REMARK 900 RELATED ID: 2WUE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
REMARK 900 WITH HOPODA
REMARK 900 RELATED ID: 2WUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
REMARK 900 WITH 4,9DSHA
REMARK 900 RELATED ID: 2WUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S114A MUTANT OF HSAD
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
REMARK 900 WITH HOPDA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 S114A MUTANT
DBREF 2WUD A 1 291 UNP P96851 P96851_MYCTU 1 291
DBREF 2WUD B 1 291 UNP P96851 P96851_MYCTU 1 291
SEQADV 2WUD ALA A 114 UNP P96851 SER 114 ENGINEERED MUTATION
SEQADV 2WUD ALA B 114 UNP P96851 SER 114 ENGINEERED MUTATION
SEQRES 1 A 291 MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER
SEQRES 2 A 291 ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU
SEQRES 3 A 291 HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL
SEQRES 4 A 291 VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP
SEQRES 5 A 291 THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS
SEQRES 6 A 291 PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS
SEQRES 7 A 291 SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR
SEQRES 8 A 291 ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY
SEQRES 9 A 291 LEU GLY ARG VAL PRO LEU VAL GLY ASN ALA LEU GLY GLY
SEQRES 10 A 291 GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG
SEQRES 11 A 291 ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER
SEQRES 12 A 291 ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS
SEQRES 13 A 291 ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN
SEQRES 14 A 291 LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN
SEQRES 15 A 291 LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU
SEQRES 16 A 291 ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET
SEQRES 17 A 291 GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET
SEQRES 18 A 291 MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU
SEQRES 19 A 291 LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP
SEQRES 20 A 291 GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN
SEQRES 21 A 291 LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL
SEQRES 22 A 291 GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE
SEQRES 23 A 291 LEU GLY GLY GLY ARG
SEQRES 1 B 291 MET THR ALA THR GLU GLU LEU THR PHE GLU SER THR SER
SEQRES 2 B 291 ARG PHE ALA GLU VAL ASP VAL ASP GLY PRO LEU LYS LEU
SEQRES 3 B 291 HIS TYR HIS GLU ALA GLY VAL GLY ASN ASP GLN THR VAL
SEQRES 4 B 291 VAL LEU LEU HIS GLY GLY GLY PRO GLY ALA ALA SER TRP
SEQRES 5 B 291 THR ASN PHE SER ARG ASN ILE ALA VAL LEU ALA ARG HIS
SEQRES 6 B 291 PHE HIS VAL LEU ALA VAL ASP GLN PRO GLY TYR GLY HIS
SEQRES 7 B 291 SER ASP LYS ARG ALA GLU HIS GLY GLN PHE ASN ARG TYR
SEQRES 8 B 291 ALA ALA MET ALA LEU LYS GLY LEU PHE ASP GLN LEU GLY
SEQRES 9 B 291 LEU GLY ARG VAL PRO LEU VAL GLY ASN ALA LEU GLY GLY
SEQRES 10 B 291 GLY THR ALA VAL ARG PHE ALA LEU ASP TYR PRO ALA ARG
SEQRES 11 B 291 ALA GLY ARG LEU VAL LEU MET GLY PRO GLY GLY LEU SER
SEQRES 12 B 291 ILE ASN LEU PHE ALA PRO ASP PRO THR GLU GLY VAL LYS
SEQRES 13 B 291 ARG LEU SER LYS PHE SER VAL ALA PRO THR ARG GLU ASN
SEQRES 14 B 291 LEU GLU ALA PHE LEU ARG VAL MET VAL TYR ASP LYS ASN
SEQRES 15 B 291 LEU ILE THR PRO GLU LEU VAL ASP GLN ARG PHE ALA LEU
SEQRES 16 B 291 ALA SER THR PRO GLU SER LEU THR ALA THR ARG ALA MET
SEQRES 17 B 291 GLY LYS SER PHE ALA GLY ALA ASP PHE GLU ALA GLY MET
SEQRES 18 B 291 MET TRP ARG GLU VAL TYR ARG LEU ARG GLN PRO VAL LEU
SEQRES 19 B 291 LEU ILE TRP GLY ARG GLU ASP ARG VAL ASN PRO LEU ASP
SEQRES 20 B 291 GLY ALA LEU VAL ALA LEU LYS THR ILE PRO ARG ALA GLN
SEQRES 21 B 291 LEU HIS VAL PHE GLY GLN CYS GLY HIS TRP VAL GLN VAL
SEQRES 22 B 291 GLU LYS PHE ASP GLU PHE ASN LYS LEU THR ILE GLU PHE
SEQRES 23 B 291 LEU GLY GLY GLY ARG
HET SCN A1289 3
HET SCN B1289 3
HETNAM SCN THIOCYANATE ION
FORMUL 3 SCN 2(C N S 1-)
FORMUL 4 HOH *275(H2 O)
HELIX 1 1 THR A 8 THR A 12 1 5
HELIX 2 2 ALA A 50 PHE A 55 1 6
HELIX 3 3 ASN A 58 ARG A 64 1 7
HELIX 4 4 GLN A 87 LYS A 97 1 11
HELIX 5 5 THR A 119 TYR A 127 1 9
HELIX 6 6 VAL A 155 ALA A 164 1 10
HELIX 7 7 THR A 166 VAL A 176 1 11
HELIX 8 8 ASP A 180 ILE A 184 5 5
HELIX 9 9 THR A 185 SER A 197 1 13
HELIX 10 10 THR A 198 MET A 208 1 11
HELIX 11 11 MET A 221 GLU A 225 5 5
HELIX 12 12 GLU A 225 LEU A 229 5 5
HELIX 13 13 ALA A 249 ILE A 256 1 8
HELIX 14 14 TRP A 270 LYS A 275 1 6
HELIX 15 15 LYS A 275 LEU A 287 1 13
HELIX 16 16 THR B 8 THR B 12 1 5
HELIX 17 17 ALA B 50 PHE B 55 1 6
HELIX 18 18 ASN B 58 ARG B 64 1 7
HELIX 19 19 GLN B 87 LYS B 97 1 11
HELIX 20 20 THR B 119 TYR B 127 1 9
HELIX 21 21 PRO B 128 ALA B 131 5 4
HELIX 22 22 VAL B 155 ALA B 164 1 10
HELIX 23 23 THR B 166 VAL B 176 1 11
HELIX 24 24 ASP B 180 ILE B 184 5 5
HELIX 25 25 THR B 185 SER B 197 1 13
HELIX 26 26 THR B 198 MET B 208 1 11
HELIX 27 27 MET B 221 GLU B 225 5 5
HELIX 28 28 GLU B 225 LEU B 229 5 5
HELIX 29 29 ALA B 249 ILE B 256 1 8
HELIX 30 30 TRP B 270 LYS B 275 1 6
HELIX 31 31 LYS B 275 LEU B 287 1 13
SHEET 1 AA 5 SER A 13 VAL A 18 0
SHEET 2 AA 5 LEU A 24 ALA A 31 -1 O LEU A 24 N VAL A 18
SHEET 3 AA 5 HIS A 67 VAL A 71 -1 O VAL A 68 N ALA A 31
SHEET 4 AA 5 THR A 38 LEU A 42 1 O VAL A 39 N LEU A 69
SHEET 5 AA 5 LEU A 110 VAL A 111 1 O VAL A 111 N LEU A 42
SHEET 1 AB 3 LEU A 134 LEU A 136 0
SHEET 2 AB 3 VAL A 233 TRP A 237 1 O LEU A 234 N LEU A 136
SHEET 3 AB 3 ALA A 259 VAL A 263 1 O GLN A 260 N LEU A 235
SHEET 1 BA 5 SER B 13 VAL B 18 0
SHEET 2 BA 5 LEU B 24 ALA B 31 -1 O LEU B 24 N VAL B 18
SHEET 3 BA 5 HIS B 67 VAL B 71 -1 O VAL B 68 N ALA B 31
SHEET 4 BA 5 THR B 38 LEU B 42 1 O VAL B 39 N LEU B 69
SHEET 5 BA 5 LEU B 110 VAL B 111 1 O VAL B 111 N LEU B 42
SHEET 1 BB 3 LEU B 134 LEU B 136 0
SHEET 2 BB 3 VAL B 233 TRP B 237 1 O LEU B 234 N LEU B 136
SHEET 3 BB 3 ALA B 259 VAL B 263 1 O GLN B 260 N LEU B 235
CISPEP 1 ASP A 150 PRO A 151 0 -0.56
CISPEP 2 ASP B 150 PRO B 151 0 -0.29
SITE 1 AC1 6 LYS A 97 TYR A 127 PRO A 128 ALA A 129
SITE 2 AC1 6 ARG A 130 ARG B 130
SITE 1 AC2 1 ARG B 57
CRYST1 112.254 118.765 182.592 90.00 90.00 90.00 F 2 2 2 32
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 0.008908 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005477 0.00000
MTRIX1 1 0.034051 0.999419 0.001446 31.16240 1
MTRIX2 1 0.999372 -0.034035 -0.009898 -31.52060 1
MTRIX3 1 -0.009844 0.001782 -0.999950 45.83120 1
END |