HEADER TRANSFERASE 13-MAY-12 4F5M
TITLE WILD-TYPE E. COLI ASPARTATE AMINOTRANSFERASE: A TEMPLATE FOR THE
TITLE 2 INTERCONVERSION OF SUBSTRATE SPECIFICITY AND ACTIVITY TO TYROSINE
TITLE 3 AMINOTRANSFERASE BY THE JANUS ALGORITHM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ASPAT, TRANSAMINASE A;
COMPND 5 EC: 2.6.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: AAT, ASPC, B0928, JW0911;
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: PET45B
KEYWDS AMINOTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.ADDINGTON,A.J.FISHER,M.D.TONEY
REVDAT 4 24-APR-13 4F5M 1 JRNL
REVDAT 3 27-FEB-13 4F5M 1 JRNL
REVDAT 2 20-FEB-13 4F5M 1 REMARK
REVDAT 1 13-FEB-13 4F5M 0
JRNL AUTH T.A.ADDINGTON,R.W.MERTZ,J.B.SIEGEL,J.M.THOMPSON,A.J.FISHER,
JRNL AUTH 2 V.FILKOV,N.M.FLEISCHMAN,A.A.SUEN,C.ZHANG,M.D.TONEY
JRNL TITL JANUS: PREDICTION AND RANKING OF MUTATIONS REQUIRED FOR
JRNL TITL 2 FUNCTIONAL INTERCONVERSION OF ENZYMES.
JRNL REF J.MOL.BIOL. V. 425 1378 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23396064
JRNL DOI 10.1016/J.JMB.2013.01.034
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 108082
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5418
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 37.1012 - 5.1226 0.92 3464 215 0.1905 0.2058
REMARK 3 2 5.1226 - 4.0676 0.99 3596 182 0.1435 0.1654
REMARK 3 3 4.0676 - 3.5539 0.99 3558 183 0.1525 0.1875
REMARK 3 4 3.5539 - 3.2291 0.99 3539 171 0.1764 0.2172
REMARK 3 5 3.2291 - 2.9978 0.99 3537 173 0.1766 0.2094
REMARK 3 6 2.9978 - 2.8211 0.99 3492 181 0.1648 0.1936
REMARK 3 7 2.8211 - 2.6799 0.98 3470 178 0.1658 0.1991
REMARK 3 8 2.6799 - 2.5633 0.98 3487 177 0.1708 0.2023
REMARK 3 9 2.5633 - 2.4646 0.98 3452 175 0.1797 0.2156
REMARK 3 10 2.4646 - 2.3796 0.98 3445 192 0.1740 0.2329
REMARK 3 11 2.3796 - 2.3052 0.98 3458 169 0.1682 0.2192
REMARK 3 12 2.3052 - 2.2393 0.98 3432 179 0.1725 0.1981
REMARK 3 13 2.2393 - 2.1803 0.98 3393 204 0.1646 0.1894
REMARK 3 14 2.1803 - 2.1272 0.98 3426 173 0.1683 0.2303
REMARK 3 15 2.1272 - 2.0788 0.97 3396 185 0.1778 0.2384
REMARK 3 16 2.0788 - 2.0346 0.98 3448 180 0.1769 0.1940
REMARK 3 17 2.0346 - 1.9939 0.97 3365 165 0.1802 0.2636
REMARK 3 18 1.9939 - 1.9562 0.97 3415 192 0.1880 0.2310
REMARK 3 19 1.9562 - 1.9213 0.97 3367 172 0.1896 0.2381
REMARK 3 20 1.9213 - 1.8887 0.97 3408 174 0.1937 0.2088
REMARK 3 21 1.8887 - 1.8583 0.97 3391 163 0.2020 0.2497
REMARK 3 22 1.8583 - 1.8297 0.97 3363 172 0.2072 0.2711
REMARK 3 23 1.8297 - 1.8028 0.97 3378 194 0.2102 0.2319
REMARK 3 24 1.8028 - 1.7774 0.97 3331 173 0.2230 0.2521
REMARK 3 25 1.7774 - 1.7534 0.97 3367 162 0.2273 0.2721
REMARK 3 26 1.7534 - 1.7306 0.96 3314 217 0.2466 0.2742
REMARK 3 27 1.7306 - 1.7090 0.96 3365 171 0.2478 0.3093
REMARK 3 28 1.7090 - 1.6884 0.96 3363 160 0.2695 0.3225
REMARK 3 29 1.6884 - 1.6687 0.96 3302 202 0.2737 0.3442
REMARK 3 30 1.6687 - 1.6500 0.96 3342 184 0.2736 0.2941
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 50.30
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26100
REMARK 3 B22 (A**2) : 5.60810
REMARK 3 B33 (A**2) : -5.34710
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 : 0.011 6469
REMARK 3 ANGLE : 1.315 8796
REMARK 3 CHIRALITY : 0.099 967
REMARK 3 PLANARITY : 0.007 1165
REMARK 3 DIHEDRAL : 13.990 2372
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 7:57 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6076 -19.8148 1.5077
REMARK 3 T TENSOR
REMARK 3 T11: 0.1397 T22: 0.2285
REMARK 3 T33: 0.2110 T12: 0.0096
REMARK 3 T13: 0.0438 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0113 L22: 0.0321
REMARK 3 L33: 0.0778 L12: 0.0235
REMARK 3 L13: 0.0230 L23: 0.0646
REMARK 3 S TENSOR
REMARK 3 S11: -0.0344 S12: -0.1819 S13: -0.0158
REMARK 3 S21: -0.0512 S22: -0.0258 S23: 0.0399
REMARK 3 S31: -0.0105 S32: 0.0007 S33: 0.0023
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 58:140 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6179 2.2442 11.7667
REMARK 3 T TENSOR
REMARK 3 T11: 0.2907 T22: 0.1145
REMARK 3 T33: 0.2486 T12: -0.1101
REMARK 3 T13: 0.0223 T23: -0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 0.0960 L22: 0.0339
REMARK 3 L33: 0.3828 L12: 0.0047
REMARK 3 L13: -0.1803 L23: 0.0319
REMARK 3 S TENSOR
REMARK 3 S11: 0.0615 S12: -0.1491 S13: 0.1022
REMARK 3 S21: -0.0471 S22: 0.0293 S23: -0.2009
REMARK 3 S31: -0.4641 S32: 0.4411 S33: 0.0230
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 141:169 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4616 2.1943 -4.1707
REMARK 3 T TENSOR
REMARK 3 T11: 0.4425 T22: 0.2194
REMARK 3 T33: 0.2242 T12: 0.0938
REMARK 3 T13: -0.0303 T23: 0.0463
REMARK 3 L TENSOR
REMARK 3 L11: -0.0006 L22: 0.0143
REMARK 3 L33: 0.0282 L12: 0.0022
REMARK 3 L13: 0.0017 L23: -0.0165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0059 S12: -0.0190 S13: 0.0439
REMARK 3 S21: -0.1420 S22: -0.0454 S23: 0.0787
REMARK 3 S31: -0.0725 S32: -0.0750 S33: -0.0075
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 170:255 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0487 10.2307 -3.5226
REMARK 3 T TENSOR
REMARK 3 T11: 0.6709 T22: -0.0132
REMARK 3 T33: 0.2010 T12: -0.0691
REMARK 3 T13: 0.0737 T23: 0.1307
REMARK 3 L TENSOR
REMARK 3 L11: 0.0134 L22: 0.0424
REMARK 3 L33: 0.0408 L12: 0.0136
REMARK 3 L13: 0.0161 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0690 S12: 0.1290 S13: 0.1064
REMARK 3 S21: -0.1376 S22: 0.0603 S23: -0.0544
REMARK 3 S31: -0.5422 S32: 0.0449 S33: 0.0825
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 256:312 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2947 1.1539 13.4455
REMARK 3 T TENSOR
REMARK 3 T11: 0.2450 T22: 0.1545
REMARK 3 T33: 0.2112 T12: -0.0737
REMARK 3 T13: 0.0162 T23: -0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 0.0174 L22: -0.0020
REMARK 3 L33: 0.0586 L12: 0.0160
REMARK 3 L13: -0.0037 L23: 0.0043
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.0157 S13: 0.0930
REMARK 3 S21: -0.0165 S22: 0.0085 S23: -0.0608
REMARK 3 S31: -0.2933 S32: 0.2011 S33: -0.0103
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 313:343 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6694 -8.4856 -10.7117
REMARK 3 T TENSOR
REMARK 3 T11: 0.2450 T22: 0.2952
REMARK 3 T33: 0.2662 T12: -0.0909
REMARK 3 T13: 0.0996 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.0401 L22: 0.0438
REMARK 3 L33: 0.0095 L12: -0.0177
REMARK 3 L13: -0.0157 L23: -0.0124
REMARK 3 S TENSOR
REMARK 3 S11: 0.0974 S12: -0.0559 S13: 0.0757
REMARK 3 S21: -0.1244 S22: -0.0355 S23: -0.1177
REMARK 3 S31: -0.1044 S32: 0.1784 S33: 0.0181
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 344:406 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3510 -14.1274 -17.6639
REMARK 3 T TENSOR
REMARK 3 T11: 0.1990 T22: 0.1629
REMARK 3 T33: 0.1774 T12: 0.0080
REMARK 3 T13: 0.0166 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0297
REMARK 3 L33: 0.0318 L12: 0.0118
REMARK 3 L13: -0.0062 L23: 0.0113
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.1222 S13: -0.0481
REMARK 3 S21: -0.2046 S22: -0.0104 S23: 0.0667
REMARK 3 S31: -0.1350 S32: 0.0351 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 10:41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3807 9.4157 32.3077
REMARK 3 T TENSOR
REMARK 3 T11: 0.5787 T22: 0.3104
REMARK 3 T33: 0.4078 T12: -0.1139
REMARK 3 T13: -0.0697 T23: -0.0914
REMARK 3 L TENSOR
REMARK 3 L11: -0.0022 L22: 0.0140
REMARK 3 L33: 0.0073 L12: -0.0051
REMARK 3 L13: -0.0032 L23: 0.0103
REMARK 3 S TENSOR
REMARK 3 S11: 0.1701 S12: -0.0943 S13: 0.0324
REMARK 3 S21: -0.0334 S22: -0.0377 S23: -0.1527
REMARK 3 S31: -0.1463 S32: 0.0611 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 42:76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7252 -16.9577 21.6973
REMARK 3 T TENSOR
REMARK 3 T11: 0.1269 T22: 0.2549
REMARK 3 T33: 0.2247 T12: 0.0082
REMARK 3 T13: -0.0312 T23: -0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.0068 L22: 0.0494
REMARK 3 L33: 0.0329 L12: 0.0135
REMARK 3 L13: -0.0166 L23: -0.0429
REMARK 3 S TENSOR
REMARK 3 S11: -0.0413 S12: -0.0849 S13: 0.0127
REMARK 3 S21: 0.0238 S22: -0.0047 S23: -0.1479
REMARK 3 S31: -0.0007 S32: 0.1261 S33: -0.0053
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 77:140 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4044 -16.1285 24.9959
REMARK 3 T TENSOR
REMARK 3 T11: 0.1326 T22: 0.1432
REMARK 3 T33: 0.1616 T12: 0.0029
REMARK 3 T13: 0.0037 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 0.0401 L22: 0.0234
REMARK 3 L33: 0.0638 L12: 0.0269
REMARK 3 L13: -0.0005 L23: -0.0219
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: -0.0338 S13: -0.0493
REMARK 3 S21: 0.0656 S22: -0.0605 S23: 0.0134
REMARK 3 S31: -0.0014 S32: -0.0209 S33: -0.0045
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 141:215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0073 -9.3023 40.3182
REMARK 3 T TENSOR
REMARK 3 T11: 0.2789 T22: 0.2275
REMARK 3 T33: 0.1805 T12: 0.0193
REMARK 3 T13: 0.0542 T23: -0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 0.0478 L22: 0.0388
REMARK 3 L33: 0.1074 L12: -0.0346
REMARK 3 L13: 0.0089 L23: 0.0306
REMARK 3 S TENSOR
REMARK 3 S11: -0.0840 S12: -0.1020 S13: 0.0710
REMARK 3 S21: 0.2482 S22: 0.0167 S23: 0.1049
REMARK 3 S31: -0.0613 S32: -0.0997 S33: -0.0598
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 216:343 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6245 -18.1077 30.2722
REMARK 3 T TENSOR
REMARK 3 T11: 0.1339 T22: 0.2220
REMARK 3 T33: 0.1603 T12: 0.0148
REMARK 3 T13: -0.0031 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.1265 L22: 0.4067
REMARK 3 L33: 0.0955 L12: -0.0537
REMARK 3 L13: -0.1355 L23: 0.0647
REMARK 3 S TENSOR
REMARK 3 S11: -0.0756 S12: -0.1205 S13: 0.0363
REMARK 3 S21: 0.1142 S22: 0.0034 S23: -0.0150
REMARK 3 S31: 0.0093 S32: 0.0216 S33: -0.0469
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 344:405 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2241 -1.7059 50.4231
REMARK 3 T TENSOR
REMARK 3 T11: 0.5383 T22: 0.4780
REMARK 3 T33: 0.1225 T12: -0.0065
REMARK 3 T13: -0.3877 T23: -0.3378
REMARK 3 L TENSOR
REMARK 3 L11: -0.0041 L22: -0.0013
REMARK 3 L33: 0.0015 L12: 0.0081
REMARK 3 L13: 0.0029 L23: 0.0079
REMARK 3 S TENSOR
REMARK 3 S11: -0.0434 S12: -0.1794 S13: 0.0832
REMARK 3 S21: 0.1903 S22: -0.0207 S23: -0.1069
REMARK 3 S31: -0.1171 S32: 0.1588 S33: -0.0188
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 4F5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : DOUBLE CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS
REMARK 200 DATA SCALING SOFTWARE : PROTEUM PLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 108279
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39300
REMARK 200 R SYM FOR SHELL (I) : 0.39300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 (%): 51.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, 0.1 M SODIUM ACETATE, PH
REMARK 280 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 29.14950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.11700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.46900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.11700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.14950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.46900
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: 6970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 ALA A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 VAL B 9
REMARK 465 LEU B 406
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 290 CD NE CZ NH1 NH2
REMARK 470 LYS A 365 CG CD CE NZ
REMARK 470 ARG B 290 NE CZ NH1 NH2
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 OE2 GLU B 83 NH2 ARG B 86 1.93
REMARK 500 O HOH A 669 O HOH A 841 1.99
REMARK 500 O HOH A 750 O HOH B 708 1.99
REMARK 500 O HOH A 1008 O HOH A 1013 2.01
REMARK 500 OE2 GLU B 236 O HOH B 965 2.04
REMARK 500 O HOH B 884 O HOH B 928 2.05
REMARK 500 O HOH A 936 O HOH A 952 2.06
REMARK 500 OD1 ASN B 142 OG SER B 145 2.06
REMARK 500 O HOH A 983 O HOH A 998 2.07
REMARK 500 O HOH A 905 O HOH A 907 2.08
REMARK 500 ND2 ASN B 142 O HOH B 939 2.09
REMARK 500 O HOH A 1011 O HOH A 1012 2.11
REMARK 500 O HOH A 965 O HOH B 849 2.12
REMARK 500 O HOH B 859 O HOH B 862 2.13
REMARK 500 O HOH B 901 O HOH B 904 2.17
REMARK 500 O HOH A 755 O HOH A 813 2.17
REMARK 500 O HOH A 840 O HOH A 893 2.17
REMARK 500 O HOH A 981 O HOH A 982 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 TYR A 159 -69.09 -150.22
REMARK 500 TYR A 261 -63.33 -29.66
REMARK 500 ARG A 264 71.15 61.42
REMARK 500 ASN A 292 -76.79 -110.07
REMARK 500 SER A 294 -57.37 80.35
REMARK 500 ALA B 32 43.27 -94.62
REMARK 500 SER B 139 -166.37 -179.47
REMARK 500 TYR B 159 -61.42 -150.07
REMARK 500 ALA B 228 -71.59 -87.56
REMARK 500 ARG B 264 73.31 62.35
REMARK 500 ASN B 292 -80.16 -108.75
REMARK 500 SER B 294 -59.29 77.94
REMARK 500 ALA B 344 -76.06 -37.41
REMARK 500 ASN B 345 -90.17 146.85
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 LLP A 256 13.0 L L OUTSIDE RANGE
REMARK 500 LLP B 256 17.7 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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 935 DISTANCE = 7.95 ANGSTROMS
REMARK 525 HOH B 943 DISTANCE = 5.68 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F5F RELATED DB: PDB
REMARK 900 RELATED ID: 4F5G RELATED DB: PDB
REMARK 900 RELATED ID: 4F5H RELATED DB: PDB
REMARK 900 RELATED ID: 4F5I RELATED DB: PDB
REMARK 900 RELATED ID: 4F5J RELATED DB: PDB
REMARK 900 RELATED ID: 4F5K RELATED DB: PDB
REMARK 900 RELATED ID: 4F5L RELATED DB: PDB
DBREF 4F5M A 12 406 UNP P00509 AAT_ECOLI 2 396
DBREF 4F5M B 12 406 UNP P00509 AAT_ECOLI 2 396
SEQADV 4F5M MET A 1 UNP P00509 EXPRESSION TAG
SEQADV 4F5M ALA A 2 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS A 3 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS A 4 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS A 5 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS A 6 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS A 7 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS A 8 UNP P00509 EXPRESSION TAG
SEQADV 4F5M VAL A 9 UNP P00509 EXPRESSION TAG
SEQADV 4F5M GLY A 10 UNP P00509 EXPRESSION TAG
SEQADV 4F5M THR A 11 UNP P00509 EXPRESSION TAG
SEQADV 4F5M MET B 1 UNP P00509 EXPRESSION TAG
SEQADV 4F5M ALA B 2 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS B 3 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS B 4 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS B 5 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS B 6 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS B 7 UNP P00509 EXPRESSION TAG
SEQADV 4F5M HIS B 8 UNP P00509 EXPRESSION TAG
SEQADV 4F5M VAL B 9 UNP P00509 EXPRESSION TAG
SEQADV 4F5M GLY B 10 UNP P00509 EXPRESSION TAG
SEQADV 4F5M THR B 11 UNP P00509 EXPRESSION TAG
SEQRES 1 A 406 MET ALA HIS HIS HIS HIS HIS HIS VAL GLY THR PHE GLU
SEQRES 2 A 406 ASN ILE THR ALA ALA PRO ALA ASP PRO ILE LEU GLY LEU
SEQRES 3 A 406 ALA ASP LEU PHE ARG ALA ASP GLU ARG PRO GLY LYS ILE
SEQRES 4 A 406 ASN LEU GLY ILE GLY VAL TYR LYS ASP GLU THR GLY LYS
SEQRES 5 A 406 THR PRO VAL LEU THR SER VAL LYS LYS ALA GLU GLN TYR
SEQRES 6 A 406 LEU LEU GLU ASN GLU THR THR LYS ASN TYR LEU GLY ILE
SEQRES 7 A 406 ASP GLY ILE PRO GLU PHE GLY ARG CYS THR GLN GLU LEU
SEQRES 8 A 406 LEU PHE GLY LYS GLY SER ALA LEU ILE ASN ASP LYS ARG
SEQRES 9 A 406 ALA ARG THR ALA GLN THR PRO GLY GLY THR GLY ALA LEU
SEQRES 10 A 406 ARG VAL ALA ALA ASP PHE LEU ALA LYS ASN THR SER VAL
SEQRES 11 A 406 LYS ARG VAL TRP VAL SER ASN PRO SER TRP PRO ASN HIS
SEQRES 12 A 406 LYS SER VAL PHE ASN SER ALA GLY LEU GLU VAL ARG GLU
SEQRES 13 A 406 TYR ALA TYR TYR ASP ALA GLU ASN HIS THR LEU ASP PHE
SEQRES 14 A 406 ASP ALA LEU ILE ASN SER LEU ASN GLU ALA GLN ALA GLY
SEQRES 15 A 406 ASP VAL VAL LEU PHE HIS GLY CYS CYS HIS ASN PRO THR
SEQRES 16 A 406 GLY ILE ASP PRO THR LEU GLU GLN TRP GLN THR LEU ALA
SEQRES 17 A 406 GLN LEU SER VAL GLU LYS GLY TRP LEU PRO LEU PHE ASP
SEQRES 18 A 406 PHE ALA TYR GLN GLY PHE ALA ARG GLY LEU GLU GLU ASP
SEQRES 19 A 406 ALA GLU GLY LEU ARG ALA PHE ALA ALA MET HIS LYS GLU
SEQRES 20 A 406 LEU ILE VAL ALA SER SER TYR SER LLP ASN PHE GLY LEU
SEQRES 21 A 406 TYR ASN GLU ARG VAL GLY ALA CYS THR LEU VAL ALA ALA
SEQRES 22 A 406 ASP SER GLU THR VAL ASP ARG ALA PHE SER GLN MET LYS
SEQRES 23 A 406 ALA ALA ILE ARG ALA ASN TYR SER ASN PRO PRO ALA HIS
SEQRES 24 A 406 GLY ALA SER VAL VAL ALA THR ILE LEU SER ASN ASP ALA
SEQRES 25 A 406 LEU ARG ALA ILE TRP GLU GLN GLU LEU THR ASP MET ARG
SEQRES 26 A 406 GLN ARG ILE GLN ARG MET ARG GLN LEU PHE VAL ASN THR
SEQRES 27 A 406 LEU GLN GLU LYS GLY ALA ASN ARG ASP PHE SER PHE ILE
SEQRES 28 A 406 ILE LYS GLN ASN GLY MET PHE SER PHE SER GLY LEU THR
SEQRES 29 A 406 LYS GLU GLN VAL LEU ARG LEU ARG GLU GLU PHE GLY VAL
SEQRES 30 A 406 TYR ALA VAL ALA SER GLY ARG VAL ASN VAL ALA GLY MET
SEQRES 31 A 406 THR PRO ASP ASN MET ALA PRO LEU CYS GLU ALA ILE VAL
SEQRES 32 A 406 ALA VAL LEU
SEQRES 1 B 406 MET ALA HIS HIS HIS HIS HIS HIS VAL GLY THR PHE GLU
SEQRES 2 B 406 ASN ILE THR ALA ALA PRO ALA ASP PRO ILE LEU GLY LEU
SEQRES 3 B 406 ALA ASP LEU PHE ARG ALA ASP GLU ARG PRO GLY LYS ILE
SEQRES 4 B 406 ASN LEU GLY ILE GLY VAL TYR LYS ASP GLU THR GLY LYS
SEQRES 5 B 406 THR PRO VAL LEU THR SER VAL LYS LYS ALA GLU GLN TYR
SEQRES 6 B 406 LEU LEU GLU ASN GLU THR THR LYS ASN TYR LEU GLY ILE
SEQRES 7 B 406 ASP GLY ILE PRO GLU PHE GLY ARG CYS THR GLN GLU LEU
SEQRES 8 B 406 LEU PHE GLY LYS GLY SER ALA LEU ILE ASN ASP LYS ARG
SEQRES 9 B 406 ALA ARG THR ALA GLN THR PRO GLY GLY THR GLY ALA LEU
SEQRES 10 B 406 ARG VAL ALA ALA ASP PHE LEU ALA LYS ASN THR SER VAL
SEQRES 11 B 406 LYS ARG VAL TRP VAL SER ASN PRO SER TRP PRO ASN HIS
SEQRES 12 B 406 LYS SER VAL PHE ASN SER ALA GLY LEU GLU VAL ARG GLU
SEQRES 13 B 406 TYR ALA TYR TYR ASP ALA GLU ASN HIS THR LEU ASP PHE
SEQRES 14 B 406 ASP ALA LEU ILE ASN SER LEU ASN GLU ALA GLN ALA GLY
SEQRES 15 B 406 ASP VAL VAL LEU PHE HIS GLY CYS CYS HIS ASN PRO THR
SEQRES 16 B 406 GLY ILE ASP PRO THR LEU GLU GLN TRP GLN THR LEU ALA
SEQRES 17 B 406 GLN LEU SER VAL GLU LYS GLY TRP LEU PRO LEU PHE ASP
SEQRES 18 B 406 PHE ALA TYR GLN GLY PHE ALA ARG GLY LEU GLU GLU ASP
SEQRES 19 B 406 ALA GLU GLY LEU ARG ALA PHE ALA ALA MET HIS LYS GLU
SEQRES 20 B 406 LEU ILE VAL ALA SER SER TYR SER LLP ASN PHE GLY LEU
SEQRES 21 B 406 TYR ASN GLU ARG VAL GLY ALA CYS THR LEU VAL ALA ALA
SEQRES 22 B 406 ASP SER GLU THR VAL ASP ARG ALA PHE SER GLN MET LYS
SEQRES 23 B 406 ALA ALA ILE ARG ALA ASN TYR SER ASN PRO PRO ALA HIS
SEQRES 24 B 406 GLY ALA SER VAL VAL ALA THR ILE LEU SER ASN ASP ALA
SEQRES 25 B 406 LEU ARG ALA ILE TRP GLU GLN GLU LEU THR ASP MET ARG
SEQRES 26 B 406 GLN ARG ILE GLN ARG MET ARG GLN LEU PHE VAL ASN THR
SEQRES 27 B 406 LEU GLN GLU LYS GLY ALA ASN ARG ASP PHE SER PHE ILE
SEQRES 28 B 406 ILE LYS GLN ASN GLY MET PHE SER PHE SER GLY LEU THR
SEQRES 29 B 406 LYS GLU GLN VAL LEU ARG LEU ARG GLU GLU PHE GLY VAL
SEQRES 30 B 406 TYR ALA VAL ALA SER GLY ARG VAL ASN VAL ALA GLY MET
SEQRES 31 B 406 THR PRO ASP ASN MET ALA PRO LEU CYS GLU ALA ILE VAL
SEQRES 32 B 406 ALA VAL LEU
MODRES 4F5M LLP A 256 LYS
MODRES 4F5M LLP B 256 LYS
HET LLP A 256 24
HET LLP B 256 24
HET EDO A 501 4
HET EDO B 501 4
HET EDO B 502 4
HET EDO B 503 4
HETNAM LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-
HETNAM 2 LLP PYRIDIN-4-YLMETHANE)
HETNAM EDO 1,2-ETHANEDIOL
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 LLP 2(C14 H24 N3 O7 P)
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 7 HOH *787(H2 O)
HELIX 1 1 ASP A 21 ASP A 33 1 13
HELIX 2 2 LEU A 56 GLU A 70 1 15
HELIX 3 3 ILE A 81 GLY A 94 1 14
HELIX 4 4 SER A 97 ASP A 102 1 6
HELIX 5 5 GLY A 112 THR A 128 1 17
HELIX 6 6 TRP A 140 ALA A 150 1 11
HELIX 7 7 ASP A 168 ASN A 177 1 10
HELIX 8 8 THR A 200 GLY A 215 1 16
HELIX 9 9 GLY A 230 ALA A 235 1 6
HELIX 10 10 ALA A 235 ALA A 243 1 9
HELIX 11 11 LEU A 260 GLU A 263 5 4
HELIX 12 12 ASP A 274 ALA A 291 1 18
HELIX 13 13 PRO A 297 SER A 309 1 13
HELIX 14 14 ASN A 310 LYS A 342 1 33
HELIX 15 15 PHE A 348 GLN A 354 5 7
HELIX 16 16 THR A 364 GLY A 376 1 13
HELIX 17 17 ALA A 388 MET A 390 5 3
HELIX 18 18 ASN A 394 LEU A 406 1 13
HELIX 19 19 ASP B 21 ALA B 32 1 12
HELIX 20 20 LEU B 56 GLU B 70 1 15
HELIX 21 21 ILE B 81 GLY B 94 1 14
HELIX 22 22 SER B 97 ASP B 102 1 6
HELIX 23 23 PRO B 111 THR B 128 1 18
HELIX 24 24 PRO B 141 ALA B 150 1 10
HELIX 25 25 ASP B 168 LEU B 176 1 9
HELIX 26 26 ASN B 177 ALA B 179 5 3
HELIX 27 27 THR B 200 GLY B 215 1 16
HELIX 28 28 GLY B 230 ALA B 235 1 6
HELIX 29 29 ALA B 235 HIS B 245 1 11
HELIX 30 30 LEU B 260 ARG B 264 5 5
HELIX 31 31 ASP B 274 ALA B 291 1 18
HELIX 32 32 PRO B 297 SER B 309 1 13
HELIX 33 33 ASN B 310 LYS B 342 1 33
HELIX 34 34 SER B 349 GLN B 354 1 6
HELIX 35 35 THR B 364 GLY B 376 1 13
HELIX 36 36 ALA B 388 MET B 390 5 3
HELIX 37 37 ASN B 394 ALA B 404 1 11
SHEET 1 A 2 ILE A 39 ASN A 40 0
SHEET 2 A 2 VAL A 377 TYR A 378 1 O TYR A 378 N ILE A 39
SHEET 1 B 7 ALA A 105 PRO A 111 0
SHEET 2 B 7 VAL A 265 VAL A 271 -1 O LEU A 270 N ARG A 106
SHEET 3 B 7 LEU A 248 SER A 253 -1 N VAL A 250 O THR A 269
SHEET 4 B 7 LEU A 217 PHE A 222 1 N PHE A 220 O ALA A 251
SHEET 5 B 7 VAL A 184 HIS A 188 1 N PHE A 187 O ASP A 221
SHEET 6 B 7 ARG A 132 SER A 136 1 N TRP A 134 O LEU A 186
SHEET 7 B 7 GLU A 153 TYR A 157 1 O ARG A 155 N VAL A 135
SHEET 1 C 2 TYR A 160 ASP A 161 0
SHEET 2 C 2 THR A 166 LEU A 167 -1 O THR A 166 N ASP A 161
SHEET 1 D 2 PHE A 358 PHE A 360 0
SHEET 2 D 2 ARG A 384 ASN A 386 -1 O VAL A 385 N SER A 359
SHEET 1 E 2 ILE B 39 ASN B 40 0
SHEET 2 E 2 VAL B 377 TYR B 378 1 O TYR B 378 N ILE B 39
SHEET 1 F 7 ALA B 105 THR B 110 0
SHEET 2 F 7 GLY B 266 VAL B 271 -1 O LEU B 270 N ARG B 106
SHEET 3 F 7 LEU B 248 SER B 253 -1 N VAL B 250 O THR B 269
SHEET 4 F 7 LEU B 217 PHE B 222 1 N PHE B 220 O ALA B 251
SHEET 5 F 7 VAL B 184 HIS B 188 1 N PHE B 187 O ASP B 221
SHEET 6 F 7 ARG B 132 ASN B 137 1 N TRP B 134 O LEU B 186
SHEET 7 F 7 GLU B 153 ALA B 158 1 O TYR B 157 N VAL B 135
SHEET 1 G 2 TYR B 160 ASP B 161 0
SHEET 2 G 2 THR B 166 LEU B 167 -1 O THR B 166 N ASP B 161
SHEET 1 H 2 PHE B 358 PHE B 360 0
SHEET 2 H 2 ARG B 384 ASN B 386 -1 O VAL B 385 N SER B 359
LINK C SER A 255 N LLP A 256 1555 1555 1.32
LINK C LLP A 256 N ASN A 257 1555 1555 1.32
LINK C SER B 255 N LLP B 256 1555 1555 1.31
LINK C LLP B 256 N ASN B 257 1555 1555 1.33
CISPEP 1 ASN A 137 PRO A 138 0 6.15
CISPEP 2 ASN A 193 PRO A 194 0 13.39
CISPEP 3 ASN B 137 PRO B 138 0 -4.29
CISPEP 4 ASN B 193 PRO B 194 0 18.11
SITE 1 AC1 5 GLY A 44 TRP A 140 ASN A 193 LLP A 256
SITE 2 AC1 5 HOH A 965
SITE 1 AC2 10 PRO B 82 GLY B 85 ARG B 86 GLN B 89
SITE 2 AC2 10 ARG B 106 THR B 107 EDO B 502 HOH B 622
SITE 3 AC2 10 HOH B 672 HOH B 700
SITE 1 AC3 7 GLN B 89 ILE B 100 LYS B 103 ARG B 104
SITE 2 AC3 7 ALA B 105 EDO B 501 HOH B 831
SITE 1 AC4 6 THR A 114 LLP A 256 TYR B 75 SER B 294
SITE 2 AC4 6 ASN B 295 HOH B 937
CRYST1 58.299 108.938 144.234 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 0.017153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009180 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006933 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
