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HEADER HYDROLASE 15-NOV-22 8HGW
TITLE CRYSTAL STRUCTURE OF MEHPH IN COMPLEX WITH MBP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOALKYL PHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GORDONIA;
SOURCE 3 ORGANISM_TAXID: 2053;
SOURCE 4 GENE: MEHPH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.M.ZHANG,Y.J.WANG,Y.B.CHEN
REVDAT 1 15-MAR-23 8HGW 0
JRNL AUTH Y.CHEN,Y.WANG,Y.XU,J.SUN,L.YANG,C.FENG,J.WANG,Y.ZHOU,
JRNL AUTH 2 Z.M.ZHANG,Y.WANG
JRNL TITL MOLECULAR INSIGHTS INTO THE CATALYTIC MECHANISM OF
JRNL TITL 2 PLASTICIZER DEGRADATION BY A MONOALKYL PHTHALATE HYDROLASE.
JRNL REF COMMUN CHEM V. 6 45 2023
JRNL REFN ESSN 2399-3669
JRNL PMID 36859434
JRNL DOI 10.1038/S42004-023-00846-0
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692+SVN
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.348
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 28590
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.054
REMARK 3 FREE R VALUE TEST SET COUNT : 1445
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 10.0000 - 6.0278 0.99 2801 170 0.1804 0.2204
REMARK 3 2 6.0278 - 4.7863 1.00 2724 153 0.2075 0.2161
REMARK 3 3 4.7863 - 4.1818 1.00 2750 137 0.1810 0.2149
REMARK 3 4 4.1818 - 3.7997 1.00 2696 144 0.2135 0.2286
REMARK 3 5 3.7997 - 3.5275 1.00 2692 148 0.2218 0.2556
REMARK 3 6 3.5275 - 3.3196 1.00 2718 143 0.2549 0.2971
REMARK 3 7 3.3196 - 3.1534 1.00 2706 128 0.2717 0.3234
REMARK 3 8 3.1534 - 3.0162 1.00 2685 138 0.2915 0.3245
REMARK 3 9 3.0162 - 2.9001 1.00 2671 145 0.3130 0.3553
REMARK 3 10 2.9001 - 2.8010 1.00 2702 139 0.3458 0.4112
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.422
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.845
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.46
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 : 0.005 8891
REMARK 3 ANGLE : 0.998 12133
REMARK 3 CHIRALITY : 0.040 1358
REMARK 3 PLANARITY : 0.008 1587
REMARK 3 DIHEDRAL : 15.733 3058
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7858 1.9486 -45.6246
REMARK 3 T TENSOR
REMARK 3 T11: 0.2956 T22: 0.6457
REMARK 3 T33: 0.3117 T12: -0.1146
REMARK 3 T13: -0.0625 T23: 0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 2.4035 L22: 1.3351
REMARK 3 L33: 2.7093 L12: -0.0880
REMARK 3 L13: -0.4971 L23: 0.5394
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: -0.5587 S13: 0.0411
REMARK 3 S21: 0.2910 S22: -0.0934 S23: -0.0974
REMARK 3 S31: 0.2172 S32: 0.4164 S33: 0.0678
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1938 2.3584 -67.7862
REMARK 3 T TENSOR
REMARK 3 T11: 0.3001 T22: 0.5365
REMARK 3 T33: 0.3974 T12: -0.0950
REMARK 3 T13: -0.0601 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 6.1417 L22: 2.6235
REMARK 3 L33: 4.5952 L12: -0.0873
REMARK 3 L13: -0.1518 L23: -0.1724
REMARK 3 S TENSOR
REMARK 3 S11: -0.0652 S12: 0.6481 S13: 0.8189
REMARK 3 S21: 0.1439 S22: 0.0751 S23: -0.7710
REMARK 3 S31: -0.0500 S32: 0.5200 S33: -0.0726
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 197 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5765 -0.2310 -54.0149
REMARK 3 T TENSOR
REMARK 3 T11: 0.2454 T22: 0.3157
REMARK 3 T33: 0.3105 T12: -0.1202
REMARK 3 T13: 0.0018 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 3.0581 L22: 0.4391
REMARK 3 L33: 2.0681 L12: -1.0722
REMARK 3 L13: 0.1633 L23: -0.0767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: 0.1640 S13: -0.0901
REMARK 3 S21: 0.0473 S22: -0.1164 S23: -0.0483
REMARK 3 S31: -0.0482 S32: 0.2222 S33: 0.0874
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9681 14.7742 -20.2042
REMARK 3 T TENSOR
REMARK 3 T11: 0.4719 T22: 1.2464
REMARK 3 T33: 0.3173 T12: -0.3227
REMARK 3 T13: -0.0750 T23: 0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 1.4802 L22: 1.3021
REMARK 3 L33: 1.7401 L12: 0.1077
REMARK 3 L13: 0.1363 L23: 0.5954
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: -0.0514 S13: 0.0162
REMARK 3 S21: -0.0723 S22: 0.0449 S23: -0.0239
REMARK 3 S31: 0.6108 S32: -0.4576 S33: -0.1166
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4057 30.9758 -9.1866
REMARK 3 T TENSOR
REMARK 3 T11: 0.2752 T22: 1.8134
REMARK 3 T33: 0.7073 T12: 0.0040
REMARK 3 T13: 0.2095 T23: 0.3313
REMARK 3 L TENSOR
REMARK 3 L11: 1.1332 L22: 0.6790
REMARK 3 L33: 0.1536 L12: 0.8658
REMARK 3 L13: -0.1638 L23: -0.0840
REMARK 3 S TENSOR
REMARK 3 S11: 0.3419 S12: 0.5912 S13: 0.9840
REMARK 3 S21: -0.1684 S22: 0.3690 S23: 0.4898
REMARK 3 S31: -0.2596 S32: -0.2850 S33: -0.1871
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 208 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5789 19.2187 -12.7030
REMARK 3 T TENSOR
REMARK 3 T11: 0.3043 T22: 1.2661
REMARK 3 T33: 0.3541 T12: -0.2074
REMARK 3 T13: 0.0064 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.4642 L22: 0.9476
REMARK 3 L33: 0.9043 L12: 0.6479
REMARK 3 L13: -0.7799 L23: 0.1291
REMARK 3 S TENSOR
REMARK 3 S11: -0.1459 S12: -0.3350 S13: -0.0149
REMARK 3 S21: -0.0374 S22: 0.2846 S23: -0.0779
REMARK 3 S31: 0.2761 S32: -0.4067 S33: -0.0615
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 24 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7494 -6.9615 -25.7494
REMARK 3 T TENSOR
REMARK 3 T11: 0.4073 T22: 0.7807
REMARK 3 T33: 0.3283 T12: -0.1951
REMARK 3 T13: 0.0221 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 3.3649 L22: 2.4917
REMARK 3 L33: 3.2148 L12: 0.1607
REMARK 3 L13: -1.5551 L23: -0.9452
REMARK 3 S TENSOR
REMARK 3 S11: 0.3527 S12: -0.0378 S13: 0.1109
REMARK 3 S21: 0.2019 S22: -0.2690 S23: -0.1360
REMARK 3 S31: -0.6408 S32: 0.0686 S33: -0.0557
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 162 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8050 -26.2072 -20.0410
REMARK 3 T TENSOR
REMARK 3 T11: 0.3414 T22: 1.3684
REMARK 3 T33: 0.8053 T12: -0.0497
REMARK 3 T13: 0.0229 T23: 0.2736
REMARK 3 L TENSOR
REMARK 3 L11: 0.3325 L22: 4.7798
REMARK 3 L33: 2.4407 L12: 0.5457
REMARK 3 L13: 0.8032 L23: -0.0088
REMARK 3 S TENSOR
REMARK 3 S11: -0.3599 S12: -0.3805 S13: -0.7154
REMARK 3 S21: -0.3769 S22: -0.0727 S23: 0.1725
REMARK 3 S31: 0.3137 S32: 0.4277 S33: 0.3074
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 197 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2527 -14.6945 -18.0201
REMARK 3 T TENSOR
REMARK 3 T11: 0.3420 T22: 0.9875
REMARK 3 T33: 0.3618 T12: -0.1978
REMARK 3 T13: 0.0191 T23: -0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 2.8224 L22: 1.5971
REMARK 3 L33: 1.0806 L12: 0.3742
REMARK 3 L13: -0.0038 L23: -1.2401
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: -0.2539 S13: -0.2150
REMARK 3 S21: 0.1956 S22: -0.2301 S23: -0.1323
REMARK 3 S31: -0.1200 S32: 0.5098 S33: 0.1095
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 24 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.1765 26.0297 -59.6487
REMARK 3 T TENSOR
REMARK 3 T11: 0.4857 T22: 0.3757
REMARK 3 T33: 0.5240 T12: 0.0761
REMARK 3 T13: 0.0468 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 1.2246 L22: 2.1702
REMARK 3 L33: 2.9021 L12: -0.0422
REMARK 3 L13: -0.2924 L23: -0.5071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0313 S12: -0.0450 S13: 0.4589
REMARK 3 S21: 0.2218 S22: 0.1836 S23: 0.0742
REMARK 3 S31: -0.8633 S32: -0.2769 S33: -0.2352
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 119 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.7276 11.6689 -59.1109
REMARK 3 T TENSOR
REMARK 3 T11: 0.2215 T22: 0.4266
REMARK 3 T33: 0.3362 T12: 0.0678
REMARK 3 T13: -0.0395 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 4.5195 L22: 2.5522
REMARK 3 L33: 3.4466 L12: 0.6808
REMARK 3 L13: -1.1500 L23: -0.9231
REMARK 3 S TENSOR
REMARK 3 S11: -0.1143 S12: 0.2272 S13: -0.1373
REMARK 3 S21: 0.1248 S22: 0.1226 S23: 0.1752
REMARK 3 S31: -0.2064 S32: -0.5516 S33: -0.0093
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 197 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5366 12.4627 -61.2733
REMARK 3 T TENSOR
REMARK 3 T11: 0.2721 T22: 0.3499
REMARK 3 T33: 0.2874 T12: -0.0217
REMARK 3 T13: 0.0027 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 2.8647 L22: 1.8476
REMARK 3 L33: 2.3071 L12: -0.2595
REMARK 3 L13: 1.0589 L23: -0.6933
REMARK 3 S TENSOR
REMARK 3 S11: 0.0416 S12: 0.1429 S13: 0.0966
REMARK 3 S21: 0.1603 S22: -0.0147 S23: 0.1855
REMARK 3 S31: -0.1794 S32: -0.3468 S33: 0.0132
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 : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'C'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'A'
REMARK 3 SELECTION : CHAIN 'D'
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8HGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1300033596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-22
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 : CAMD
REMARK 200 BEAMLINE : GCPCC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97914
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32749
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: ALPHAFOLD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS, PH 6.2, 22% (W/V) PEG
REMARK 280 3350 AND 250 MM MGCL2.6H2O, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
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+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
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 28.51184
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.47500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 152.83811
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.51184
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.47500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 152.83811
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 76.95000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 48.95000
REMARK 350 BIOMT3 2 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 23
REMARK 465 MET B 23
REMARK 465 GLY B 175
REMARK 465 GLY B 176
REMARK 465 MET C 23
REMARK 465 GLY C 175
REMARK 465 GLY C 176
REMARK 465 MET D 23
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 GLU A 70 CG CD OE1 OE2
REMARK 470 GLU A 74 CG CD OE1 OE2
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 ARG A 171 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 GLU A 192 CG CD OE1 OE2
REMARK 470 ASP A 194 CG OD1 OD2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 GLU A 210 CG CD OE1 OE2
REMARK 470 GLN B 86 CG CD OE1 NE2
REMARK 470 GLU B 96 CG CD OE1 OE2
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 GLU B 167 CG CD OE1 OE2
REMARK 470 ARG B 171 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 ARG B 182 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 192 CG CD OE1 OE2
REMARK 470 ASP B 194 CG OD1 OD2
REMARK 470 GLU B 197 CG CD OE1 OE2
REMARK 470 ASP B 198 CG OD1 OD2
REMARK 470 LYS B 205 CG CD CE NZ
REMARK 470 LEU B 207 CG CD1 CD2
REMARK 470 SER B 209 OG
REMARK 470 GLU B 210 CG CD OE1 OE2
REMARK 470 GLN B 212 CG CD OE1 NE2
REMARK 470 ARG B 221 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 225 CG CD OE1 OE2
REMARK 470 GLU B 299 CG CD OE1 OE2
REMARK 470 GLU C 105 CG CD OE1 OE2
REMARK 470 GLU C 167 CG CD OE1 OE2
REMARK 470 ARG C 171 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 179 CG CD OE1 OE2
REMARK 470 ASP C 194 CG OD1 OD2
REMARK 470 GLU C 197 CG CD OE1 OE2
REMARK 470 LYS C 205 CG CD CE NZ
REMARK 470 GLU C 210 CG CD OE1 OE2
REMARK 470 LYS C 211 CG CD CE NZ
REMARK 470 LEU C 213 CG CD1 CD2
REMARK 470 GLU C 233 CG CD OE1 OE2
REMARK 470 GLU C 240 CG CD OE1 OE2
REMARK 470 ARG C 241 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 244 CG OD1 OD2
REMARK 470 GLU D 88 CG CD OE1 OE2
REMARK 470 GLU D 96 CG CD OE1 OE2
REMARK 470 LYS D 143 CG CD CE NZ
REMARK 470 GLU D 167 CG CD OE1 OE2
REMARK 470 ARG D 171 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 179 CG CD OE1 OE2
REMARK 470 GLU D 192 CG CD OE1 OE2
REMARK 470 ASP D 194 CG OD1 OD2
REMARK 470 GLU D 197 CG CD OE1 OE2
REMARK 470 LYS D 205 CG CD CE NZ
REMARK 470 GLU D 210 CG CD OE1 OE2
REMARK 470 GLU D 225 CG CD OE1 OE2
REMARK 470 GLU D 233 CG CD OE1 OE2
REMARK 470 GLU D 299 CG CD OE1 OE2
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 GLN D 86 OG1 THR D 89 2.05
REMARK 500 OE1 GLU C 192 OG SER C 295 2.17
REMARK 500 OE1 GLU B 105 OH TYR B 138 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 125 -121.95 52.76
REMARK 500 ASP A 244 -80.65 -97.21
REMARK 500 SER B 125 -120.50 52.20
REMARK 500 HIS B 226 -52.50 -120.39
REMARK 500 ASP B 244 -80.13 -98.63
REMARK 500 SER C 125 -122.97 53.36
REMARK 500 ASP C 244 -80.59 -98.55
REMARK 500 SER D 125 -122.23 52.63
REMARK 500 ASN D 191 75.04 -115.35
REMARK 500 ASP D 244 -80.53 -98.96
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8HGW A 24 311 UNP Q2MHH5 Q2MHH5_9ACTN 24 311
DBREF 8HGW B 24 311 UNP Q2MHH5 Q2MHH5_9ACTN 24 311
DBREF 8HGW C 24 311 UNP Q2MHH5 Q2MHH5_9ACTN 24 311
DBREF 8HGW D 24 311 UNP Q2MHH5 Q2MHH5_9ACTN 24 311
SEQADV 8HGW MET A 23 UNP Q2MHH5 INITIATING METHIONINE
SEQADV 8HGW ASN A 259 UNP Q2MHH5 ASP 259 CONFLICT
SEQADV 8HGW MET B 23 UNP Q2MHH5 INITIATING METHIONINE
SEQADV 8HGW ASN B 259 UNP Q2MHH5 ASP 259 CONFLICT
SEQADV 8HGW MET C 23 UNP Q2MHH5 INITIATING METHIONINE
SEQADV 8HGW ASN C 259 UNP Q2MHH5 ASP 259 CONFLICT
SEQADV 8HGW MET D 23 UNP Q2MHH5 INITIATING METHIONINE
SEQADV 8HGW ASN D 259 UNP Q2MHH5 ASP 259 CONFLICT
SEQRES 1 A 289 MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG
SEQRES 2 A 289 TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU
SEQRES 3 A 289 ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY
SEQRES 4 A 289 ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU
SEQRES 5 A 289 TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY
SEQRES 6 A 289 GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL
SEQRES 7 A 289 ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN
SEQRES 8 A 289 LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG
SEQRES 9 A 289 GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO
SEQRES 10 A 289 GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR
SEQRES 11 A 289 ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE
SEQRES 12 A 289 TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA
SEQRES 13 A 289 GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN
SEQRES 14 A 289 GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR
SEQRES 15 A 289 LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA
SEQRES 16 A 289 GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER
SEQRES 17 A 289 LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA
SEQRES 18 A 289 ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY
SEQRES 19 A 289 VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY
SEQRES 20 A 289 LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER
SEQRES 21 A 289 LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER
SEQRES 22 A 289 ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE
SEQRES 23 A 289 ILE SER LEU
SEQRES 1 B 289 MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG
SEQRES 2 B 289 TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU
SEQRES 3 B 289 ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY
SEQRES 4 B 289 ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU
SEQRES 5 B 289 TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY
SEQRES 6 B 289 GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL
SEQRES 7 B 289 ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN
SEQRES 8 B 289 LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG
SEQRES 9 B 289 GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO
SEQRES 10 B 289 GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR
SEQRES 11 B 289 ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE
SEQRES 12 B 289 TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA
SEQRES 13 B 289 GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN
SEQRES 14 B 289 GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR
SEQRES 15 B 289 LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA
SEQRES 16 B 289 GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER
SEQRES 17 B 289 LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA
SEQRES 18 B 289 ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY
SEQRES 19 B 289 VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY
SEQRES 20 B 289 LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER
SEQRES 21 B 289 LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER
SEQRES 22 B 289 ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE
SEQRES 23 B 289 ILE SER LEU
SEQRES 1 C 289 MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG
SEQRES 2 C 289 TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU
SEQRES 3 C 289 ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY
SEQRES 4 C 289 ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU
SEQRES 5 C 289 TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY
SEQRES 6 C 289 GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL
SEQRES 7 C 289 ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN
SEQRES 8 C 289 LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG
SEQRES 9 C 289 GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO
SEQRES 10 C 289 GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR
SEQRES 11 C 289 ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE
SEQRES 12 C 289 TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA
SEQRES 13 C 289 GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN
SEQRES 14 C 289 GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR
SEQRES 15 C 289 LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA
SEQRES 16 C 289 GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER
SEQRES 17 C 289 LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA
SEQRES 18 C 289 ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY
SEQRES 19 C 289 VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY
SEQRES 20 C 289 LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER
SEQRES 21 C 289 LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER
SEQRES 22 C 289 ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE
SEQRES 23 C 289 ILE SER LEU
SEQRES 1 D 289 MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG
SEQRES 2 D 289 TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU
SEQRES 3 D 289 ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY
SEQRES 4 D 289 ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU
SEQRES 5 D 289 TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY
SEQRES 6 D 289 GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL
SEQRES 7 D 289 ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN
SEQRES 8 D 289 LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG
SEQRES 9 D 289 GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO
SEQRES 10 D 289 GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR
SEQRES 11 D 289 ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE
SEQRES 12 D 289 TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA
SEQRES 13 D 289 GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN
SEQRES 14 D 289 GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR
SEQRES 15 D 289 LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA
SEQRES 16 D 289 GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER
SEQRES 17 D 289 LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA
SEQRES 18 D 289 ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY
SEQRES 19 D 289 VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY
SEQRES 20 D 289 LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER
SEQRES 21 D 289 LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER
SEQRES 22 D 289 ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE
SEQRES 23 D 289 ILE SER LEU
HET 1BO A 401 5
HET PHT A1000 12
HET PHT B1000 12
HET PHT C1000 12
HET PHT D1000 12
HETNAM 1BO 1-BUTANOL
HETNAM PHT PHTHALIC ACID
HETSYN 1BO BUTAN-1-OL
FORMUL 5 1BO C4 H10 O
FORMUL 6 PHT 4(C8 H6 O4)
HELIX 1 AA1 GLY A 61 GLY A 66 5 6
HELIX 2 AA2 ASN A 67 PHE A 72 1 6
HELIX 3 AA3 ASN A 94 TRP A 98 5 5
HELIX 4 AA4 THR A 99 LEU A 114 1 16
HELIX 5 AA5 SER A 125 TYR A 138 1 14
HELIX 6 AA6 MET A 163 THR A 172 1 10
HELIX 7 AA7 GLY A 176 ALA A 189 1 14
HELIX 8 AA8 PRO A 196 SER A 209 1 14
HELIX 9 AA9 SER A 209 ALA A 223 1 15
HELIX 10 AB1 HIS A 226 ALA A 245 1 20
HELIX 11 AB2 PRO A 263 ALA A 276 1 14
HELIX 12 AB3 HIS A 292 GLN A 297 1 6
HELIX 13 AB4 GLN A 297 SER A 310 1 14
HELIX 14 AB5 GLY B 61 TRP B 65 5 5
HELIX 15 AB6 GLY B 66 PHE B 72 1 7
HELIX 16 AB7 ASN B 94 TRP B 98 5 5
HELIX 17 AB8 THR B 99 LEU B 114 1 16
HELIX 18 AB9 SER B 125 TYR B 138 1 14
HELIX 19 AC1 MET B 163 THR B 172 1 10
HELIX 20 AC2 ALA B 178 ALA B 189 1 12
HELIX 21 AC3 PRO B 196 SER B 209 1 14
HELIX 22 AC4 SER B 209 ALA B 223 1 15
HELIX 23 AC5 HIS B 226 ALA B 243 1 18
HELIX 24 AC6 PRO B 263 ALA B 276 1 14
HELIX 25 AC7 HIS B 292 GLN B 297 1 6
HELIX 26 AC8 GLN B 297 SER B 310 1 14
HELIX 27 AC9 GLY C 61 TRP C 65 5 5
HELIX 28 AD1 GLY C 66 PHE C 72 1 7
HELIX 29 AD2 ASN C 94 TRP C 98 5 5
HELIX 30 AD3 THR C 99 LEU C 114 1 16
HELIX 31 AD4 SER C 125 TYR C 138 1 14
HELIX 32 AD5 MET C 163 THR C 172 1 10
HELIX 33 AD6 ALA C 178 ALA C 189 1 12
HELIX 34 AD7 PRO C 196 SER C 209 1 14
HELIX 35 AD8 SER C 209 ALA C 223 1 15
HELIX 36 AD9 HIS C 226 ALA C 245 1 20
HELIX 37 AE1 PRO C 263 THR C 278 1 16
HELIX 38 AE2 HIS C 292 GLN C 297 1 6
HELIX 39 AE3 GLN C 297 SER C 310 1 14
HELIX 40 AE4 GLY D 61 GLY D 66 5 6
HELIX 41 AE5 ASN D 67 PHE D 72 1 6
HELIX 42 AE6 ASN D 94 TRP D 98 5 5
HELIX 43 AE7 THR D 99 LEU D 114 1 16
HELIX 44 AE8 SER D 125 TYR D 138 1 14
HELIX 45 AE9 MET D 163 THR D 172 1 10
HELIX 46 AF1 GLY D 176 ALA D 189 1 14
HELIX 47 AF2 PRO D 196 SER D 209 1 14
HELIX 48 AF3 SER D 209 ALA D 223 1 15
HELIX 49 AF4 HIS D 226 ALA D 245 1 20
HELIX 50 AF5 PRO D 263 THR D 278 1 16
HELIX 51 AF6 HIS D 292 GLN D 297 1 6
HELIX 52 AF7 GLN D 297 SER D 310 1 14
SHEET 1 AA116 HIS A 25 VAL A 29 0
SHEET 2 AA116 VAL A 32 ASP A 38 -1 O THR A 34 N VAL A 27
SHEET 3 AA116 ARG A 77 VAL A 81 -1 O ALA A 80 N PHE A 37
SHEET 4 AA116 PRO A 45 ILE A 49 1 N ILE A 46 O LEU A 79
SHEET 5 AA116 LEU A 119 HIS A 124 1 O VAL A 122 N LEU A 47
SHEET 6 AA116 VAL A 142 ILE A 148 1 O VAL A 146 N LEU A 121
SHEET 7 AA116 THR A 251 GLY A 256 1 O VAL A 254 N ILE A 147
SHEET 8 AA116 SER A 281 ILE A 286 1 O TYR A 284 N VAL A 253
SHEET 9 AA116 SER D 281 ILE D 286 -1 O LEU D 283 N LEU A 285
SHEET 10 AA116 THR D 251 GLY D 256 1 N VAL D 253 O TYR D 284
SHEET 11 AA116 VAL D 142 ILE D 148 1 N ILE D 147 O VAL D 254
SHEET 12 AA116 LEU D 119 HIS D 124 1 N LEU D 121 O VAL D 146
SHEET 13 AA116 PRO D 45 ILE D 49 1 N LEU D 47 O THR D 120
SHEET 14 AA116 ARG D 77 VAL D 81 1 O LEU D 79 N ILE D 46
SHEET 15 AA116 VAL D 32 ASP D 38 -1 N PHE D 37 O ALA D 80
SHEET 16 AA116 HIS D 25 VAL D 29 -1 N VAL D 27 O THR D 34
SHEET 1 AA2 8 HIS B 25 VAL B 29 0
SHEET 2 AA2 8 VAL B 32 ASP B 38 -1 O THR B 34 N VAL B 27
SHEET 3 AA2 8 ARG B 77 VAL B 81 -1 O ALA B 80 N PHE B 37
SHEET 4 AA2 8 PRO B 45 ILE B 49 1 N ILE B 46 O LEU B 79
SHEET 5 AA2 8 LEU B 119 HIS B 124 1 O VAL B 122 N ILE B 49
SHEET 6 AA2 8 VAL B 142 ILE B 148 1 O VAL B 146 N LEU B 121
SHEET 7 AA2 8 THR B 251 GLY B 256 1 O VAL B 254 N ILE B 147
SHEET 8 AA2 8 SER B 281 ILE B 286 1 O TYR B 284 N VAL B 253
SHEET 1 AA3 8 HIS C 25 VAL C 29 0
SHEET 2 AA3 8 VAL C 32 ASP C 38 -1 O THR C 34 N VAL C 27
SHEET 3 AA3 8 ARG C 77 VAL C 81 -1 O ALA C 80 N PHE C 37
SHEET 4 AA3 8 PRO C 45 ILE C 49 1 N ILE C 46 O LEU C 79
SHEET 5 AA3 8 LEU C 119 HIS C 124 1 O VAL C 122 N LEU C 47
SHEET 6 AA3 8 VAL C 142 ILE C 148 1 O VAL C 146 N LEU C 121
SHEET 7 AA3 8 THR C 251 GLY C 256 1 O VAL C 254 N ILE C 147
SHEET 8 AA3 8 SER C 281 ILE C 286 1 O TYR C 284 N VAL C 253
LINK CB SER A 125 O11 PHT A1000 1555 1555 1.39
LINK CB SER B 125 O11 PHT B1000 1555 1555 1.42
LINK CB SER C 125 O12 PHT C1000 1555 1555 1.41
LINK CB SER D 125 O11 PHT D1000 1555 1555 1.40
CRYST1 76.950 48.950 306.325 90.00 93.73 90.00 I 1 2 1 16
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 0.012995 0.000000 0.000847 0.00000
SCALE2 0.000000 0.020429 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003271 0.00000
TER 2180 LEU A 311
TER 4313 LEU B 311
TER 6465 LEU C 311
TER 8625 LEU D 311
MASTER 528 0 5 52 32 0 0 6 8674 4 57 92
END |