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HEADER HYDROLASE 20-AUG-19 6U2M
TITLE CRYSTAL STRUCTURE OF A HALOTAG-BASED CALCIUM INDICATOR, HALOCAMP V2,
TITLE 2 BOUND TO JF635
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOCAMP V2;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOTAG, CALCIUM, SENSOR, FLUORESCENT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DEO,E.R.SCHREITER
REVDAT 1 30-SEP-20 6U2M 0
JRNL AUTH C.DEO,L.D.LAVIS,E.R.SCHREITER
JRNL TITL CRYSTAL STRUCTURE OF A HALOTAG-BASED CALCIUM INDICATOR,
JRNL TITL 2 HALOCAMP V2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 122.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 86312
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4438
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6270
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE SET COUNT : 323
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7420
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.16000
REMARK 3 B22 (A**2) : -0.75000
REMARK 3 B33 (A**2) : 1.90000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7724 ; 0.026 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7086 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10492 ; 2.440 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16456 ; 1.285 ; 2.983
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 924 ; 7.406 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 382 ;33.783 ;24.136
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1268 ;16.937 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;21.358 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1108 ; 0.163 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8568 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1582 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 26
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0790 38.1540 75.9960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1483 T22: 0.0477
REMARK 3 T33: 0.1964 T12: -0.0197
REMARK 3 T13: 0.0145 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 3.0590 L22: 2.1199
REMARK 3 L33: 2.0479 L12: 1.9960
REMARK 3 L13: -2.0886 L23: -2.0720
REMARK 3 S TENSOR
REMARK 3 S11: 0.0166 S12: 0.0491 S13: -0.1307
REMARK 3 S21: -0.0714 S22: -0.0356 S23: 0.0289
REMARK 3 S31: 0.0485 S32: 0.0386 S33: 0.0190
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 27 A 31
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5466 31.2902 60.7087
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.1812
REMARK 3 T33: 0.0400 T12: -0.0802
REMARK 3 T13: 0.0324 T23: -0.0709
REMARK 3 L TENSOR
REMARK 3 L11: 1.5921 L22: 15.1139
REMARK 3 L33: 29.7974 L12: -3.7662
REMARK 3 L13: 2.3335 L23: 7.2582
REMARK 3 S TENSOR
REMARK 3 S11: -0.1884 S12: -0.0829 S13: -0.0712
REMARK 3 S21: 0.7658 S22: -0.0454 S23: 0.3268
REMARK 3 S31: 0.4566 S32: -0.6810 S33: 0.2338
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 32 A 109
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0250 24.7376 45.0532
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.2080
REMARK 3 T33: 0.2147 T12: -0.0382
REMARK 3 T13: 0.0146 T23: -0.1168
REMARK 3 L TENSOR
REMARK 3 L11: 0.6256 L22: 0.9200
REMARK 3 L33: 0.8898 L12: -0.3899
REMARK 3 L13: -0.6199 L23: -0.0450
REMARK 3 S TENSOR
REMARK 3 S11: 0.0778 S12: -0.3586 S13: 0.2045
REMARK 3 S21: 0.1119 S22: 0.2441 S23: 0.0530
REMARK 3 S31: -0.1804 S32: 0.3401 S33: -0.3219
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 110 A 159
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2776 4.5467 50.3778
REMARK 3 T TENSOR
REMARK 3 T11: 0.2027 T22: 0.2521
REMARK 3 T33: 0.2158 T12: 0.1836
REMARK 3 T13: 0.0450 T23: 0.1668
REMARK 3 L TENSOR
REMARK 3 L11: 2.2762 L22: 2.4985
REMARK 3 L33: 1.8114 L12: 0.9382
REMARK 3 L13: -0.7610 L23: 1.0911
REMARK 3 S TENSOR
REMARK 3 S11: -0.4554 S12: -0.5770 S13: -0.3126
REMARK 3 S21: 0.1745 S22: 0.2263 S23: 0.2043
REMARK 3 S31: 0.3982 S32: 0.5174 S33: 0.2291
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 160 A 179
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6347 -3.0227 41.1947
REMARK 3 T TENSOR
REMARK 3 T11: 0.2007 T22: 0.0549
REMARK 3 T33: 0.2502 T12: 0.0869
REMARK 3 T13: 0.0155 T23: 0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 3.7212 L22: 5.6940
REMARK 3 L33: 6.5898 L12: 4.2196
REMARK 3 L13: 2.5054 L23: 4.8665
REMARK 3 S TENSOR
REMARK 3 S11: -0.2058 S12: -0.1232 S13: -0.3212
REMARK 3 S21: 0.1566 S22: 0.0188 S23: -0.2538
REMARK 3 S31: 0.6398 S32: 0.2021 S33: 0.1871
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 202 A 335
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5045 11.3174 33.7627
REMARK 3 T TENSOR
REMARK 3 T11: 0.0962 T22: 0.0242
REMARK 3 T33: 0.2196 T12: 0.0107
REMARK 3 T13: -0.0332 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.1972 L22: 0.5396
REMARK 3 L33: 0.9352 L12: -0.0306
REMARK 3 L13: -0.7590 L23: -0.0716
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: -0.1031 S13: -0.0953
REMARK 3 S21: -0.0845 S22: 0.0738 S23: -0.0296
REMARK 3 S31: 0.0680 S32: 0.0867 S33: -0.0184
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 336 A 351
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9949 21.3339 65.9808
REMARK 3 T TENSOR
REMARK 3 T11: 0.2085 T22: 0.2449
REMARK 3 T33: 0.2043 T12: 0.1002
REMARK 3 T13: -0.0359 T23: -0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 1.2299 L22: 1.1493
REMARK 3 L33: 9.7994 L12: 1.1828
REMARK 3 L13: 3.4568 L23: 3.3153
REMARK 3 S TENSOR
REMARK 3 S11: 0.2497 S12: 0.1742 S13: -0.0869
REMARK 3 S21: 0.2582 S22: 0.1132 S23: -0.0562
REMARK 3 S31: 0.8129 S32: 0.5238 S33: -0.3630
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 352 A 419
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2102 30.7691 86.2387
REMARK 3 T TENSOR
REMARK 3 T11: 0.1124 T22: 0.0587
REMARK 3 T33: 0.2042 T12: -0.0328
REMARK 3 T13: 0.0141 T23: -0.0697
REMARK 3 L TENSOR
REMARK 3 L11: 1.8315 L22: 1.0288
REMARK 3 L33: 0.1433 L12: 0.8363
REMARK 3 L13: -0.2146 L23: -0.3619
REMARK 3 S TENSOR
REMARK 3 S11: 0.2609 S12: -0.1805 S13: 0.0384
REMARK 3 S21: -0.0098 S22: -0.1861 S23: 0.0956
REMARK 3 S31: 0.0059 S32: 0.0793 S33: -0.0748
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 420 A 436
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5987 42.2963 73.7193
REMARK 3 T TENSOR
REMARK 3 T11: 0.1473 T22: 0.0388
REMARK 3 T33: 0.2035 T12: 0.0063
REMARK 3 T13: -0.0561 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 1.8527 L22: 1.7402
REMARK 3 L33: 5.3473 L12: 0.8616
REMARK 3 L13: 2.7303 L23: -0.0243
REMARK 3 S TENSOR
REMARK 3 S11: 0.0997 S12: 0.0339 S13: -0.0514
REMARK 3 S21: 0.1235 S22: 0.1314 S23: 0.0368
REMARK 3 S31: 0.1480 S32: -0.0867 S33: -0.2312
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 437 A 489
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8191 49.9831 73.8060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1564 T22: 0.0562
REMARK 3 T33: 0.1642 T12: -0.0427
REMARK 3 T13: -0.0546 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 2.7092 L22: 0.7762
REMARK 3 L33: 1.1315 L12: -0.2941
REMARK 3 L13: 0.1330 L23: -0.4767
REMARK 3 S TENSOR
REMARK 3 S11: -0.0927 S12: 0.2878 S13: 0.2805
REMARK 3 S21: 0.1172 S22: -0.1162 S23: -0.0418
REMARK 3 S31: -0.2183 S32: 0.1819 S33: 0.2090
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 26
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8961 26.4791 136.7338
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.0453
REMARK 3 T33: 0.2663 T12: 0.0383
REMARK 3 T13: -0.0132 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 2.1440 L22: 2.2756
REMARK 3 L33: 0.9251 L12: 2.0869
REMARK 3 L13: 0.9548 L23: 1.2734
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: 0.0410 S13: 0.0816
REMARK 3 S21: -0.0371 S22: -0.0368 S23: 0.0604
REMARK 3 S31: -0.0010 S32: -0.0830 S33: 0.0729
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 27 C 31
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8231 33.6916 121.9078
REMARK 3 T TENSOR
REMARK 3 T11: 0.2027 T22: 0.3120
REMARK 3 T33: 0.1020 T12: -0.0205
REMARK 3 T13: 0.0271 T23: 0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 0.0537 L22: 2.8450
REMARK 3 L33: 11.6139 L12: -0.3860
REMARK 3 L13: -0.7754 L23: 5.7437
REMARK 3 S TENSOR
REMARK 3 S11: -0.0463 S12: 0.0424 S13: -0.0151
REMARK 3 S21: 0.2451 S22: -0.2652 S23: 0.1464
REMARK 3 S31: 0.4541 S32: -0.5557 S33: 0.3115
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 32 C 109
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9997 39.9834 106.9309
REMARK 3 T TENSOR
REMARK 3 T11: 0.0941 T22: 0.2778
REMARK 3 T33: 0.2252 T12: -0.1150
REMARK 3 T13: -0.0517 T23: 0.0745
REMARK 3 L TENSOR
REMARK 3 L11: 0.3616 L22: 1.0725
REMARK 3 L33: 0.8622 L12: -0.4114
REMARK 3 L13: 0.5048 L23: -0.5603
REMARK 3 S TENSOR
REMARK 3 S11: 0.0878 S12: -0.2948 S13: -0.1170
REMARK 3 S21: 0.0922 S22: 0.2212 S23: -0.0136
REMARK 3 S31: 0.1190 S32: -0.3627 S33: -0.3090
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 110 C 154
REMARK 3 ORIGIN FOR THE GROUP (A): 35.1215 60.9782 112.5217
REMARK 3 T TENSOR
REMARK 3 T11: 0.1439 T22: 0.3155
REMARK 3 T33: 0.3042 T12: 0.1951
REMARK 3 T13: -0.1802 T23: -0.2870
REMARK 3 L TENSOR
REMARK 3 L11: 4.3886 L22: 2.8013
REMARK 3 L33: 0.7400 L12: 2.6410
REMARK 3 L13: 0.1764 L23: -0.8362
REMARK 3 S TENSOR
REMARK 3 S11: -0.4172 S12: -0.8080 S13: 0.4291
REMARK 3 S21: 0.0774 S22: -0.0349 S23: -0.2940
REMARK 3 S31: -0.2726 S32: -0.3809 S33: 0.4521
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 155 C 337
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9617 54.8929 97.2107
REMARK 3 T TENSOR
REMARK 3 T11: 0.0787 T22: 0.0413
REMARK 3 T33: 0.2206 T12: 0.0000
REMARK 3 T13: 0.0015 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 0.8617 L22: 0.5142
REMARK 3 L33: 0.9286 L12: 0.0520
REMARK 3 L13: 0.7457 L23: 0.0606
REMARK 3 S TENSOR
REMARK 3 S11: -0.0847 S12: -0.1499 S13: 0.1440
REMARK 3 S21: -0.1103 S22: 0.0316 S23: 0.0279
REMARK 3 S31: -0.0554 S32: -0.1218 S33: 0.0532
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 338 C 345
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9521 46.0877 123.5233
REMARK 3 T TENSOR
REMARK 3 T11: 0.1373 T22: 0.2533
REMARK 3 T33: 0.1435 T12: 0.0627
REMARK 3 T13: 0.0461 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 1.9001 L22: 6.4042
REMARK 3 L33: 8.3649 L12: 2.9030
REMARK 3 L13: -1.5760 L23: -6.1320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0274 S12: 0.4019 S13: -0.1940
REMARK 3 S21: 0.2206 S22: 0.6411 S23: 0.1015
REMARK 3 S31: -0.4526 S32: -0.4061 S33: -0.6137
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 346 C 357
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4311 37.6750 137.8942
REMARK 3 T TENSOR
REMARK 3 T11: 0.1176 T22: 0.1015
REMARK 3 T33: 0.1244 T12: 0.0434
REMARK 3 T13: -0.0378 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.0675 L22: 2.5727
REMARK 3 L33: 6.9170 L12: 1.1378
REMARK 3 L13: 0.6132 L23: -1.7039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0533 S12: -0.0474 S13: -0.0298
REMARK 3 S21: -0.0710 S22: -0.0707 S23: 0.1436
REMARK 3 S31: -0.1669 S32: -0.2640 S33: 0.0173
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 358 C 419
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7964 33.7107 147.4929
REMARK 3 T TENSOR
REMARK 3 T11: 0.0982 T22: 0.0661
REMARK 3 T33: 0.2035 T12: -0.0023
REMARK 3 T13: -0.0153 T23: 0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 2.0302 L22: 0.7813
REMARK 3 L33: 0.1947 L12: 0.7821
REMARK 3 L13: 0.2464 L23: 0.1942
REMARK 3 S TENSOR
REMARK 3 S11: 0.2566 S12: -0.1901 S13: -0.0563
REMARK 3 S21: 0.0107 S22: -0.2092 S23: -0.0653
REMARK 3 S31: -0.0009 S32: -0.0634 S33: -0.0473
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 420 C 436
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3417 22.1922 134.6044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1105 T22: 0.0476
REMARK 3 T33: 0.2056 T12: 0.0662
REMARK 3 T13: 0.0024 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 4.1515 L22: 4.7335
REMARK 3 L33: 3.4427 L12: 1.0164
REMARK 3 L13: -3.7773 L23: -0.8976
REMARK 3 S TENSOR
REMARK 3 S11: 0.1273 S12: 0.1900 S13: 0.2175
REMARK 3 S21: 0.2149 S22: 0.1029 S23: -0.0759
REMARK 3 S31: -0.1057 S32: -0.1638 S33: -0.2302
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 437 C 489
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1069 14.6671 134.5818
REMARK 3 T TENSOR
REMARK 3 T11: 0.1653 T22: 0.0388
REMARK 3 T33: 0.1870 T12: -0.0119
REMARK 3 T13: 0.0210 T23: -0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 3.0650 L22: 0.1536
REMARK 3 L33: 1.6940 L12: -0.4113
REMARK 3 L13: -0.2414 L23: 0.4322
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: 0.2533 S13: -0.2725
REMARK 3 S21: 0.0681 S22: -0.0715 S23: 0.0531
REMARK 3 S31: 0.1955 S32: -0.1709 S33: 0.0817
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6U2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1000243781.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-18
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 : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9774
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90798
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 122.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 1.34700
REMARK 200 R SYM FOR SHELL (I) : 1.34700
REMARK 200 FOR SHELL : 0.500
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: 5UY1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (V/V) PEG 200, 100 MM MES/ SODIUM
REMARK 280 HYDROXIDE PH 6.0, AND 5% (W/V) PEG 3000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 VAL A 1
REMARK 465 ARG A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 180
REMARK 465 GLY A 181
REMARK 465 GLY A 182
REMARK 465 THR A 183
REMARK 465 GLY A 184
REMARK 465 GLY A 185
REMARK 465 SER A 186
REMARK 465 GLY A 187
REMARK 465 GLY A 188
REMARK 465 THR A 189
REMARK 465 GLY A 190
REMARK 465 GLY A 191
REMARK 465 SER A 192
REMARK 465 GLY A 193
REMARK 465 GLY A 194
REMARK 465 THR A 195
REMARK 465 GLY A 196
REMARK 465 GLY A 197
REMARK 465 SER A 198
REMARK 465 MET A 199
REMARK 465 ALA A 200
REMARK 465 GLU A 201
REMARK 465 LYS A 490
REMARK 465 MET C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 GLY C 0
REMARK 465 VAL C 1
REMARK 465 ARG C 2
REMARK 465 VAL C 3
REMARK 465 GLY C 180
REMARK 465 GLY C 181
REMARK 465 GLY C 182
REMARK 465 THR C 183
REMARK 465 GLY C 184
REMARK 465 GLY C 185
REMARK 465 SER C 186
REMARK 465 GLY C 187
REMARK 465 GLY C 188
REMARK 465 THR C 189
REMARK 465 GLY C 190
REMARK 465 GLY C 191
REMARK 465 SER C 192
REMARK 465 GLY C 193
REMARK 465 GLY C 194
REMARK 465 THR C 195
REMARK 465 GLY C 196
REMARK 465 GLY C 197
REMARK 465 SER C 198
REMARK 465 MET C 199
REMARK 465 ALA C 200
REMARK 465 GLU C 201
REMARK 465 LYS C 490
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 OD1 ASP A 304 C27 PUJ A 600 1.96
REMARK 500 OD1 ASP C 304 C27 PUJ C 600 2.09
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 6 CD ARG A 6 NE -0.117
REMARK 500 THR A 31 CB THR A 31 CG2 0.225
REMARK 500 ASP A 110 CB ASP A 110 CG -0.155
REMARK 500 GLU A 291 CD GLU A 291 OE2 0.068
REMARK 500 GLU A 319 CG GLU A 319 CD 0.112
REMARK 500 TRP A 339 CB TRP A 339 CG 0.177
REMARK 500 GLU A 396 CG GLU A 396 CD 0.094
REMARK 500 GLU A 396 CD GLU A 396 OE2 -0.068
REMARK 500 ILE C 4 N ILE C 4 CA 0.125
REMARK 500 ARG C 6 CD ARG C 6 NE -0.120
REMARK 500 GLU C 177 CG GLU C 177 CD 0.097
REMARK 500 GLU C 319 CG GLU C 319 CD 0.113
REMARK 500 GLU C 353 CD GLU C 353 OE1 0.067
REMARK 500 GLU C 396 CD GLU C 396 OE2 -0.080
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 PROTEIN: 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 6 CD - NE - CZ ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 6 NE - CZ - NH2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 LEU A 12 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG A 21 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 LEU A 104 CA - CB - CG ANGL. DEV. = 23.0 DEGREES
REMARK 500 LEU A 104 CB - CG - CD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500 MET A 109 CG - SD - CE ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP A 110 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 PRO A 152 C - N - CA ANGL. DEV. = -14.3 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 GLU A 319 OE1 - CD - OE2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG A 379 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 MET A 393 CG - SD - CE ANGL. DEV. = -12.2 DEGREES
REMARK 500 ASP A 437 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG C 6 CD - NE - CZ ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG C 6 NE - CZ - NH2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 ASP C 8 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU C 12 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG C 21 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG C 73 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 LEU C 104 CA - CB - CG ANGL. DEV. = 21.8 DEGREES
REMARK 500 LEU C 104 CB - CG - CD2 ANGL. DEV. = 17.4 DEGREES
REMARK 500 ASP C 110 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP C 149 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 GLU C 177 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG C 219 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP C 274 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 GLU C 319 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP C 366 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 448 CG - CD - NE ANGL. DEV. = -12.6 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 LYS A 29 -46.00 72.94
REMARK 500 GLU A 30 -54.36 72.68
REMARK 500 THR A 31 -61.40 87.94
REMARK 500 ASP A 39 -56.26 82.13
REMARK 500 VAL A 128 -70.27 -128.90
REMARK 500 LEU A 154 -97.29 -115.68
REMARK 500 ASN A 161 62.35 -150.48
REMARK 500 THR A 241 -164.10 -101.59
REMARK 500 GLU A 296 -86.76 -110.23
REMARK 500 ASP A 304 -130.38 60.02
REMARK 500 ASN A 317 48.52 -140.67
REMARK 500 TRP A 339 -8.60 -50.25
REMARK 500 ASP A 344 73.24 -108.71
REMARK 500 GLN A 345 98.81 -179.79
REMARK 500 GLU A 424 -63.14 121.77
REMARK 500 PHE C 26 -71.57 -105.45
REMARK 500 ARG C 27 -5.75 59.67
REMARK 500 PRO C 28 89.26 -38.64
REMARK 500 LYS C 29 -85.47 69.35
REMARK 500 GLU C 30 -88.16 118.01
REMARK 500 THR C 31 -97.59 109.51
REMARK 500 THR C 38 -72.61 -28.61
REMARK 500 VAL C 128 -66.27 -128.52
REMARK 500 LEU C 154 -100.04 -115.48
REMARK 500 PRO C 240 50.05 -109.13
REMARK 500 THR C 241 -163.47 -101.52
REMARK 500 GLU C 296 -89.15 -106.75
REMARK 500 ASP C 304 -124.18 56.00
REMARK 500 ASN C 317 53.60 -140.35
REMARK 500 ASP C 337 58.10 -111.38
REMARK 500 TRP C 339 -54.07 -20.73
REMARK 500 ASP C 344 50.87 -100.01
REMARK 500 GLU C 424 -67.72 114.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 207 PHE A 208 -139.66
REMARK 500 ARG C 27 PRO C 28 -137.29
REMARK 500 PRO C 207 PHE C 208 -144.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG C 6 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 605 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 362 OD1
REMARK 620 2 ASP A 364 OD1 80.5
REMARK 620 3 ASP A 366 OD1 83.3 89.5
REMARK 620 4 THR A 368 O 83.7 156.9 72.0
REMARK 620 5 GLU A 373 OE1 112.2 121.2 146.7 80.4
REMARK 620 6 GLU A 373 OE2 99.7 69.2 157.4 130.5 52.4
REMARK 620 7 HOH A 766 O 157.6 80.7 84.6 110.1 87.9 84.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 398 OD1
REMARK 620 2 ASP A 400 OD1 65.7
REMARK 620 3 ASN A 402 OD1 91.7 65.5
REMARK 620 4 THR A 404 O 99.4 146.5 86.1
REMARK 620 5 GLU A 409 OE1 77.1 85.4 150.9 121.9
REMARK 620 6 GLU A 409 OE2 110.8 128.8 156.6 84.1 47.2
REMARK 620 7 HOH A 784 O 149.1 91.1 97.0 110.6 81.2 67.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 603 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 435 OD1
REMARK 620 2 ASP A 437 OD1 83.2
REMARK 620 3 ASN A 439 OD1 86.5 76.1
REMARK 620 4 TYR A 441 O 93.6 161.9 85.9
REMARK 620 5 GLU A 446 OE1 106.8 127.1 153.6 70.9
REMARK 620 6 GLU A 446 OE2 99.8 76.6 151.0 121.5 50.7
REMARK 620 7 HOH A 802 O 171.6 89.8 87.4 91.7 81.1 82.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 471 OD1
REMARK 620 2 ASP A 473 OD1 80.6
REMARK 620 3 ASP A 475 OD1 88.0 79.2
REMARK 620 4 GLN A 477 O 82.3 148.1 73.5
REMARK 620 5 GLU A 482 OE1 95.2 82.2 160.4 126.2
REMARK 620 6 GLU A 482 OE2 116.3 131.7 141.2 80.2 52.9
REMARK 620 7 HOH A 788 O 163.3 87.1 78.5 103.0 94.3 80.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 362 OD1
REMARK 620 2 ASP C 364 OD1 77.7
REMARK 620 3 ASP C 366 OD1 85.5 79.0
REMARK 620 4 THR C 368 O 88.0 154.2 78.6
REMARK 620 5 GLU C 373 OE1 114.9 126.6 148.8 78.9
REMARK 620 6 GLU C 373 OE2 99.0 76.9 153.8 127.1 50.5
REMARK 620 7 HOH C 741 O 161.0 83.7 86.9 107.6 79.7 80.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 603 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 398 OD1
REMARK 620 2 ASP C 400 OD1 65.7
REMARK 620 3 ASN C 402 OD1 94.1 72.4
REMARK 620 4 THR C 404 O 101.7 153.0 85.5
REMARK 620 5 GLU C 409 OE1 76.6 79.8 152.0 122.0
REMARK 620 6 GLU C 409 OE2 112.0 122.7 153.3 83.8 47.6
REMARK 620 7 HOH C 752 O 147.9 86.2 91.5 110.2 83.8 69.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 435 OD1
REMARK 620 2 ASP C 437 OD1 82.2
REMARK 620 3 ASN C 439 OD1 88.7 74.9
REMARK 620 4 TYR C 441 O 88.3 155.8 82.8
REMARK 620 5 GLU C 446 OE1 106.0 124.5 156.4 79.4
REMARK 620 6 GLU C 446 OE2 100.7 71.1 143.0 132.7 53.4
REMARK 620 7 HOH C 783 O 168.4 95.9 79.8 88.9 84.5 89.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 605 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 471 OD1
REMARK 620 2 ASP C 473 OD1 77.7
REMARK 620 3 ASP C 475 OD1 85.1 84.2
REMARK 620 4 GLN C 477 O 86.3 155.7 76.3
REMARK 620 5 GLU C 482 OE1 86.4 75.2 158.9 122.4
REMARK 620 6 GLU C 482 OE2 109.1 125.6 148.5 76.8 52.5
REMARK 620 7 HOH C 769 O 165.3 91.9 83.5 100.0 101.2 85.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PUJ A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PUJ C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 605
DBREF 6U2M A -7 490 PDB 6U2M 6U2M -7 490
DBREF 6U2M C -7 490 PDB 6U2M 6U2M -7 490
SEQRES 1 A 498 MET HIS HIS HIS HIS HIS HIS GLY VAL ARG VAL ILE PRO
SEQRES 2 A 498 ARG LEU ASP THR LEU ILE LEU VAL LYS ALA MET GLY HIS
SEQRES 3 A 498 ARG LYS ARG PHE GLY ASN PRO PHE ARG PRO LYS GLU THR
SEQRES 4 A 498 PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG LYS LEU
SEQRES 5 A 498 ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR LEU PRO
SEQRES 6 A 498 MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU MET ASP
SEQRES 7 A 498 HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP ARG GLU
SEQRES 8 A 498 PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE ALA GLY
SEQRES 9 A 498 GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU TYR MET
SEQRES 10 A 498 ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU LEU PHE
SEQRES 11 A 498 TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA GLU ALA
SEQRES 12 A 498 ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS ALA VAL
SEQRES 13 A 498 ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU ASP ASN
SEQRES 14 A 498 PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP LEU SER
SEQRES 15 A 498 THR LEU GLU ILE SER GLY GLY GLY THR GLY GLY SER GLY
SEQRES 16 A 498 GLY THR GLY GLY SER GLY GLY THR GLY GLY SER MET ALA
SEQRES 17 A 498 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 18 A 498 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 19 A 498 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 20 A 498 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 21 A 498 VAL ALA PRO LYS HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 22 A 498 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 23 A 498 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 24 A 498 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 25 A 498 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 26 A 498 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 27 A 498 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO PHE ALA ARG
SEQRES 28 A 498 ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU
SEQRES 29 A 498 ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE
SEQRES 30 A 498 THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY
SEQRES 31 A 498 GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN
SEQRES 32 A 498 GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO
SEQRES 33 A 498 GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR
SEQRES 34 A 498 ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE
SEQRES 35 A 498 ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU
SEQRES 36 A 498 ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP
SEQRES 37 A 498 GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP
SEQRES 38 A 498 GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET
SEQRES 39 A 498 MET THR ALA LYS
SEQRES 1 C 498 MET HIS HIS HIS HIS HIS HIS GLY VAL ARG VAL ILE PRO
SEQRES 2 C 498 ARG LEU ASP THR LEU ILE LEU VAL LYS ALA MET GLY HIS
SEQRES 3 C 498 ARG LYS ARG PHE GLY ASN PRO PHE ARG PRO LYS GLU THR
SEQRES 4 C 498 PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG LYS LEU
SEQRES 5 C 498 ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR LEU PRO
SEQRES 6 C 498 MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU MET ASP
SEQRES 7 C 498 HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP ARG GLU
SEQRES 8 C 498 PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE ALA GLY
SEQRES 9 C 498 GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU TYR MET
SEQRES 10 C 498 ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU LEU PHE
SEQRES 11 C 498 TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA GLU ALA
SEQRES 12 C 498 ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS ALA VAL
SEQRES 13 C 498 ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU ASP ASN
SEQRES 14 C 498 PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP LEU SER
SEQRES 15 C 498 THR LEU GLU ILE SER GLY GLY GLY THR GLY GLY SER GLY
SEQRES 16 C 498 GLY THR GLY GLY SER GLY GLY THR GLY GLY SER MET ALA
SEQRES 17 C 498 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 18 C 498 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 19 C 498 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 20 C 498 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 21 C 498 VAL ALA PRO LYS HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 22 C 498 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 23 C 498 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 24 C 498 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 25 C 498 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 26 C 498 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 27 C 498 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO PHE ALA ARG
SEQRES 28 C 498 ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU
SEQRES 29 C 498 ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE
SEQRES 30 C 498 THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY
SEQRES 31 C 498 GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN
SEQRES 32 C 498 GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO
SEQRES 33 C 498 GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR
SEQRES 34 C 498 ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE
SEQRES 35 C 498 ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU
SEQRES 36 C 498 ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP
SEQRES 37 C 498 GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP
SEQRES 38 C 498 GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET
SEQRES 39 C 498 MET THR ALA LYS
HET PUJ A 600 50
HET CL A 601 1
HET CA A 602 1
HET CA A 603 1
HET CA A 604 1
HET CA A 605 1
HET PUJ C 600 50
HET CL C 601 1
HET CA C 602 1
HET CA C 603 1
HET CA C 604 1
HET CA C 605 1
HETNAM PUJ (1E,3S)-1-{10-[2-CARBOXY-5-({2-[2-(HEXYLOXY)
HETNAM 2 PUJ ETHOXY]ETHYL}CARBAMOYL)PHENYL]-7-(3-FLUOROAZETIDIN-1-
HETNAM 3 PUJ YL)-5,5-DIMETHYLDIBENZ O[B,E]SILIN-3(5H)-YLIDENE}-3-
HETNAM 4 PUJ FLUOROAZETIDIN-1-IUM
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
HETSYN PUJ JF635
FORMUL 3 PUJ 2(C39 H48 F2 N3 O5 SI 1+)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 CA 8(CA 2+)
FORMUL 15 HOH *203(H2 O)
HELIX 1 AA1 ARG A 6 ARG A 19 1 14
HELIX 2 AA2 THR A 31 ARG A 36 1 6
HELIX 3 AA3 ASP A 39 ILE A 46 1 8
HELIX 4 AA4 ASN A 49 GLY A 54 1 6
HELIX 5 AA5 LEU A 56 VAL A 60 5 5
HELIX 6 AA6 THR A 65 GLU A 74 1 10
HELIX 7 AA7 PRO A 75 LEU A 77 5 3
HELIX 8 AA8 ASN A 78 ASP A 81 5 4
HELIX 9 AA9 ARG A 82 PHE A 88 1 7
HELIX 10 AB1 PRO A 98 SER A 115 1 18
HELIX 11 AB2 PRO A 131 LEU A 142 1 12
HELIX 12 AB3 LEU A 156 ASN A 161 1 6
HELIX 13 AB4 ASN A 161 LEU A 176 1 16
HELIX 14 AB5 SER A 242 ARG A 247 5 6
HELIX 15 AB6 ILE A 249 ALA A 254 1 6
HELIX 16 AB7 PHE A 278 LEU A 293 1 16
HELIX 17 AB8 ASP A 304 ASN A 317 1 14
HELIX 18 AB9 THR A 347 ASP A 362 1 16
HELIX 19 AC1 THR A 370 LEU A 381 1 12
HELIX 20 AC2 THR A 386 GLU A 396 1 11
HELIX 21 AC3 PHE A 407 MET A 418 1 12
HELIX 22 AC4 GLU A 424 ASP A 435 1 12
HELIX 23 AC5 SER A 443 LEU A 454 1 12
HELIX 24 AC6 THR A 459 ASP A 471 1 13
HELIX 25 AC7 TYR A 480 ALA A 489 1 10
HELIX 26 AC8 ARG C 6 LYS C 20 1 15
HELIX 27 AC9 THR C 31 ARG C 36 1 6
HELIX 28 AD1 THR C 37 ILE C 46 1 10
HELIX 29 AD2 ASN C 49 GLY C 54 1 6
HELIX 30 AD3 LEU C 56 VAL C 60 5 5
HELIX 31 AD4 THR C 65 GLU C 74 1 10
HELIX 32 AD5 PRO C 75 LEU C 77 5 3
HELIX 33 AD6 ASN C 78 ASP C 81 5 4
HELIX 34 AD7 ARG C 82 LEU C 92 1 11
HELIX 35 AD8 PRO C 98 SER C 115 1 18
HELIX 36 AD9 PRO C 131 LEU C 142 1 12
HELIX 37 AE1 LEU C 156 ASN C 161 1 6
HELIX 38 AE2 ASN C 161 THR C 175 1 15
HELIX 39 AE3 SER C 242 ARG C 247 5 6
HELIX 40 AE4 ILE C 249 VAL C 253 5 5
HELIX 41 AE5 PHE C 278 LEU C 293 1 16
HELIX 42 AE6 ASP C 304 ASN C 317 1 14
HELIX 43 AE7 THR C 347 ASP C 362 1 16
HELIX 44 AE8 THR C 370 LEU C 381 1 12
HELIX 45 AE9 THR C 386 GLU C 396 1 11
HELIX 46 AF1 PHE C 407 ASP C 420 1 14
HELIX 47 AF2 GLU C 424 ASP C 435 1 12
HELIX 48 AF3 ALA C 444 LEU C 454 1 11
HELIX 49 AF4 THR C 459 ASP C 471 1 13
HELIX 50 AF5 TYR C 480 THR C 488 1 9
SHEET 1 AA1 8 CYS A 145 GLY A 153 0
SHEET 2 AA1 8 LYS A 119 PRO A 126 1 N TRP A 123 O ILE A 150
SHEET 3 AA1 8 VAL A 321 MET A 327 1 O PHE A 326 N LEU A 120
SHEET 4 AA1 8 VAL A 298 HIS A 303 1 N ILE A 302 O ALA A 325
SHEET 5 AA1 8 VAL A 233 LEU A 236 1 N LEU A 234 O VAL A 299
SHEET 6 AA1 8 CYS A 259 PRO A 262 1 O ILE A 260 N PHE A 235
SHEET 7 AA1 8 GLU A 218 VAL A 225 -1 N VAL A 225 O CYS A 259
SHEET 8 AA1 8 HIS A 211 VAL A 215 -1 N VAL A 215 O GLU A 218
SHEET 1 AA2 2 THR A 368 ILE A 369 0
SHEET 2 AA2 2 ILE A 405 ASP A 406 -1 O ILE A 405 N ILE A 369
SHEET 1 AA3 2 TYR A 441 ILE A 442 0
SHEET 2 AA3 2 VAL A 478 ASN A 479 -1 O VAL A 478 N ILE A 442
SHEET 1 AA4 8 CYS C 145 GLY C 153 0
SHEET 2 AA4 8 LYS C 119 PRO C 126 1 N LEU C 121 O LYS C 146
SHEET 3 AA4 8 VAL C 321 MET C 327 1 O PHE C 326 N LEU C 120
SHEET 4 AA4 8 VAL C 298 HIS C 303 1 N ILE C 302 O ALA C 325
SHEET 5 AA4 8 VAL C 233 LEU C 236 1 N LEU C 234 O VAL C 301
SHEET 6 AA4 8 CYS C 259 PRO C 262 1 O ILE C 260 N PHE C 235
SHEET 7 AA4 8 GLU C 218 VAL C 225 -1 N VAL C 225 O CYS C 259
SHEET 8 AA4 8 HIS C 211 VAL C 215 -1 N VAL C 215 O GLU C 218
SHEET 1 AA5 2 THR C 368 ILE C 369 0
SHEET 2 AA5 2 ILE C 405 ASP C 406 -1 O ILE C 405 N ILE C 369
SHEET 1 AA6 2 TYR C 441 SER C 443 0
SHEET 2 AA6 2 GLN C 477 ASN C 479 -1 O VAL C 478 N ILE C 442
LINK OD1 ASP A 362 CA CA A 605 1555 1555 2.30
LINK OD1 ASP A 364 CA CA A 605 1555 1555 2.43
LINK OD1 ASP A 366 CA CA A 605 1555 1555 2.34
LINK O THR A 368 CA CA A 605 1555 1555 2.38
LINK OE1 GLU A 373 CA CA A 605 1555 1555 2.37
LINK OE2 GLU A 373 CA CA A 605 1555 1555 2.51
LINK OD1 ASP A 398 CA CA A 602 1555 1555 2.58
LINK OD1 ASP A 400 CA CA A 602 1555 1555 2.92
LINK OD1 ASN A 402 CA CA A 602 1555 1555 2.49
LINK O THR A 404 CA CA A 602 1555 1555 2.45
LINK OE1 GLU A 409 CA CA A 602 1555 1555 2.66
LINK OE2 GLU A 409 CA CA A 602 1555 1555 2.72
LINK OD1 ASP A 435 CA CA A 603 1555 1555 2.37
LINK OD1 ASP A 437 CA CA A 603 1555 1555 2.22
LINK OD1 ASN A 439 CA CA A 603 1555 1555 2.42
LINK O TYR A 441 CA CA A 603 1555 1555 2.20
LINK OE1 GLU A 446 CA CA A 603 1555 1555 2.57
LINK OE2 GLU A 446 CA CA A 603 1555 1555 2.46
LINK OD1 ASP A 471 CA CA A 604 1555 1555 2.15
LINK OD1 ASP A 473 CA CA A 604 1555 1555 2.39
LINK OD1 ASP A 475 CA CA A 604 1555 1555 2.53
LINK O GLN A 477 CA CA A 604 1555 1555 2.53
LINK OE1 GLU A 482 CA CA A 604 1555 1555 2.37
LINK OE2 GLU A 482 CA CA A 604 1555 1555 2.57
LINK CA CA A 602 O HOH A 784 1555 1555 2.45
LINK CA CA A 603 O HOH A 802 1555 1555 2.42
LINK CA CA A 604 O HOH A 788 1555 1555 2.07
LINK CA CA A 605 O HOH A 766 1555 1555 2.20
LINK OD1 ASP C 362 CA CA C 602 1555 1555 2.33
LINK OD1 ASP C 364 CA CA C 602 1555 1555 2.65
LINK OD1 ASP C 366 CA CA C 602 1555 1555 2.34
LINK O THR C 368 CA CA C 602 1555 1555 2.33
LINK OE1 GLU C 373 CA CA C 602 1555 1555 2.39
LINK OE2 GLU C 373 CA CA C 602 1555 1555 2.59
LINK OD1 ASP C 398 CA CA C 603 1555 1555 2.50
LINK OD1 ASP C 400 CA CA C 603 1555 1555 2.96
LINK OD1 ASN C 402 CA CA C 603 1555 1555 2.46
LINK O THR C 404 CA CA C 603 1555 1555 2.47
LINK OE1 GLU C 409 CA CA C 603 1555 1555 2.60
LINK OE2 GLU C 409 CA CA C 603 1555 1555 2.74
LINK OD1 ASP C 435 CA CA C 604 1555 1555 2.39
LINK OD1 ASP C 437 CA CA C 604 1555 1555 2.38
LINK OD1 ASN C 439 CA CA C 604 1555 1555 2.48
LINK O TYR C 441 CA CA C 604 1555 1555 2.22
LINK OE1 GLU C 446 CA CA C 604 1555 1555 2.47
LINK OE2 GLU C 446 CA CA C 604 1555 1555 2.55
LINK OD1 ASP C 471 CA CA C 605 1555 1555 2.31
LINK OD1 ASP C 473 CA CA C 605 1555 1555 2.33
LINK OD1 ASP C 475 CA CA C 605 1555 1555 2.28
LINK O GLN C 477 CA CA C 605 1555 1555 2.51
LINK OE1 GLU C 482 CA CA C 605 1555 1555 2.41
LINK OE2 GLU C 482 CA CA C 605 1555 1555 2.59
LINK CA CA C 602 O HOH C 741 1555 1555 2.10
LINK CA CA C 603 O HOH C 752 1555 1555 2.43
LINK CA CA C 604 O HOH C 783 1555 1555 2.46
LINK CA CA C 605 O HOH C 769 1555 1555 2.39
CISPEP 1 GLU A 97 PRO A 98 0 -9.00
CISPEP 2 THR A 125 PRO A 126 0 2.42
CISPEP 3 ASN A 239 PRO A 240 0 9.91
CISPEP 4 GLU C 97 PRO C 98 0 -6.89
CISPEP 5 THR C 125 PRO C 126 0 -5.50
CISPEP 6 ASN C 239 PRO C 240 0 -1.18
SITE 1 AC1 12 THR A 31 PHE A 32 LEU A 44 GLN A 48
SITE 2 AC1 12 GLU A 53 GLY A 54 THR A 55 MET A 58
SITE 3 AC1 12 VAL A 128 ASN A 155 ASP A 304 CL A 601
SITE 1 AC2 4 PRO A 89 ASN A 239 TRP A 305 PUJ A 600
SITE 1 AC3 6 ASP A 398 ASP A 400 ASN A 402 THR A 404
SITE 2 AC3 6 GLU A 409 HOH A 784
SITE 1 AC4 6 ASP A 435 ASP A 437 ASN A 439 TYR A 441
SITE 2 AC4 6 GLU A 446 HOH A 802
SITE 1 AC5 6 ASP A 471 ASP A 473 ASP A 475 GLN A 477
SITE 2 AC5 6 GLU A 482 HOH A 788
SITE 1 AC6 6 ASP A 362 ASP A 364 ASP A 366 THR A 368
SITE 2 AC6 6 GLU A 373 HOH A 766
SITE 1 AC7 12 THR C 31 LEU C 44 GLN C 48 GLU C 53
SITE 2 AC7 12 THR C 55 PRO C 57 MET C 58 VAL C 128
SITE 3 AC7 12 ASN C 155 ASN C 239 ASP C 304 CL C 601
SITE 1 AC8 4 PRO C 89 ASN C 239 TRP C 305 PUJ C 600
SITE 1 AC9 6 ASP C 362 ASP C 364 ASP C 366 THR C 368
SITE 2 AC9 6 GLU C 373 HOH C 741
SITE 1 AD1 6 ASP C 398 ASP C 400 ASN C 402 THR C 404
SITE 2 AD1 6 GLU C 409 HOH C 752
SITE 1 AD2 6 ASP C 435 ASP C 437 ASN C 439 TYR C 441
SITE 2 AD2 6 GLU C 446 HOH C 783
SITE 1 AD3 6 ASP C 471 ASP C 473 ASP C 475 GLN C 477
SITE 2 AD3 6 GLU C 482 HOH C 769
CRYST1 92.560 60.662 122.600 90.00 91.02 90.00 P 1 2 1 4
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 0.010804 0.000000 0.000192 0.00000
SCALE2 0.000000 0.016485 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008158 0.00000
TER 3711 ALA A 489
TER 7422 ALA C 489
MASTER 992 0 12 50 24 0 24 6 7733 2 172 78
END |