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HEADER HYDROLASE 29-OCT-12 4HS9
TITLE METHANOL TOLERANT MUTANT OF THE PROTEUS MIRABILIS LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROTEUS MIRABILIS;
SOURCE 3 ORGANISM_TAXID: 584;
SOURCE 4 STRAIN: ATCC;
SOURCE 5 GENE: LIPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21GOLD(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS LIPASE, HYDROLASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.KORMAN
REVDAT 1 22-MAY-13 4HS9 0
JRNL AUTH T.P.KORMAN,B.SAHACHARTSIRI,D.M.CHARBONNEAU,G.L.HUANG,
JRNL AUTH 2 M.BEAUREGARD,J.U.BOWIE
JRNL TITL DIESELZYMES: DEVELOPMENT OF A STABLE AND METHANOL TOLERANT
JRNL TITL 2 LIPASE FOR BIODIESEL PRODUCTION BY DIRECTED EVOLUTION.
JRNL REF BIOTECHNOL BIOFUELS V. 6 70 2013
JRNL REFN
JRNL PMID 23648063
JRNL DOI 10.1186/1754-6834-6-70
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 23320
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1184
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1593
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2237
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 117
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08000
REMARK 3 B22 (A**2) : 0.24000
REMARK 3 B33 (A**2) : -0.16000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.139
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.655
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2329 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2207 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3146 ; 1.976 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5071 ; 0.958 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 286 ; 6.162 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 109 ;35.103 ;24.862
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 371 ;14.603 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;12.591 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 348 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2650 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 545 ; 0.001 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 15
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 1 A 5
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4360 17.9660 -3.1560
REMARK 3 T TENSOR
REMARK 3 T11: 0.2563 T22: 0.1335
REMARK 3 T33: 0.2919 T12: -0.0334
REMARK 3 T13: 0.0637 T23: 0.1082
REMARK 3 L TENSOR
REMARK 3 L11: 8.3895 L22: 16.8663
REMARK 3 L33: 44.2230 L12: 3.2627
REMARK 3 L13: 3.0456 L23: 12.6985
REMARK 3 S TENSOR
REMARK 3 S11: 0.2021 S12: 0.3460 S13: 0.4655
REMARK 3 S21: -0.4967 S22: 0.2968 S23: -0.3353
REMARK 3 S31: -1.9894 S32: 0.7478 S33: -0.4988
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 6 A 31
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3180 5.8540 9.5860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1818 T22: 0.0882
REMARK 3 T33: 0.2420 T12: 0.0386
REMARK 3 T13: 0.0096 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 3.3523 L22: 1.0163
REMARK 3 L33: 4.2805 L12: 0.7297
REMARK 3 L13: -2.1344 L23: -0.0679
REMARK 3 S TENSOR
REMARK 3 S11: 0.0598 S12: 0.1657 S13: 0.0565
REMARK 3 S21: 0.1386 S22: -0.0192 S23: 0.1601
REMARK 3 S31: -0.1399 S32: -0.3744 S33: -0.0406
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 38
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5430 18.5030 5.3840
REMARK 3 T TENSOR
REMARK 3 T11: 0.2757 T22: 0.0439
REMARK 3 T33: 0.4187 T12: 0.0464
REMARK 3 T13: 0.0535 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 7.2271 L22: 15.2747
REMARK 3 L33: 19.9125 L12: 0.6717
REMARK 3 L13: -1.0037 L23: 0.0220
REMARK 3 S TENSOR
REMARK 3 S11: 0.0840 S12: 0.4364 S13: 1.1780
REMARK 3 S21: 0.3267 S22: -0.2176 S23: 0.7610
REMARK 3 S31: -0.7650 S32: -0.4856 S33: 0.1336
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 39 A 60
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6580 -1.7630 -1.7600
REMARK 3 T TENSOR
REMARK 3 T11: 0.2079 T22: 0.1733
REMARK 3 T33: 0.2258 T12: -0.0357
REMARK 3 T13: -0.0088 T23: -0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 2.7765 L22: 3.6146
REMARK 3 L33: 3.3114 L12: 0.1415
REMARK 3 L13: -0.8218 L23: -1.8164
REMARK 3 S TENSOR
REMARK 3 S11: -0.1335 S12: 0.5036 S13: -0.2315
REMARK 3 S21: -0.3774 S22: 0.0388 S23: 0.1495
REMARK 3 S31: 0.4057 S32: -0.4984 S33: 0.0946
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 61 A 71
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2430 11.7440 -10.3500
REMARK 3 T TENSOR
REMARK 3 T11: 0.2667 T22: 0.2752
REMARK 3 T33: 0.1592 T12: 0.0808
REMARK 3 T13: 0.0214 T23: 0.1033
REMARK 3 L TENSOR
REMARK 3 L11: 11.4987 L22: 11.1598
REMARK 3 L33: 3.3270 L12: -1.2083
REMARK 3 L13: 1.5518 L23: -3.6835
REMARK 3 S TENSOR
REMARK 3 S11: 0.2185 S12: 0.9703 S13: 0.3211
REMARK 3 S21: -0.1247 S22: -0.0273 S23: 0.0245
REMARK 3 S31: 0.0181 S32: 0.1526 S33: -0.1911
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 72 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5450 0.5530 -1.2840
REMARK 3 T TENSOR
REMARK 3 T11: 0.1951 T22: 0.1152
REMARK 3 T33: 0.2382 T12: 0.0177
REMARK 3 T13: 0.0383 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 2.1721 L22: 2.2500
REMARK 3 L33: 4.4486 L12: 0.3961
REMARK 3 L13: -0.6541 L23: -1.1657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0551 S12: 0.3024 S13: -0.2200
REMARK 3 S21: -0.2102 S22: -0.0578 S23: -0.0742
REMARK 3 S31: 0.2503 S32: 0.0589 S33: 0.1129
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 108 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8450 -18.8110 13.0430
REMARK 3 T TENSOR
REMARK 3 T11: 0.3768 T22: 0.0231
REMARK 3 T33: 0.3739 T12: 0.0676
REMARK 3 T13: 0.0711 T23: 0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 5.9522 L22: 10.7850
REMARK 3 L33: 4.3266 L12: 7.8233
REMARK 3 L13: -0.8568 L23: -1.8902
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: -0.0574 S13: -0.2734
REMARK 3 S21: -0.0744 S22: -0.0814 S23: -0.2515
REMARK 3 S31: 0.5224 S32: -0.0303 S33: 0.0975
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 120 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7510 -25.9670 18.9960
REMARK 3 T TENSOR
REMARK 3 T11: 0.3909 T22: 0.0335
REMARK 3 T33: 0.4215 T12: 0.0333
REMARK 3 T13: 0.1231 T23: 0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 10.5511 L22: 16.5445
REMARK 3 L33: 56.7328 L12: 6.8298
REMARK 3 L13: 11.2389 L23: 20.1381
REMARK 3 S TENSOR
REMARK 3 S11: 0.0352 S12: 0.1625 S13: -0.7190
REMARK 3 S21: -0.2142 S22: 0.6620 S23: 0.0651
REMARK 3 S31: 1.2399 S32: 0.8924 S33: -0.6972
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 128 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8900 -11.4380 21.8800
REMARK 3 T TENSOR
REMARK 3 T11: 0.2963 T22: 0.0182
REMARK 3 T33: 0.2902 T12: -0.0302
REMARK 3 T13: 0.0571 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 8.6386 L22: 17.8289
REMARK 3 L33: 3.9583 L12: -9.1771
REMARK 3 L13: 1.0966 L23: -4.7766
REMARK 3 S TENSOR
REMARK 3 S11: 0.1835 S12: -0.0073 S13: 0.0190
REMARK 3 S21: -0.2292 S22: -0.1171 S23: 0.3099
REMARK 3 S31: -0.1001 S32: -0.0756 S33: -0.0664
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 149 A 174
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2760 -13.4440 2.2650
REMARK 3 T TENSOR
REMARK 3 T11: 0.4996 T22: 0.1542
REMARK 3 T33: 0.5737 T12: 0.0492
REMARK 3 T13: 0.0651 T23: -0.2042
REMARK 3 L TENSOR
REMARK 3 L11: 4.6252 L22: 4.3767
REMARK 3 L33: 7.9150 L12: 0.5599
REMARK 3 L13: -4.8634 L23: -3.1017
REMARK 3 S TENSOR
REMARK 3 S11: -0.3897 S12: 0.6012 S13: -0.9834
REMARK 3 S21: -0.4151 S22: -0.0056 S23: 0.1087
REMARK 3 S31: 1.0881 S32: -0.3159 S33: 0.3954
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 : A 175 A 198
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5960 -0.6050 0.7010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1858 T22: 0.3559
REMARK 3 T33: 0.3831 T12: 0.0952
REMARK 3 T13: 0.0766 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.4521 L22: 2.2831
REMARK 3 L33: 7.9039 L12: 0.9360
REMARK 3 L13: -0.3250 L23: -0.7073
REMARK 3 S TENSOR
REMARK 3 S11: -0.0592 S12: 0.0312 S13: -0.3160
REMARK 3 S21: -0.1356 S22: -0.1173 S23: -0.5524
REMARK 3 S31: 0.3558 S32: 1.2300 S33: 0.1765
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 : A 199 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8350 0.7360 26.7320
REMARK 3 T TENSOR
REMARK 3 T11: 0.3424 T22: 0.2510
REMARK 3 T33: 0.2651 T12: -0.0835
REMARK 3 T13: -0.0571 T23: 0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 6.9381 L22: 2.9925
REMARK 3 L33: 7.8700 L12: -0.2675
REMARK 3 L13: -4.5979 L23: 0.1036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0514 S12: -1.2380 S13: -0.0748
REMARK 3 S21: 0.5422 S22: -0.1658 S23: -0.2820
REMARK 3 S31: -0.4377 S32: 1.0067 S33: 0.1144
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 : A 214 A 220
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9980 -4.4590 25.0730
REMARK 3 T TENSOR
REMARK 3 T11: 0.3383 T22: 0.1313
REMARK 3 T33: 0.3151 T12: -0.0563
REMARK 3 T13: 0.0425 T23: 0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 28.6598 L22: 25.2049
REMARK 3 L33: 0.8729 L12: -17.1280
REMARK 3 L13: -3.6990 L23: -0.2168
REMARK 3 S TENSOR
REMARK 3 S11: -0.0621 S12: -0.8071 S13: 0.1574
REMARK 3 S21: 1.0358 S22: 0.0431 S23: -0.1692
REMARK 3 S31: -0.1431 S32: 0.1806 S33: 0.0189
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 : A 221 A 254
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7420 -4.7790 14.8010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1803 T22: 0.1437
REMARK 3 T33: 0.3276 T12: 0.0567
REMARK 3 T13: 0.0044 T23: 0.1055
REMARK 3 L TENSOR
REMARK 3 L11: 1.4688 L22: 2.1410
REMARK 3 L33: 3.4283 L12: 0.5126
REMARK 3 L13: -1.1462 L23: -0.6259
REMARK 3 S TENSOR
REMARK 3 S11: -0.0274 S12: -0.1289 S13: -0.3048
REMARK 3 S21: 0.1354 S22: -0.2095 S23: -0.2607
REMARK 3 S31: 0.2311 S32: 0.5357 S33: 0.2369
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 : A 255 A 287
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7890 9.6650 12.8080
REMARK 3 T TENSOR
REMARK 3 T11: 0.2342 T22: 0.0838
REMARK 3 T33: 0.2236 T12: -0.0487
REMARK 3 T13: -0.0014 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 2.8673 L22: 2.5972
REMARK 3 L33: 5.7111 L12: 2.1882
REMARK 3 L13: -3.1054 L23: -3.7111
REMARK 3 S TENSOR
REMARK 3 S11: 0.1563 S12: -0.1558 S13: 0.0029
REMARK 3 S21: 0.2271 S22: -0.2375 S23: -0.1035
REMARK 3 S31: -0.3583 S32: 0.4060 S33: 0.0813
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: RESIDUAL ONLY
REMARK 4
REMARK 4 4HS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB075856.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23372
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 90.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1X MMT BUFFER PH 5.0, 20% PEG1500,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 24.04950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.00650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.42450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.00650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.04950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.42450
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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 CYS A 181 CA - CB - SG ANGL. DEV. = -11.4 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 71 -55.94 74.39
REMARK 500 SER A 79 -115.70 57.65
REMARK 500 PRO A 180 127.05 -32.37
REMARK 500 LEU A 203 -169.51 -112.48
REMARK 500 ASN A 208 -115.00 53.90
REMARK 500 ILE A 246 -69.36 -94.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 91 24.8 L L OUTSIDE RANGE
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 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 256 OD1
REMARK 620 2 LEU A 264 O 95.6
REMARK 620 3 ASP A 213 OD2 169.1 94.9
REMARK 620 4 ASN A 210 OD1 88.2 83.0 90.4
REMARK 620 5 HOH A 508 O 90.4 173.9 79.0 97.2
REMARK 620 6 GLN A 260 O 95.8 80.8 88.6 163.6 98.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GW3 RELATED DB: PDB
REMARK 900 WILD-TYPE PROTEUS MIRABILIS LIPASE
REMARK 900 RELATED ID: 4GXN RELATED DB: PDB
REMARK 900 DEP INHIBITED PROTEUS MIRABILIS LIPASE
DBREF 4HS9 A 1 287 UNP B4EVM3 B4EVM3_PROMH 1 287
SEQADV 4HS9 MET A -19 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 GLY A -18 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 SER A -17 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 SER A -16 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 HIS A -15 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 HIS A -14 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 HIS A -13 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 HIS A -12 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 HIS A -11 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 HIS A -10 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 SER A -9 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 SER A -8 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 GLY A -7 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 LEU A -6 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 VAL A -5 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 PRO A -4 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 ARG A -3 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 GLY A -2 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 SER A -1 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 HIS A 0 UNP B4EVM3 EXPRESSION TAG
SEQADV 4HS9 SER A 17 UNP B4EVM3 ASN 17 ENGINEERED MUTATION
SEQADV 4HS9 THR A 33 UNP B4EVM3 ARG 33 ENGINEERED MUTATION
SEQADV 4HS9 ILE A 64 UNP B4EVM3 LEU 64 ENGINEERED MUTATION
SEQADV 4HS9 THR A 70 UNP B4EVM3 ALA 70 ENGINEERED MUTATION
SEQADV 4HS9 ILE A 119 UNP B4EVM3 MET 119 ENGINEERED MUTATION
SEQADV 4HS9 CYS A 181 UNP B4EVM3 GLY 181 ENGINEERED MUTATION
SEQADV 4HS9 GLU A 202 UNP B4EVM3 GLY 202 ENGINEERED MUTATION
SEQADV 4HS9 ASN A 208 UNP B4EVM3 LYS 208 ENGINEERED MUTATION
SEQADV 4HS9 LEU A 225 UNP B4EVM3 PHE 225 ENGINEERED MUTATION
SEQADV 4HS9 CYS A 238 UNP B4EVM3 SER 238 ENGINEERED MUTATION
SEQADV 4HS9 PHE A 255 UNP B4EVM3 ILE 255 ENGINEERED MUTATION
SEQADV 4HS9 SER A 266 UNP B4EVM3 GLY 266 ENGINEERED MUTATION
SEQADV 4HS9 ASN A 270 UNP B4EVM3 ASP 270 ENGINEERED MUTATION
SEQADV 4HS9 LEU A 277 UNP B4EVM3 GLN 277 ENGINEERED MUTATION
SEQRES 1 A 307 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 307 LEU VAL PRO ARG GLY SER HIS MET SER THR LYS TYR PRO
SEQRES 3 A 307 ILE VAL LEU VAL HIS GLY LEU ALA GLY PHE SER GLU ILE
SEQRES 4 A 307 VAL GLY PHE PRO TYR PHE TYR GLY ILE ALA ASP ALA LEU
SEQRES 5 A 307 THR GLN ASP GLY HIS GLN VAL PHE THR ALA SER LEU SER
SEQRES 6 A 307 ALA PHE ASN SER ASN GLU VAL ARG GLY LYS GLN LEU TRP
SEQRES 7 A 307 GLN PHE VAL GLN THR ILE LEU GLN GLU THR GLN THR LYS
SEQRES 8 A 307 LYS VAL ASN PHE ILE GLY HIS SER GLN GLY PRO LEU ALA
SEQRES 9 A 307 CYS ARG TYR VAL ALA ALA ASN TYR PRO ASP SER VAL ALA
SEQRES 10 A 307 SER VAL THR SER ILE ASN GLY VAL ASN HIS GLY SER GLU
SEQRES 11 A 307 ILE ALA ASP LEU TYR ARG ARG ILE ILE ARG LYS ASP SER
SEQRES 12 A 307 ILE PRO GLU TYR ILE VAL GLU LYS VAL LEU ASN ALA PHE
SEQRES 13 A 307 GLY THR ILE ILE SER THR PHE SER GLY HIS ARG GLY ASP
SEQRES 14 A 307 PRO GLN ASP ALA ILE ALA ALA LEU GLU SER LEU THR THR
SEQRES 15 A 307 GLU GLN VAL THR GLU PHE ASN ASN LYS TYR PRO GLN ALA
SEQRES 16 A 307 LEU PRO LYS THR PRO CYS GLY GLU GLY ASP GLU ILE VAL
SEQRES 17 A 307 ASN GLY VAL HIS TYR TYR CYS PHE GLY SER TYR ILE GLN
SEQRES 18 A 307 GLU LEU ILE ALA GLY GLU ASN GLY ASN LEU LEU ASP PRO
SEQRES 19 A 307 THR HIS ALA ALA MET ARG VAL LEU ASN THR LEU PHE THR
SEQRES 20 A 307 GLU LYS GLN ASN ASP GLY LEU VAL GLY ARG CYS SER MET
SEQRES 21 A 307 ARG LEU GLY LYS LEU ILE LYS ASP ASP TYR ALA GLN ASP
SEQRES 22 A 307 HIS PHE ASP MET VAL ASN GLN VAL ALA GLY LEU VAL SER
SEQRES 23 A 307 TYR ASN GLU ASN ILE VAL ALA ILE TYR THR LEU HIS ALA
SEQRES 24 A 307 LYS TYR LEU ALA SER LYS GLN LEU
HET CA A 401 1
HET CL A 402 1
HET GOL A 403 6
HET 1PE A 404 16
HET PE4 A 405 24
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN 1PE PEG400
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 2 CA CA 2+
FORMUL 3 CL CL 1-
FORMUL 4 GOL C3 H8 O3
FORMUL 5 1PE C10 H22 O6
FORMUL 6 PE4 C16 H34 O8
FORMUL 7 HOH *117(H2 O)
HELIX 1 1 GLY A 15 GLY A 21 1 7
HELIX 2 2 GLY A 27 ASP A 35 1 9
HELIX 3 3 SER A 49 GLN A 69 1 21
HELIX 4 4 GLN A 80 TYR A 92 1 13
HELIX 5 5 SER A 109 ARG A 120 1 12
HELIX 6 6 PRO A 125 GLY A 145 1 21
HELIX 7 7 ASP A 149 ASP A 152 5 4
HELIX 8 8 ALA A 153 GLU A 158 1 6
HELIX 9 9 THR A 161 TYR A 172 1 12
HELIX 10 10 GLU A 207 LEU A 212 5 6
HELIX 11 11 ASP A 213 ASN A 223 1 11
HELIX 12 12 THR A 224 PHE A 226 5 3
HELIX 13 13 GLY A 236 ARG A 241 5 6
HELIX 14 14 PHE A 255 ASN A 259 5 5
HELIX 15 15 VAL A 265 GLU A 269 5 5
HELIX 16 16 ASN A 270 LYS A 285 1 16
SHEET 1 A 6 VAL A 39 SER A 43 0
SHEET 2 A 6 ILE A 7 HIS A 11 1 N LEU A 9 O ALA A 42
SHEET 3 A 6 VAL A 73 HIS A 78 1 O ASN A 74 N VAL A 8
SHEET 4 A 6 VAL A 96 ILE A 102 1 O SER A 98 N PHE A 75
SHEET 5 A 6 VAL A 191 SER A 198 1 O PHE A 196 N SER A 101
SHEET 6 A 6 ILE A 187 VAL A 188 -1 N VAL A 188 O VAL A 191
SHEET 1 B 6 VAL A 39 SER A 43 0
SHEET 2 B 6 ILE A 7 HIS A 11 1 N LEU A 9 O ALA A 42
SHEET 3 B 6 VAL A 73 HIS A 78 1 O ASN A 74 N VAL A 8
SHEET 4 B 6 VAL A 96 ILE A 102 1 O SER A 98 N PHE A 75
SHEET 5 B 6 VAL A 191 SER A 198 1 O PHE A 196 N SER A 101
SHEET 6 B 6 LYS A 244 TYR A 250 1 O ILE A 246 N CYS A 195
SSBOND 1 CYS A 181 CYS A 238 1555 1555 2.04
LINK OD1 ASP A 256 CA CA A 401 1555 1555 2.19
LINK O LEU A 264 CA CA A 401 1555 1555 2.32
LINK OD2 ASP A 213 CA CA A 401 1555 1555 2.34
LINK OD1 ASN A 210 CA CA A 401 1555 1555 2.37
LINK CA CA A 401 O HOH A 508 1555 1555 2.39
LINK O GLN A 260 CA CA A 401 1555 1555 2.46
CISPEP 1 GLY A 206 GLU A 207 0 6.57
CISPEP 2 GLN A 260 VAL A 261 0 0.97
SITE 1 AC1 7 ASN A 210 ASP A 213 ASP A 256 GLN A 260
SITE 2 AC1 7 VAL A 261 LEU A 264 HOH A 508
SITE 1 AC2 4 HIS A 11 TYR A 24 GLN A 286 HOH A 551
SITE 1 AC3 2 ASN A 259 HOH A 606
SITE 1 AC4 6 ALA A 14 ILE A 19 PHE A 47 ILE A 139
SITE 2 AC4 6 PHE A 143 PE4 A 405
SITE 1 AC5 8 LEU A 13 TYR A 24 SER A 79 SER A 144
SITE 2 AC5 8 HIS A 146 ASP A 152 PHE A 255 1PE A 404
CRYST1 48.099 54.849 96.013 90.00 90.00 90.00 P 21 21 21 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 0.020790 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018232 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010415 0.00000
TER 2238 LEU A 287
MASTER 629 0 5 16 12 0 8 6 2402 1 56 24
END |