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HEADER HYDROLASE 31-AUG-12 4GW3
TITLE CRYSTAL STRUCTURE OF THE LIPASE FROM PROTEUS MIRABILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROTEUS MIRABILIS;
SOURCE 3 ORGANISM_TAXID: 584;
SOURCE 4 STRAIN: HAUSER D1;
SOURCE 5 GENE: LIPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21GOLD(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.KORMAN
REVDAT 1 06-FEB-13 4GW3 0
JRNL AUTH T.P.KORMAN,J.U.BOWIE
JRNL TITL CRYSTAL STRUCTURE OF PROTEUS MIRABILIS LIPASE, A NOVEL
JRNL TITL 2 LIPASE FROM THE PROTEUS/PSYCHROPHILIC SUBFAMILY OF LIPASE
JRNL TITL 3 FAMILY I.1.
JRNL REF PLOS ONE V. 7 52890 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 23300806
JRNL DOI 10.1371/JOURNAL.PONE.0052890
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 19181
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1042
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) : 1385
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2211
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.02000
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): 0.175
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.308
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2293 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2175 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3095 ; 0.871 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4992 ; 0.697 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 4.853 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 109 ;36.321 ;24.862
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 366 ;11.771 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;10.787 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 340 ; 0.052 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2622 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 541 ; 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 2 A 33
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4820 14.0690 -0.6040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0278 T22: 0.0712
REMARK 3 T33: 0.1151 T12: -0.0240
REMARK 3 T13: -0.0154 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.1533 L22: 0.8819
REMARK 3 L33: 2.0531 L12: -0.0440
REMARK 3 L13: -0.0782 L23: 0.0426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: -0.0506 S13: 0.0957
REMARK 3 S21: -0.0316 S22: -0.0564 S23: 0.2088
REMARK 3 S31: 0.0346 S32: -0.1978 S33: 0.1117
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 34 A 53
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5100 9.3050 -3.4510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0563 T22: 0.0870
REMARK 3 T33: 0.0618 T12: -0.0472
REMARK 3 T13: 0.0018 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 3.7988 L22: 3.1883
REMARK 3 L33: 2.2931 L12: -1.4657
REMARK 3 L13: 1.7747 L23: -1.2020
REMARK 3 S TENSOR
REMARK 3 S11: -0.1917 S12: -0.0626 S13: -0.0573
REMARK 3 S21: 0.0638 S22: 0.1217 S23: 0.1087
REMARK 3 S31: 0.0300 S32: -0.1139 S33: 0.0701
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 54 A 71
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9330 5.7800 -14.1700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0464 T22: 0.0925
REMARK 3 T33: 0.0398 T12: -0.0261
REMARK 3 T13: 0.0187 T23: -0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 8.6386 L22: 4.1196
REMARK 3 L33: 5.9301 L12: -2.3676
REMARK 3 L13: 5.6704 L23: -1.3097
REMARK 3 S TENSOR
REMARK 3 S11: 0.1813 S12: 0.2842 S13: -0.0643
REMARK 3 S21: -0.2287 S22: -0.2228 S23: -0.0122
REMARK 3 S31: 0.1952 S32: 0.0967 S33: 0.0415
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 72 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8560 12.2970 -4.4940
REMARK 3 T TENSOR
REMARK 3 T11: 0.0731 T22: 0.0801
REMARK 3 T33: 0.0877 T12: -0.0132
REMARK 3 T13: 0.0040 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.1087 L22: 0.6821
REMARK 3 L33: 1.2839 L12: -0.0629
REMARK 3 L13: 0.9095 L23: -0.4563
REMARK 3 S TENSOR
REMARK 3 S11: -0.0324 S12: 0.0779 S13: 0.0483
REMARK 3 S21: 0.0091 S22: 0.0516 S23: 0.0128
REMARK 3 S31: -0.0271 S32: 0.0220 S33: -0.0192
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 115 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1500 2.6560 16.0720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1093 T22: 0.0988
REMARK 3 T33: 0.0802 T12: -0.0127
REMARK 3 T13: -0.0375 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 13.5476 L22: 13.8851
REMARK 3 L33: 20.2107 L12: -0.0423
REMARK 3 L13: -3.2921 L23: 0.4654
REMARK 3 S TENSOR
REMARK 3 S11: 0.4429 S12: 0.7931 S13: -0.8349
REMARK 3 S21: 0.2632 S22: -0.5687 S23: 0.2082
REMARK 3 S31: 0.7464 S32: -0.4289 S33: 0.1257
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 120 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2510 6.9030 22.1270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1257 T22: 0.0955
REMARK 3 T33: 0.0089 T12: -0.0758
REMARK 3 T13: -0.0173 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 13.0914 L22: 3.2907
REMARK 3 L33: 1.8776 L12: -4.0956
REMARK 3 L13: 0.5752 L23: -0.0369
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: -0.3379 S13: -0.0393
REMARK 3 S21: 0.3870 S22: -0.0373 S23: -0.0825
REMARK 3 S31: 0.1610 S32: -0.1134 S33: 0.0256
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 143 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3360 3.2540 17.7360
REMARK 3 T TENSOR
REMARK 3 T11: 0.7567 T22: 0.5812
REMARK 3 T33: 0.4611 T12: -0.1861
REMARK 3 T13: -0.0581 T23: 0.1190
REMARK 3 L TENSOR
REMARK 3 L11: 0.0917 L22: 2.4610
REMARK 3 L33: 16.3859 L12: -0.4302
REMARK 3 L13: 1.1429 L23: -5.0638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: -0.1330 S13: -0.0579
REMARK 3 S21: 0.5410 S22: 0.4281 S23: 0.1089
REMARK 3 S31: 0.7133 S32: -1.1539 S33: -0.4302
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 155 A 169
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2600 5.3670 3.1020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0791 T22: 0.0464
REMARK 3 T33: 0.0762 T12: 0.0141
REMARK 3 T13: -0.0144 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 8.1135 L22: 1.7032
REMARK 3 L33: 7.6481 L12: 2.7704
REMARK 3 L13: -4.2912 L23: -2.1423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0377 S12: -0.2373 S13: -0.4131
REMARK 3 S21: -0.0880 S22: -0.0504 S23: -0.1442
REMARK 3 S31: 0.3085 S32: 0.2858 S33: 0.0881
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 170 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1840 12.0980 -8.0720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1015 T22: 0.1149
REMARK 3 T33: 0.1398 T12: -0.0388
REMARK 3 T13: 0.0996 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 7.1012 L22: 2.4862
REMARK 3 L33: 4.7632 L12: -3.5098
REMARK 3 L13: -0.8620 L23: 1.7555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: 0.1534 S13: -0.0898
REMARK 3 S21: -0.1914 S22: 0.0174 S23: -0.1779
REMARK 3 S31: -0.0167 S32: 0.2075 S33: -0.0140
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 179 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6950 21.0190 -10.8860
REMARK 3 T TENSOR
REMARK 3 T11: 0.0826 T22: 0.0853
REMARK 3 T33: 0.0886 T12: -0.0242
REMARK 3 T13: 0.0332 T23: 0.0518
REMARK 3 L TENSOR
REMARK 3 L11: 9.8030 L22: 5.9705
REMARK 3 L33: 13.5534 L12: 2.0012
REMARK 3 L13: 7.5242 L23: 3.9368
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: 0.1374 S13: 0.1270
REMARK 3 S21: -0.0681 S22: 0.1159 S23: -0.3265
REMARK 3 S31: -0.1403 S32: 0.2165 S33: -0.1088
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 193 A 202
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7510 24.0210 2.5690
REMARK 3 T TENSOR
REMARK 3 T11: 0.1311 T22: 0.1011
REMARK 3 T33: 0.2883 T12: 0.0110
REMARK 3 T13: 0.0259 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.4736 L22: 1.7041
REMARK 3 L33: 5.2040 L12: 0.6051
REMARK 3 L13: 0.3239 L23: 2.4754
REMARK 3 S TENSOR
REMARK 3 S11: 0.1131 S12: 0.0940 S13: 0.2589
REMARK 3 S21: 0.0637 S22: 0.1074 S23: 0.0859
REMARK 3 S31: -0.0650 S32: -0.1617 S33: -0.2205
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 203 A 215
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5840 24.8550 19.8530
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.2630
REMARK 3 T33: 0.0829 T12: 0.0537
REMARK 3 T13: 0.0267 T23: -0.0918
REMARK 3 L TENSOR
REMARK 3 L11: 4.2504 L22: 15.0895
REMARK 3 L33: 2.2627 L12: 6.0968
REMARK 3 L13: 1.6767 L23: 2.6461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0337 S12: -0.7316 S13: 0.3427
REMARK 3 S21: 0.6408 S22: -0.2732 S23: 0.5073
REMARK 3 S31: -0.1821 S32: -0.3649 S33: 0.2394
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 216 A 230
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3260 18.8740 16.6280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0795 T22: 0.1182
REMARK 3 T33: 0.0346 T12: -0.0436
REMARK 3 T13: -0.0256 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 5.5807 L22: 2.4122
REMARK 3 L33: 2.8189 L12: -0.6957
REMARK 3 L13: -3.2040 L23: 0.1185
REMARK 3 S TENSOR
REMARK 3 S11: -0.0785 S12: -0.1662 S13: -0.0831
REMARK 3 S21: 0.1052 S22: 0.0200 S23: -0.1426
REMARK 3 S31: 0.2520 S32: -0.1030 S33: 0.0585
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 231 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9780 23.3250 5.8650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0671 T22: 0.0565
REMARK 3 T33: 0.1214 T12: -0.0043
REMARK 3 T13: -0.0103 T23: -0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 1.5141 L22: 0.6534
REMARK 3 L33: 1.2182 L12: 0.0698
REMARK 3 L13: 0.2134 L23: 0.4393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0160 S12: -0.1288 S13: 0.2735
REMARK 3 S21: 0.0158 S22: -0.0777 S23: 0.0612
REMARK 3 S31: -0.1356 S32: -0.0259 S33: 0.0938
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 277 A 287
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8630 26.9240 -11.8490
REMARK 3 T TENSOR
REMARK 3 T11: 0.1001 T22: 0.0540
REMARK 3 T33: 0.1984 T12: -0.0358
REMARK 3 T13: -0.0545 T23: 0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 6.5361 L22: 5.7733
REMARK 3 L33: 19.5217 L12: 0.2800
REMARK 3 L13: 2.0340 L23: 3.0802
REMARK 3 S TENSOR
REMARK 3 S11: -0.1881 S12: 0.2590 S13: 0.8724
REMARK 3 S21: -0.2664 S22: 0.3863 S23: -0.0730
REMARK 3 S31: -0.7014 S32: 0.1879 S33: -0.1982
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 4GW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074705.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.502
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX CONFOCAL OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20166
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.1000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
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 (%): 47.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.095 M SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE PH 5.6, 19% V/V 2-PROPANOL, 19% W/V PEG 4000, 5%
REMARK 280 GLYCEROL, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.64400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 21.32200
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 465 MET A 1
REMARK 465 ARG A 147
REMARK 465 GLY A 148
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 LEU A 13 76.57 94.49
REMARK 500 PHE A 47 55.62 -92.69
REMARK 500 GLN A 69 16.83 59.28
REMARK 500 SER A 79 -120.05 58.45
REMARK 500 LYS A 208 -117.95 51.78
REMARK 500 ILE A 246 -60.58 -96.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 406
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 HOH A 537 O 90.4
REMARK 620 3 ASP A 213 OD2 171.7 82.6
REMARK 620 4 LEU A 264 O 97.6 169.5 88.8
REMARK 620 5 GLN A 260 O 94.4 108.9 92.1 77.3
REMARK 620 6 ASN A 210 OD1 81.7 96.1 94.6 78.6 154.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 666 O
REMARK 620 2 GLU A 51 OE1 122.8
REMARK 620 3 HOH A 659 O 105.0 84.0
REMARK 620 4 ASN A 50 OD1 91.9 114.5 142.8
REMARK 620 N 1 2 3
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 CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GXN RELATED DB: PDB
DBREF 4GW3 A 1 287 UNP B4EVM3 B4EVM3_PROMH 1 287
SEQADV 4GW3 MET A -19 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 GLY A -18 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 SER A -17 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 SER A -16 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 HIS A -15 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 HIS A -14 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 HIS A -13 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 HIS A -12 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 HIS A -11 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 HIS A -10 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 SER A -9 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 SER A -8 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 GLY A -7 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 LEU A -6 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 VAL A -5 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 PRO A -4 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 ARG A -3 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 GLY A -2 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 SER A -1 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GW3 HIS A 0 UNP B4EVM3 EXPRESSION TAG
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 ASN GLU ILE
SEQRES 4 A 307 VAL GLY PHE PRO TYR PHE TYR GLY ILE ALA ASP ALA LEU
SEQRES 5 A 307 ARG 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 LEU LEU GLN GLU THR GLN ALA 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 MET 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 GLY 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 GLY LEU ILE ALA GLY GLU LYS GLY ASN LEU LEU ASP PRO
SEQRES 19 A 307 THR HIS ALA ALA MET ARG VAL LEU ASN THR PHE PHE THR
SEQRES 20 A 307 GLU LYS GLN ASN ASP GLY LEU VAL GLY ARG SER SER MET
SEQRES 21 A 307 ARG LEU GLY LYS LEU ILE LYS ASP ASP TYR ALA GLN ASP
SEQRES 22 A 307 HIS ILE ASP MET VAL ASN GLN VAL ALA GLY LEU VAL GLY
SEQRES 23 A 307 TYR ASN GLU ASP ILE VAL ALA ILE TYR THR GLN HIS ALA
SEQRES 24 A 307 LYS TYR LEU ALA SER LYS GLN LEU
HET CA A 401 1
HET CA A 402 1
HET IPA A 403 4
HET GOL A 404 6
HET 1PE A 405 16
HET 1PE A 406 13
HETNAM CA CALCIUM ION
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM GOL GLYCEROL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN IPA 2-PROPANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN 1PE PEG400
FORMUL 2 CA 2(CA 2+)
FORMUL 4 IPA C3 H8 O
FORMUL 5 GOL C3 H8 O3
FORMUL 6 1PE 2(C10 H22 O6)
FORMUL 8 HOH *192(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 LEU A 203 LEU A 212 5 10
HELIX 11 11 ASP A 213 THR A 224 1 12
HELIX 12 12 ARG A 237 ARG A 241 5 5
HELIX 13 13 ILE A 255 ASN A 259 5 5
HELIX 14 14 ASP A 270 LYS A 285 1 16
SHEET 1 A 6 VAL A 39 LEU A 44 0
SHEET 2 A 6 ILE A 7 GLY A 12 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 LEU A 44 0
SHEET 2 B 6 ILE A 7 GLY A 12 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
LINK OD1 ASP A 256 CA CA A 401 1555 1555 2.25
LINK CA CA A 401 O HOH A 537 1555 1555 2.29
LINK OD2 ASP A 213 CA CA A 401 1555 1555 2.30
LINK O LEU A 264 CA CA A 401 1555 1555 2.35
LINK O GLN A 260 CA CA A 401 1555 1555 2.47
LINK OD1 ASN A 210 CA CA A 401 1555 1555 2.48
LINK CA CA A 402 O HOH A 666 1555 1555 2.59
LINK OE1 GLU A 51 CA CA A 402 1555 1555 2.71
LINK CA CA A 402 O HOH A 659 1555 1555 2.78
LINK OD1 ASN A 50 CA CA A 402 1555 1555 3.14
CISPEP 1 GLN A 260 VAL A 261 0 0.33
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 537
SITE 1 AC2 4 ASN A 50 GLU A 51 HOH A 659 HOH A 666
SITE 1 AC3 4 LEU A 13 SER A 79 GLN A 80 HOH A 503
SITE 1 AC4 8 GLU A 167 ASN A 170 ILE A 200 GLN A 201
SITE 2 AC4 8 GLY A 202 ARG A 220 ASN A 223 HOH A 558
SITE 1 AC5 5 ILE A 19 PHE A 60 THR A 63 GLU A 67
SITE 2 AC5 5 1PE A 406
SITE 1 AC6 2 ALA A 153 1PE A 405
CRYST1 65.438 65.438 63.966 90.00 90.00 120.00 P 32 3
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 0.015282 0.008823 0.000000 0.00000
SCALE2 0.000000 0.017646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015633 0.00000
TER 2212 LEU A 287
MASTER 609 0 6 14 12 0 9 6 2444 1 52 24
END |