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HEADER HYDROLASE 26-JAN-11 2Y6V
TITLE PEROXISOMAL ALPHA-BETA-HYDROLASE LPX1 (YOR084W) FROM
TITLE 2 SACCHAROMYCES CEREVISIAE (CRYSTAL FORM I)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOMAL MEMBRANE PROTEIN LPX1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: LIPASE OF PEROXISOMES PROTEIN 1, LPX1-YOR084W;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: CODONPLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET21D;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PST281
KEYWDS HYDROLASE, PUTATIVE ESTERASE, PUTATIVE LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.THOMS,H.H.NIEMANN
REVDAT 1 13-JUL-11 2Y6V 0
JRNL AUTH S.THOMS,J.HOFHUIS,C.THOING,J.GARTNER,H.H.NIEMANN
JRNL TITL THE UNUSUAL EXTENDED C-TERMINAL HELIX OF THE PEROXISOMAL
JRNL TITL 2 ALPHA-BETA-HYDROLASE LPX1 IS INVOLVED IN DIMER CONTACTS BUT
JRNL TITL 3 DISPENSABLE FOR DIMERIZATION
JRNL REF J.STRUCT.BIOL. 2011
JRNL REFN ESSN 1095-8657
JRNL DOI 10.1016/J.JSB.2011.06.008
REMARK 2
REMARK 2 RESOLUTION. 2.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 33131
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) : 0.20938
REMARK 3 R VALUE (WORKING SET) : 0.20707
REMARK 3 FREE R VALUE : 0.25408
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1744
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) : 2.827
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.899
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1700
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.263
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8793
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.557
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19
REMARK 3 B22 (A**2) : -0.35
REMARK 3 B33 (A**2) : 0.20
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.24
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.378
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.283
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8995 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6131 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12184 ; 1.475 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14897 ; 0.967 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1112 ;18.628 ; 5.234
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 433 ;34.289 ;23.580
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1522 ;15.396 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;17.662 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1367 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9886 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1838 ; 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): 5478 ; 0.304 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2187 ; 0.143 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8883 ; 0.553 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3517 ; 0.913 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3301 ; 1.294 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 381 1
REMARK 3 1 A 1 A 381 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 B (A): 4836 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 A (A): 4836 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 B (A**2): 4836 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 4836 ; 0.10 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 44 1
REMARK 3 1 A 1 A 44 1
REMARK 3 2 C 52 C 77 1
REMARK 3 2 A 52 A 77 1
REMARK 3 3 C 85 C 132 1
REMARK 3 3 A 85 A 132 1
REMARK 3 4 C 134 C 173 1
REMARK 3 4 A 134 A 173 1
REMARK 3 5 C 186 C 205 1
REMARK 3 5 A 186 A 205 1
REMARK 3 6 C 209 C 344 1
REMARK 3 6 A 209 A 344 1
REMARK 3 7 C 358 C 381 1
REMARK 3 7 A 358 A 381 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 4410 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 A (A): 4410 ; 0.05 ; 0.05
REMARK 3 TIGHT THERMAL 2 C (A**2): 4410 ; 0.11 ; 0.50
REMARK 3 TIGHT THERMAL 2 A (A**2): 4410 ; 0.11 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
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 3 A 191
REMARK 3 ORIGIN FOR THE GROUP (A): 103.9396 52.3618 15.2640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0816 T22: 0.0300
REMARK 3 T33: 0.0397 T12: -0.0004
REMARK 3 T13: 0.0308 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 2.6004 L22: 1.9342
REMARK 3 L33: 2.2969 L12: -0.7972
REMARK 3 L13: 0.0227 L23: -0.1965
REMARK 3 S TENSOR
REMARK 3 S11: -0.0345 S12: 0.1166 S13: -0.1937
REMARK 3 S21: -0.0867 S22: 0.1073 S23: -0.0505
REMARK 3 S31: 0.2139 S32: 0.1512 S33: -0.0728
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 192 A 283
REMARK 3 ORIGIN FOR THE GROUP (A): 114.5842 64.7537 8.1668
REMARK 3 T TENSOR
REMARK 3 T11: 0.1653 T22: 0.2375
REMARK 3 T33: 0.2105 T12: -0.0416
REMARK 3 T13: 0.0560 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.5672 L22: 1.4218
REMARK 3 L33: 2.5571 L12: -0.5281
REMARK 3 L13: -0.8079 L23: 0.5656
REMARK 3 S TENSOR
REMARK 3 S11: 0.0537 S12: 0.3689 S13: 0.2752
REMARK 3 S21: -0.3358 S22: -0.0085 S23: -0.3664
REMARK 3 S31: -0.2697 S32: 0.3023 S33: -0.0452
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 284 A 348
REMARK 3 ORIGIN FOR THE GROUP (A): 117.1126 53.0470 27.5857
REMARK 3 T TENSOR
REMARK 3 T11: 0.1151 T22: 0.1480
REMARK 3 T33: 0.0921 T12: 0.0653
REMARK 3 T13: -0.0786 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 5.1456 L22: 2.6621
REMARK 3 L33: 3.1682 L12: 0.0445
REMARK 3 L13: -0.5190 L23: 1.8026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0915 S12: -0.2262 S13: 0.0157
REMARK 3 S21: 0.3481 S22: 0.1233 S23: -0.2951
REMARK 3 S31: 0.1572 S32: 0.4749 S33: -0.0318
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 349 A 381
REMARK 3 ORIGIN FOR THE GROUP (A): 84.8551 34.0038 38.3006
REMARK 3 T TENSOR
REMARK 3 T11: 0.4099 T22: 0.3449
REMARK 3 T33: 0.2667 T12: 0.1159
REMARK 3 T13: -0.0241 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 4.6170 L22: 5.5974
REMARK 3 L33: 0.6893 L12: -0.1119
REMARK 3 L13: 0.2915 L23: 0.9551
REMARK 3 S TENSOR
REMARK 3 S11: -0.2314 S12: 0.1902 S13: -0.2219
REMARK 3 S21: 0.2989 S22: 0.4080 S23: -0.4366
REMARK 3 S31: 0.3249 S32: 0.4093 S33: -0.1766
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 : B 3 B 191
REMARK 3 ORIGIN FOR THE GROUP (A): 77.3129 57.3052 23.9902
REMARK 3 T TENSOR
REMARK 3 T11: 0.0901 T22: 0.0654
REMARK 3 T33: 0.0525 T12: -0.0152
REMARK 3 T13: 0.0219 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 2.5514 L22: 3.1746
REMARK 3 L33: 1.4233 L12: -0.0872
REMARK 3 L13: -0.4080 L23: 0.0162
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: 0.1320 S13: 0.0924
REMARK 3 S21: -0.2554 S22: 0.0541 S23: 0.2387
REMARK 3 S31: 0.0007 S32: -0.2973 S33: -0.0070
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 : B 192 B 283
REMARK 3 ORIGIN FOR THE GROUP (A): 70.2722 48.9503 38.8368
REMARK 3 T TENSOR
REMARK 3 T11: 0.2002 T22: 0.2048
REMARK 3 T33: 0.2109 T12: -0.0450
REMARK 3 T13: 0.0612 T23: 0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 2.6444 L22: 0.8462
REMARK 3 L33: 0.7458 L12: 0.3843
REMARK 3 L13: 0.3140 L23: -0.0395
REMARK 3 S TENSOR
REMARK 3 S11: 0.0445 S12: -0.3630 S13: -0.3087
REMARK 3 S21: 0.2145 S22: 0.0326 S23: 0.2674
REMARK 3 S31: 0.1870 S32: -0.3505 S33: -0.0771
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 : B 284 B 348
REMARK 3 ORIGIN FOR THE GROUP (A): 75.2475 70.9643 35.4114
REMARK 3 T TENSOR
REMARK 3 T11: 0.1524 T22: 0.0562
REMARK 3 T33: 0.1291 T12: 0.0484
REMARK 3 T13: 0.0435 T23: -0.0514
REMARK 3 L TENSOR
REMARK 3 L11: 6.1478 L22: 2.6741
REMARK 3 L33: 4.0829 L12: 0.5026
REMARK 3 L13: 0.3251 L23: 0.0154
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: -0.3132 S13: 0.3399
REMARK 3 S21: 0.2433 S22: -0.0036 S23: 0.2909
REMARK 3 S31: -0.2932 S32: -0.0953 S33: -0.0063
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 : B 349 B 381
REMARK 3 ORIGIN FOR THE GROUP (A): 97.1969 76.6211 4.1669
REMARK 3 T TENSOR
REMARK 3 T11: 0.3731 T22: 0.1824
REMARK 3 T33: 0.4476 T12: -0.0510
REMARK 3 T13: -0.0174 T23: 0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 2.3130 L22: 2.1213
REMARK 3 L33: 4.9918 L12: -1.9909
REMARK 3 L13: 0.3421 L23: 0.2432
REMARK 3 S TENSOR
REMARK 3 S11: -0.2101 S12: 0.1674 S13: 0.1949
REMARK 3 S21: 0.0116 S22: -0.1483 S23: 0.2022
REMARK 3 S31: -0.2539 S32: -0.6032 S33: 0.3584
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 : C 3 C 174
REMARK 3 ORIGIN FOR THE GROUP (A): 74.8513 100.6383 51.8464
REMARK 3 T TENSOR
REMARK 3 T11: 0.0503 T22: 0.0199
REMARK 3 T33: 0.1047 T12: -0.0064
REMARK 3 T13: 0.0042 T23: 0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.3204 L22: 1.2410
REMARK 3 L33: 2.1657 L12: 0.2994
REMARK 3 L13: -0.2861 L23: 0.1554
REMARK 3 S TENSOR
REMARK 3 S11: -0.0760 S12: 0.1425 S13: 0.1945
REMARK 3 S21: -0.1315 S22: -0.0347 S23: -0.0019
REMARK 3 S31: -0.2197 S32: -0.0220 S33: 0.1107
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 : C 175 C 191
REMARK 3 ORIGIN FOR THE GROUP (A): 84.6904 76.8405 71.8495
REMARK 3 T TENSOR
REMARK 3 T11: 0.4735 T22: 0.4036
REMARK 3 T33: 0.4992 T12: 0.0341
REMARK 3 T13: -0.0159 T23: 0.0896
REMARK 3 L TENSOR
REMARK 3 L11: 9.3240 L22: 2.8453
REMARK 3 L33: 11.8778 L12: -2.9221
REMARK 3 L13: -2.5330 L23: 3.1744
REMARK 3 S TENSOR
REMARK 3 S11: -0.4622 S12: -0.7356 S13: -0.5502
REMARK 3 S21: 0.7474 S22: -0.0680 S23: 0.0393
REMARK 3 S31: 1.8327 S32: -0.2638 S33: 0.5302
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 192 C 283
REMARK 3 ORIGIN FOR THE GROUP (A): 92.2985 94.3230 58.1372
REMARK 3 T TENSOR
REMARK 3 T11: 0.0556 T22: 0.1989
REMARK 3 T33: 0.1586 T12: -0.0100
REMARK 3 T13: 0.0124 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 2.6845 L22: 1.8643
REMARK 3 L33: 1.3343 L12: 1.1576
REMARK 3 L13: -0.4814 L23: -0.2699
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: -0.1741 S13: 0.0589
REMARK 3 S21: 0.1760 S22: -0.1048 S23: -0.3050
REMARK 3 S31: -0.0458 S32: 0.5126 S33: 0.0653
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 284 C 348
REMARK 3 ORIGIN FOR THE GROUP (A): 78.1544 84.2887 43.3183
REMARK 3 T TENSOR
REMARK 3 T11: 0.0932 T22: 0.0451
REMARK 3 T33: 0.1069 T12: 0.0225
REMARK 3 T13: 0.0226 T23: -0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 4.1046 L22: 3.8773
REMARK 3 L33: 3.2874 L12: -0.1873
REMARK 3 L13: -1.4620 L23: -0.6040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0886 S12: 0.3260 S13: -0.4549
REMARK 3 S21: -0.2523 S22: -0.0862 S23: 0.0200
REMARK 3 S31: 0.2686 S32: 0.1034 S33: -0.0024
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 349 C 381
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3578 97.7152 45.5689
REMARK 3 T TENSOR
REMARK 3 T11: 0.3057 T22: 0.2031
REMARK 3 T33: 0.2131 T12: -0.0725
REMARK 3 T13: -0.0796 T23: -0.0566
REMARK 3 L TENSOR
REMARK 3 L11: 1.4779 L22: 1.3024
REMARK 3 L33: 1.8884 L12: -1.3078
REMARK 3 L13: -0.5428 L23: 0.0396
REMARK 3 S TENSOR
REMARK 3 S11: 0.0976 S12: 0.0509 S13: 0.1316
REMARK 3 S21: -0.2225 S22: 0.0036 S23: -0.0748
REMARK 3 S31: 0.1287 S32: -0.0748 S33: -0.1012
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 382 C 387
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7907 71.9750 51.3469
REMARK 3 T TENSOR
REMARK 3 T11: 0.3010 T22: 0.2641
REMARK 3 T33: 0.5630 T12: -0.0603
REMARK 3 T13: -0.0761 T23: 0.0799
REMARK 3 L TENSOR
REMARK 3 L11: 36.0616 L22: 35.7237
REMARK 3 L33: 36.0108 L12: 18.6686
REMARK 3 L13: -9.4550 L23: 7.5015
REMARK 3 S TENSOR
REMARK 3 S11: 0.6285 S12: -0.3454 S13: -2.5095
REMARK 3 S21: 0.4726 S22: -0.1701 S23: 0.8738
REMARK 3 S31: -0.2331 S32: -0.0483 S33: -0.4584
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2Y6V COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JAN-11.
REMARK 100 THE PDBE ID CODE IS EBI-45785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 MICRO MAX 007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX HF CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34876
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.83
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.6
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.4
REMARK 200 R MERGE FOR SHELL (I) : 0.40
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.97
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: ENSEMBLE OF TEN ALPHA-BETA HYDROLASES AS
REMARK 200 POLY-ALA MODELS TRIMMED TO THE COMMON CORE.
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING OR SITTING DROP VAPOR DIFFUSION
REMARK 280 AT 20 DEGREES CELSIUS. 4 UL OF PROTEIN (7.9 MG/ML) MIXED WITH 2UL
REMARK 280 RESERVOIR (0.1 M HEPES, PH 7.5, 10 % PEG 8000).
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 70.24000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.88500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.24000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.88500
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.3 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 129.36466
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 124.54497
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 42
REMARK 465 ARG A 43
REMARK 465 GLN A 44
REMARK 465 ALA A 80
REMARK 465 GLU A 81
REMARK 465 GLY A 82
REMARK 465 ASN A 83
REMARK 465 ALA A 180
REMARK 465 GLY A 181
REMARK 465 ARG A 182
REMARK 465 PRO A 183
REMARK 465 GLY A 184
REMARK 465 LEU A 185
REMARK 465 ALA A 243
REMARK 465 SER A 244
REMARK 465 GLY A 245
REMARK 465 ASP A 246
REMARK 465 ASP A 247
REMARK 465 GLU A 248
REMARK 465 ASP A 249
REMARK 465 GLY A 250
REMARK 465 HIS A 354
REMARK 465 ILE A 355
REMARK 465 THR A 382
REMARK 465 THR A 383
REMARK 465 LYS A 384
REMARK 465 GLN A 385
REMARK 465 LYS A 386
REMARK 465 LEU A 387
REMARK 465 ALA A 388
REMARK 465 ALA A 389
REMARK 465 ALA A 390
REMARK 465 LEU A 391
REMARK 465 GLU A 392
REMARK 465 HIS A 393
REMARK 465 HIS A 394
REMARK 465 HIS A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 GLN B 44
REMARK 465 GLY B 179
REMARK 465 ALA B 180
REMARK 465 GLY B 181
REMARK 465 ARG B 182
REMARK 465 PRO B 183
REMARK 465 GLY B 184
REMARK 465 LEU B 185
REMARK 465 ALA B 243
REMARK 465 SER B 244
REMARK 465 GLY B 245
REMARK 465 ASP B 246
REMARK 465 ASP B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 GLY B 250
REMARK 465 THR B 382
REMARK 465 THR B 383
REMARK 465 LYS B 384
REMARK 465 GLN B 385
REMARK 465 LYS B 386
REMARK 465 LEU B 387
REMARK 465 ALA B 388
REMARK 465 ALA B 389
REMARK 465 ALA B 390
REMARK 465 LEU B 391
REMARK 465 GLU B 392
REMARK 465 HIS B 393
REMARK 465 HIS B 394
REMARK 465 HIS B 395
REMARK 465 HIS B 396
REMARK 465 HIS B 397
REMARK 465 HIS B 398
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ALA C 243
REMARK 465 SER C 244
REMARK 465 GLY C 245
REMARK 465 ASP C 246
REMARK 465 ASP C 247
REMARK 465 GLU C 248
REMARK 465 ASP C 249
REMARK 465 GLY C 250
REMARK 465 ALA C 388
REMARK 465 ALA C 389
REMARK 465 ALA C 390
REMARK 465 LEU C 391
REMARK 465 GLU C 392
REMARK 465 HIS C 393
REMARK 465 HIS C 394
REMARK 465 HIS C 395
REMARK 465 HIS C 396
REMARK 465 HIS C 397
REMARK 465 HIS C 398
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLN A 3 NH2 ARG B 369 4645 2.15
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 PRO C 186 C - N - CA ANGL. DEV. = 10.4 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 ARG A 46 121.13 -35.44
REMARK 500 THR A 49 43.35 -93.78
REMARK 500 MET A 63 -146.73 -106.06
REMARK 500 VAL A 76 123.40 -38.77
REMARK 500 ALA A 85 140.23 -174.52
REMARK 500 SER A 145 -122.62 49.16
REMARK 500 GLN A 158 80.87 -160.26
REMARK 500 VAL A 172 -56.80 -124.45
REMARK 500 PHE A 272 -15.19 -143.96
REMARK 500 LEU A 324 37.15 -93.70
REMARK 500 GLN A 351 55.38 109.72
REMARK 500 GLN A 357 99.25 -53.44
REMARK 500 GLU B 42 30.42 -163.30
REMARK 500 THR B 49 41.46 -96.10
REMARK 500 MET B 63 -147.09 -107.16
REMARK 500 VAL B 76 123.41 -38.51
REMARK 500 ALA B 80 -73.52 -54.21
REMARK 500 ASN B 83 51.47 76.01
REMARK 500 SER B 145 -118.56 48.57
REMARK 500 GLN B 158 79.86 -156.52
REMARK 500 VAL B 172 -64.38 -124.64
REMARK 500 LEU B 324 38.52 -92.90
REMARK 500 GLN B 351 54.24 111.80
REMARK 500 SER B 353 -30.43 71.94
REMARK 500 GLN B 357 98.48 -54.36
REMARK 500 ARG C 43 3.79 -63.68
REMARK 500 THR C 49 58.22 -140.42
REMARK 500 MET C 63 -147.54 -104.23
REMARK 500 VAL C 76 126.96 -38.07
REMARK 500 ALA C 85 143.83 178.79
REMARK 500 SER C 145 -119.29 47.30
REMARK 500 GLN C 158 78.91 -157.46
REMARK 500 VAL C 172 -57.96 -121.75
REMARK 500 PHE C 272 -9.93 -150.48
REMARK 500 LEU C 324 34.82 -92.12
REMARK 500 THR C 347 -41.85 151.04
REMARK 500 GLN C 357 96.71 54.42
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 SER B 353 23.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1382
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1382
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C1388
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Y6U RELATED DB: PDB
REMARK 900 PEROXISOMAL ALPHA-BETA-HYDROLASE LPX1 (YOR084W)
REMARK 900 FROM SACCHAROMYCES CEREVISIAE (CRYSTAL FORM II)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 C-TERMINAL ELEVEN RESIDUES ARE CLONING ARTEFACT (AAALE)
REMARK 999 AND HEXA-HISTIDINE TAG.
DBREF 2Y6V A 1 387 UNP Q12405 LPX1_YEAST 1 387
DBREF 2Y6V B 1 387 UNP Q12405 LPX1_YEAST 1 387
DBREF 2Y6V C 1 387 UNP Q12405 LPX1_YEAST 1 387
SEQADV 2Y6V ALA A 388 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA A 389 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA A 390 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V LEU A 391 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V GLU A 392 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS A 393 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS A 394 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS A 395 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS A 396 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS A 397 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS A 398 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA B 388 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA B 389 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA B 390 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V LEU B 391 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V GLU B 392 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS B 393 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS B 394 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS B 395 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS B 396 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS B 397 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS B 398 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA C 388 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA C 389 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V ALA C 390 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V LEU C 391 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V GLU C 392 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS C 393 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS C 394 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS C 395 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS C 396 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS C 397 UNP Q12405 EXPRESSION TAG
SEQADV 2Y6V HIS C 398 UNP Q12405 EXPRESSION TAG
SEQRES 1 A 398 MET GLU GLN ASN ARG PHE LYS LYS GLU THR LYS THR CME
SEQRES 2 A 398 SER ALA SER TRP PRO ARG ALA PRO GLN SER THR LEU CSO
SEQRES 3 A 398 ALA THR ASP ARG LEU GLU LEU THR TYR ASP VAL TYR THR
SEQRES 4 A 398 SER ALA GLU ARG GLN ARG ARG SER ARG THR ALA THR ARG
SEQRES 5 A 398 LEU ASN LEU VAL PHE LEU HIS GLY SER GLY MET SER LYS
SEQRES 6 A 398 VAL VAL TRP GLU TYR TYR LEU PRO ARG LEU VAL ALA ALA
SEQRES 7 A 398 ASP ALA GLU GLY ASN TYR ALA ILE ASP LYS VAL LEU LEU
SEQRES 8 A 398 ILE ASP GLN VAL ASN HIS GLY ASP SER ALA VAL ARG ASN
SEQRES 9 A 398 ARG GLY ARG LEU GLY THR ASN PHE ASN TRP ILE ASP GLY
SEQRES 10 A 398 ALA ARG ASP VAL LEU LYS ILE ALA THR CSO GLU LEU GLY
SEQRES 11 A 398 SER ILE ASP SER HIS PRO ALA LEU ASN VAL VAL ILE GLY
SEQRES 12 A 398 HIS SER MET GLY GLY PHE GLN ALA LEU ALA CYS ASP VAL
SEQRES 13 A 398 LEU GLN PRO ASN LEU PHE HIS LEU LEU ILE LEU ILE GLU
SEQRES 14 A 398 PRO VAL VAL ILE THR ARG LYS ALA ILE GLY ALA GLY ARG
SEQRES 15 A 398 PRO GLY LEU PRO PRO ASP SER PRO GLN ILE PRO GLU ASN
SEQRES 16 A 398 LEU TYR ASN SER LEU ARG LEU LYS THR CSO ASP HIS PHE
SEQRES 17 A 398 ALA ASN GLU SER GLU TYR VAL LYS TYR MET ARG ASN GLY
SEQRES 18 A 398 SER PHE PHE THR ASN ALA HIS SER GLN ILE LEU GLN ASN
SEQRES 19 A 398 ILE ILE ASP PHE GLU ARG THR LYS ALA SER GLY ASP ASP
SEQRES 20 A 398 GLU ASP GLY GLY PRO VAL ARG THR LYS MET GLU GLN ALA
SEQRES 21 A 398 GLN ASN LEU LEU CYS TYR MET ASN MET GLN THR PHE ALA
SEQRES 22 A 398 PRO PHE LEU ILE SER ASN VAL LYS PHE VAL ARG LYS ARG
SEQRES 23 A 398 THR ILE HIS ILE VAL GLY ALA ARG SER ASN TRP CSO PRO
SEQRES 24 A 398 PRO GLN ASN GLN LEU PHE LEU GLN LYS THR LEU GLN ASN
SEQRES 25 A 398 TYR HIS LEU ASP VAL ILE PRO GLY GLY SER HIS LEU VAL
SEQRES 26 A 398 ASN VAL GLU ALA PRO ASP LEU VAL ILE GLU ARG ILE ASN
SEQRES 27 A 398 HIS HIS ILE HIS GLU PHE VAL LEU THR SER PRO LEU GLN
SEQRES 28 A 398 SER SER HIS ILE PRO GLN LEU THR LEU GLU GLU ARG ALA
SEQRES 29 A 398 VAL MET PHE ASP ARG ALA PHE ASP SER PHE LYS ASN GLU
SEQRES 30 A 398 ALA LEU VAL LYS THR THR LYS GLN LYS LEU ALA ALA ALA
SEQRES 31 A 398 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 398 MET GLU GLN ASN ARG PHE LYS LYS GLU THR LYS THR CME
SEQRES 2 B 398 SER ALA SER TRP PRO ARG ALA PRO GLN SER THR LEU CSO
SEQRES 3 B 398 ALA THR ASP ARG LEU GLU LEU THR TYR ASP VAL TYR THR
SEQRES 4 B 398 SER ALA GLU ARG GLN ARG ARG SER ARG THR ALA THR ARG
SEQRES 5 B 398 LEU ASN LEU VAL PHE LEU HIS GLY SER GLY MET SER LYS
SEQRES 6 B 398 VAL VAL TRP GLU TYR TYR LEU PRO ARG LEU VAL ALA ALA
SEQRES 7 B 398 ASP ALA GLU GLY ASN TYR ALA ILE ASP LYS VAL LEU LEU
SEQRES 8 B 398 ILE ASP GLN VAL ASN HIS GLY ASP SER ALA VAL ARG ASN
SEQRES 9 B 398 ARG GLY ARG LEU GLY THR ASN PHE ASN TRP ILE ASP GLY
SEQRES 10 B 398 ALA ARG ASP VAL LEU LYS ILE ALA THR CSO GLU LEU GLY
SEQRES 11 B 398 SER ILE ASP SER HIS PRO ALA LEU ASN VAL VAL ILE GLY
SEQRES 12 B 398 HIS SER MET GLY GLY PHE GLN ALA LEU ALA CYS ASP VAL
SEQRES 13 B 398 LEU GLN PRO ASN LEU PHE HIS LEU LEU ILE LEU ILE GLU
SEQRES 14 B 398 PRO VAL VAL ILE THR ARG LYS ALA ILE GLY ALA GLY ARG
SEQRES 15 B 398 PRO GLY LEU PRO PRO ASP SER PRO GLN ILE PRO GLU ASN
SEQRES 16 B 398 LEU TYR ASN SER LEU ARG LEU LYS THR CSO ASP HIS PHE
SEQRES 17 B 398 ALA ASN GLU SER GLU TYR VAL LYS TYR MET ARG ASN GLY
SEQRES 18 B 398 SER PHE PHE THR ASN ALA HIS SER GLN ILE LEU GLN ASN
SEQRES 19 B 398 ILE ILE ASP PHE GLU ARG THR LYS ALA SER GLY ASP ASP
SEQRES 20 B 398 GLU ASP GLY GLY PRO VAL ARG THR LYS MET GLU GLN ALA
SEQRES 21 B 398 GLN ASN LEU LEU CYS TYR MET ASN MET GLN THR PHE ALA
SEQRES 22 B 398 PRO PHE LEU ILE SER ASN VAL LYS PHE VAL ARG LYS ARG
SEQRES 23 B 398 THR ILE HIS ILE VAL GLY ALA ARG SER ASN TRP CSO PRO
SEQRES 24 B 398 PRO GLN ASN GLN LEU PHE LEU GLN LYS THR LEU GLN ASN
SEQRES 25 B 398 TYR HIS LEU ASP VAL ILE PRO GLY GLY SER HIS LEU VAL
SEQRES 26 B 398 ASN VAL GLU ALA PRO ASP LEU VAL ILE GLU ARG ILE ASN
SEQRES 27 B 398 HIS HIS ILE HIS GLU PHE VAL LEU THR SER PRO LEU GLN
SEQRES 28 B 398 SER SER HIS ILE PRO GLN LEU THR LEU GLU GLU ARG ALA
SEQRES 29 B 398 VAL MET PHE ASP ARG ALA PHE ASP SER PHE LYS ASN GLU
SEQRES 30 B 398 ALA LEU VAL LYS THR THR LYS GLN LYS LEU ALA ALA ALA
SEQRES 31 B 398 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 398 MET GLU GLN ASN ARG PHE LYS LYS GLU THR LYS THR CME
SEQRES 2 C 398 SER ALA SER TRP PRO ARG ALA PRO GLN SER THR LEU CSO
SEQRES 3 C 398 ALA THR ASP ARG LEU GLU LEU THR TYR ASP VAL TYR THR
SEQRES 4 C 398 SER ALA GLU ARG GLN ARG ARG SER ARG THR ALA THR ARG
SEQRES 5 C 398 LEU ASN LEU VAL PHE LEU HIS GLY SER GLY MET SER LYS
SEQRES 6 C 398 VAL VAL TRP GLU TYR TYR LEU PRO ARG LEU VAL ALA ALA
SEQRES 7 C 398 ASP ALA GLU GLY ASN TYR ALA ILE ASP LYS VAL LEU LEU
SEQRES 8 C 398 ILE ASP GLN VAL ASN HIS GLY ASP SER ALA VAL ARG ASN
SEQRES 9 C 398 ARG GLY ARG LEU GLY THR ASN PHE ASN TRP ILE ASP GLY
SEQRES 10 C 398 ALA ARG ASP VAL LEU LYS ILE ALA THR CSO GLU LEU GLY
SEQRES 11 C 398 SER ILE ASP SER HIS PRO ALA LEU ASN VAL VAL ILE GLY
SEQRES 12 C 398 HIS SER MET GLY GLY PHE GLN ALA LEU ALA CYS ASP VAL
SEQRES 13 C 398 LEU GLN PRO ASN LEU PHE HIS LEU LEU ILE LEU ILE GLU
SEQRES 14 C 398 PRO VAL VAL ILE THR ARG LYS ALA ILE GLY ALA GLY ARG
SEQRES 15 C 398 PRO GLY LEU PRO PRO ASP SER PRO GLN ILE PRO GLU ASN
SEQRES 16 C 398 LEU TYR ASN SER LEU ARG LEU LYS THR CSO ASP HIS PHE
SEQRES 17 C 398 ALA ASN GLU SER GLU TYR VAL LYS TYR MET ARG ASN GLY
SEQRES 18 C 398 SER PHE PHE THR ASN ALA HIS SER GLN ILE LEU GLN ASN
SEQRES 19 C 398 ILE ILE ASP PHE GLU ARG THR LYS ALA SER GLY ASP ASP
SEQRES 20 C 398 GLU ASP GLY GLY PRO VAL ARG THR LYS MET GLU GLN ALA
SEQRES 21 C 398 GLN ASN LEU LEU CYS TYR MET ASN MET GLN THR PHE ALA
SEQRES 22 C 398 PRO PHE LEU ILE SER ASN VAL LYS PHE VAL ARG LYS ARG
SEQRES 23 C 398 THR ILE HIS ILE VAL GLY ALA ARG SER ASN TRP CSO PRO
SEQRES 24 C 398 PRO GLN ASN GLN LEU PHE LEU GLN LYS THR LEU GLN ASN
SEQRES 25 C 398 TYR HIS LEU ASP VAL ILE PRO GLY GLY SER HIS LEU VAL
SEQRES 26 C 398 ASN VAL GLU ALA PRO ASP LEU VAL ILE GLU ARG ILE ASN
SEQRES 27 C 398 HIS HIS ILE HIS GLU PHE VAL LEU THR SER PRO LEU GLN
SEQRES 28 C 398 SER SER HIS ILE PRO GLN LEU THR LEU GLU GLU ARG ALA
SEQRES 29 C 398 VAL MET PHE ASP ARG ALA PHE ASP SER PHE LYS ASN GLU
SEQRES 30 C 398 ALA LEU VAL LYS THR THR LYS GLN LYS LEU ALA ALA ALA
SEQRES 31 C 398 LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 2Y6V CME A 13 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2Y6V CSO A 26 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO A 127 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO A 205 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO A 298 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CME B 13 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2Y6V CSO B 26 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO B 127 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO B 205 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO B 298 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CME C 13 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2Y6V CSO C 26 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO C 127 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO C 205 CYS S-HYDROXYCYSTEINE
MODRES 2Y6V CSO C 298 CYS S-HYDROXYCYSTEINE
HET CME A 13 10
HET CSO A 26 7
HET CSO A 127 7
HET CSO A 205 7
HET CSO A 298 7
HET CME B 13 10
HET CSO B 26 7
HET CSO B 127 7
HET CSO B 205 7
HET CSO B 298 7
HET CME C 13 10
HET CSO C 26 7
HET CSO C 127 7
HET CSO C 205 7
HET CSO C 298 14
HET PO4 A1382 5
HET PO4 B1382 5
HET PO4 C1388 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM PO4 PHOSPHATE ION
FORMUL 4 CME 3(C5 H11 N O3 S2)
FORMUL 5 CSO 12(C3 H7 N O3 S)
FORMUL 6 PO4 3(O4 P 3-)
FORMUL 7 HOH *71(H2 O)
HELIX 1 1 SER A 64 LEU A 75 5 12
HELIX 2 2 HIS A 97 ASN A 104 1 8
HELIX 3 3 ASN A 113 LEU A 129 1 17
HELIX 4 4 SER A 131 HIS A 135 5 5
HELIX 5 5 SER A 145 GLN A 158 1 14
HELIX 6 6 GLU A 194 LYS A 203 1 10
HELIX 7 7 ASN A 210 GLY A 221 1 12
HELIX 8 8 HIS A 228 GLU A 239 1 12
HELIX 9 9 GLU A 258 CYS A 265 1 8
HELIX 10 10 ASN A 268 THR A 271 5 4
HELIX 11 11 PHE A 272 SER A 278 1 7
HELIX 12 12 ASN A 279 VAL A 283 5 5
HELIX 13 13 PRO A 299 LEU A 310 1 12
HELIX 14 14 LEU A 324 ALA A 329 1 6
HELIX 15 15 ALA A 329 SER A 348 1 20
HELIX 16 16 THR A 359 ALA A 378 1 20
HELIX 17 17 SER B 64 LEU B 75 5 12
HELIX 18 18 HIS B 97 ASN B 104 1 8
HELIX 19 19 ASN B 113 LEU B 129 1 17
HELIX 20 20 SER B 131 HIS B 135 5 5
HELIX 21 21 SER B 145 GLN B 158 1 14
HELIX 22 22 GLU B 194 LYS B 203 1 10
HELIX 23 23 ASN B 210 GLY B 221 1 12
HELIX 24 24 HIS B 228 GLU B 239 1 12
HELIX 25 25 GLU B 258 CYS B 265 1 8
HELIX 26 26 ASN B 268 THR B 271 5 4
HELIX 27 27 PHE B 272 SER B 278 1 7
HELIX 28 28 ASN B 279 VAL B 283 5 5
HELIX 29 29 PRO B 299 LEU B 310 1 12
HELIX 30 30 LEU B 324 ALA B 329 1 6
HELIX 31 31 ALA B 329 SER B 348 1 20
HELIX 32 32 THR B 359 ALA B 378 1 20
HELIX 33 33 SER C 64 LEU C 75 5 12
HELIX 34 34 HIS C 97 ASN C 104 1 8
HELIX 35 35 ASN C 113 LEU C 129 1 17
HELIX 36 36 SER C 131 HIS C 135 5 5
HELIX 37 37 SER C 145 GLN C 158 1 14
HELIX 38 38 PRO C 193 LYS C 203 1 11
HELIX 39 39 ASN C 210 GLY C 221 1 12
HELIX 40 40 HIS C 228 ARG C 240 1 13
HELIX 41 41 GLU C 258 CYS C 265 1 8
HELIX 42 42 ASN C 268 THR C 271 5 4
HELIX 43 43 PHE C 272 VAL C 280 1 9
HELIX 44 44 LYS C 281 VAL C 283 5 3
HELIX 45 45 PRO C 299 LEU C 310 1 12
HELIX 46 46 LEU C 324 ALA C 329 1 6
HELIX 47 47 ALA C 329 LEU C 346 1 18
HELIX 48 48 THR C 359 LEU C 379 1 21
HELIX 49 49 THR C 382 LEU C 387 1 6
SHEET 1 AA 8 PHE A 6 SER A 14 0
SHEET 2 AA 8 GLU A 32 SER A 40 -1 O LEU A 33 N CME A 13
SHEET 3 AA 8 ALA A 85 ASP A 93 -1 O ASP A 87 N SER A 40
SHEET 4 AA 8 ARG A 52 LEU A 58 1 O LEU A 53 N ASP A 87
SHEET 5 AA 8 ALA A 137 HIS A 144 1 O LEU A 138 N ASN A 54
SHEET 6 AA 8 LEU A 164 ILE A 168 1 O LEU A 164 N VAL A 141
SHEET 7 AA 8 ARG A 286 GLY A 292 1 O ARG A 286 N LEU A 165
SHEET 8 AA 8 TYR A 313 ILE A 318 1 O HIS A 314 N HIS A 289
SHEET 1 AB 2 ILE A 192 PRO A 193 0
SHEET 2 AB 2 LEU B 379 VAL B 380 1 N VAL B 380 O ILE A 192
SHEET 1 AC 3 HIS A 207 PHE A 208 0
SHEET 2 AC 3 VAL A 253 THR A 255 -1 O VAL A 253 N PHE A 208
SHEET 3 AC 3 ARG A 240 THR A 241 -1 O THR A 241 N ARG A 254
SHEET 1 AD 2 LEU A 379 VAL A 380 0
SHEET 2 AD 2 ILE B 192 PRO B 193 1 O ILE B 192 N VAL A 380
SHEET 1 BA 8 PHE B 6 SER B 14 0
SHEET 2 BA 8 GLU B 32 SER B 40 -1 O LEU B 33 N CME B 13
SHEET 3 BA 8 TYR B 84 ASP B 93 -1 O ASP B 87 N SER B 40
SHEET 4 BA 8 THR B 51 LEU B 58 1 O THR B 51 N ALA B 85
SHEET 5 BA 8 ALA B 137 HIS B 144 1 O LEU B 138 N ASN B 54
SHEET 6 BA 8 LEU B 164 ILE B 168 1 O LEU B 164 N VAL B 141
SHEET 7 BA 8 ARG B 286 GLY B 292 1 O ARG B 286 N LEU B 165
SHEET 8 BA 8 TYR B 313 ILE B 318 1 O HIS B 314 N HIS B 289
SHEET 1 BB 3 HIS B 207 PHE B 208 0
SHEET 2 BB 3 VAL B 253 THR B 255 -1 O VAL B 253 N PHE B 208
SHEET 3 BB 3 ARG B 240 THR B 241 -1 O THR B 241 N ARG B 254
SHEET 1 CA 8 PHE C 6 SER C 14 0
SHEET 2 CA 8 GLU C 32 SER C 40 -1 O LEU C 33 N CME C 13
SHEET 3 CA 8 TYR C 84 ILE C 92 -1 O ASP C 87 N SER C 40
SHEET 4 CA 8 THR C 51 LEU C 58 1 O THR C 51 N ALA C 85
SHEET 5 CA 8 ALA C 137 HIS C 144 1 O LEU C 138 N ASN C 54
SHEET 6 CA 8 LEU C 164 ILE C 168 1 O LEU C 164 N VAL C 141
SHEET 7 CA 8 ARG C 286 GLY C 292 1 O ARG C 286 N LEU C 165
SHEET 8 CA 8 TYR C 313 ILE C 318 1 O HIS C 314 N HIS C 289
SHEET 1 CB 2 HIS C 207 PHE C 208 0
SHEET 2 CB 2 VAL C 253 ARG C 254 -1 O VAL C 253 N PHE C 208
LINK C THR A 12 N CME A 13 1555 1555 1.33
LINK C CME A 13 N SER A 14 1555 1555 1.33
LINK C LEU A 25 N CSO A 26 1555 1555 1.34
LINK C CSO A 26 N ALA A 27 1555 1555 1.33
LINK C THR A 126 N CSO A 127 1555 1555 1.32
LINK C CSO A 127 N GLU A 128 1555 1555 1.33
LINK C THR A 204 N CSO A 205 1555 1555 1.33
LINK C CSO A 205 N ASP A 206 1555 1555 1.33
LINK C TRP A 297 N CSO A 298 1555 1555 1.34
LINK C CSO A 298 N PRO A 299 1555 1555 1.34
LINK C THR B 12 N CME B 13 1555 1555 1.32
LINK C CME B 13 N SER B 14 1555 1555 1.34
LINK C LEU B 25 N CSO B 26 1555 1555 1.33
LINK C CSO B 26 N ALA B 27 1555 1555 1.33
LINK C THR B 126 N CSO B 127 1555 1555 1.31
LINK C CSO B 127 N GLU B 128 1555 1555 1.34
LINK C THR B 204 N CSO B 205 1555 1555 1.34
LINK C CSO B 205 N ASP B 206 1555 1555 1.34
LINK C TRP B 297 N CSO B 298 1555 1555 1.34
LINK C CSO B 298 N PRO B 299 1555 1555 1.33
LINK C THR C 12 N CME C 13 1555 1555 1.33
LINK C CME C 13 N SER C 14 1555 1555 1.33
LINK C LEU C 25 N CSO C 26 1555 1555 1.33
LINK C CSO C 26 N ALA C 27 1555 1555 1.33
LINK C THR C 126 N CSO C 127 1555 1555 1.33
LINK C CSO C 127 N GLU C 128 1555 1555 1.32
LINK C THR C 204 N CSO C 205 1555 1555 1.34
LINK C CSO C 205 N ASP C 206 1555 1555 1.33
LINK C TRP C 297 N BCSO C 298 1555 1555 1.33
LINK C TRP C 297 N ACSO C 298 1555 1555 1.34
LINK C BCSO C 298 N PRO C 299 1555 1555 1.35
LINK C ACSO C 298 N PRO C 299 1555 1555 1.35
CISPEP 1 TRP A 17 PRO A 18 0 -5.61
CISPEP 2 HIS A 135 PRO A 136 0 0.40
CISPEP 3 LEU A 350 GLN A 351 0 14.88
CISPEP 4 TRP B 17 PRO B 18 0 -5.34
CISPEP 5 HIS B 135 PRO B 136 0 3.03
CISPEP 6 LEU B 350 GLN B 351 0 12.02
CISPEP 7 TRP C 17 PRO C 18 0 -5.56
CISPEP 8 HIS C 135 PRO C 136 0 1.18
CISPEP 9 ALA C 180 GLY C 181 0 18.05
SITE 1 AC1 4 ASN A 296 TRP A 297 SER A 322 HIS A 323
SITE 1 AC2 5 SER B 295 ASN B 296 TRP B 297 SER B 322
SITE 2 AC2 5 HIS B 323
SITE 1 AC3 5 SER C 295 ASN C 296 TRP C 297 SER C 322
SITE 2 AC3 5 HIS C 323
CRYST1 140.480 87.770 125.040 90.00 95.10 90.00 C 1 2 1 12
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 0.007118 0.000000 0.000635 0.00000
SCALE2 0.000000 0.011393 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008029 0.00000
MTRIX1 1 -0.736100 0.366600 0.569000 126.30000 1
MTRIX2 1 0.367300 -0.489600 0.790800 32.10000 1
MTRIX3 1 0.568500 0.791100 0.225700 -79.37000 1
MTRIX1 2 0.709000 0.402100 -0.579400 -10.21000 1
MTRIX2 2 -0.349000 -0.513800 -0.783700 174.00000 1
MTRIX3 2 -0.612800 0.757800 -0.223900 81.13000 1
TER 2856 LYS A 381
TER 5772 LYS B 381
TER 8796 LEU C 387
MASTER 775 0 18 49 36 0 5 12 8879 3 166 93
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