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HEADER HYDROLASE/HYDROLASE INHIBITOR 07-MAR-14 4PSE
TITLE TRICHODERMA REESEI CUTINASE IN COMPLEX WITH A C11Y4 PHOSPHONATE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE FAMILY 5;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: MATURE FORM, COMPLEXED;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRICHODERMA REESEI;
SOURCE 3 ORGANISM_TAXID: 431241;
SOURCE 4 STRAIN: QM6A;
SOURCE 5 GENE: TRIREDRAFT_60489;
SOURCE 6 EXPRESSION_SYSTEM: TRICHODERMA REESEI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 51453
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROUSSEL,S.AMARA,A.NYYSSOLA,E.MATEOS-DIAZ,S.BLANGY,H.KONTKANEN,
AUTHOR 2 A.WESTERHOLM-PARVINEN,F.CARRIERE,C.CAMBILLAU
REVDAT 1 17-SEP-14 4PSE 0
JRNL AUTH A.ROUSSEL,S.AMARA,A.NYYSSOLA,E.MATEOS-DIAZ,S.BLANGY,
JRNL AUTH 2 H.KONTKANEN,A.WESTERHOLM-PARVINEN,F.CARRIERE,C.CAMBILLAU
JRNL TITL A CUTINASE FROM TRICHODERMA REESEI WITH A LID-COVERED ACTIVE
JRNL TITL 2 SITE AND KINETIC PROPERTIES OF TRUE LIPASES DEFINES A NEW
JRNL TITL 3 CLASS OF LIPOLYTIC ENZYMES
JRNL REF J.MOL.BIOL. 2014
JRNL REFN ESSN 1089-8638
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 51220
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2627
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.75
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.39
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3721
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3130
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3523
REMARK 3 BIN R VALUE (WORKING SET) : 0.3127
REMARK 3 BIN FREE R VALUE : 0.3196
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.32
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 198
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3182
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.71280
REMARK 3 B22 (A**2) : -13.31680
REMARK 3 B33 (A**2) : 14.02970
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.07360
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.264
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.115
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3338 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4549 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1097 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 78 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 484 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3338 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 451 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4239 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.15
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.23
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.85
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|31 - A|43}
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1027 6.2159 40.2502
REMARK 3 T TENSOR
REMARK 3 T11: -0.0123 T22: 0.0091
REMARK 3 T33: 0.0003 T12: -0.0153
REMARK 3 T13: 0.0022 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.0367 L22: 0.0056
REMARK 3 L33: 0.0288 L12: 0.0194
REMARK 3 L13: -0.0149 L23: 0.0113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0003 S12: 0.0012 S13: -0.0012
REMARK 3 S21: -0.0012 S22: 0.0005 S23: -0.0008
REMARK 3 S31: 0.0007 S32: 0.0007 S33: -0.0008
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|44 - A|55}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2886 18.0286 39.8181
REMARK 3 T TENSOR
REMARK 3 T11: 0.0106 T22: -0.0076
REMARK 3 T33: 0.0016 T12: -0.0079
REMARK 3 T13: 0.0073 T23: 0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 0.0309 L22: 0.0048
REMARK 3 L33: 0.0169 L12: -0.0568
REMARK 3 L13: 0.0671 L23: -0.2642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: -0.0018 S13: -0.0014
REMARK 3 S21: 0.0013 S22: 0.0072 S23: -0.0014
REMARK 3 S31: 0.0022 S32: 0.0027 S33: -0.0071
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|56 - A|78}
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9771 13.1350 48.9891
REMARK 3 T TENSOR
REMARK 3 T11: -0.0077 T22: -0.0173
REMARK 3 T33: 0.0254 T12: 0.0403
REMARK 3 T13: -0.0447 T23: 0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 0.0407 L22: 0.0594
REMARK 3 L33: -0.0407 L12: -0.8729
REMARK 3 L13: -0.1545 L23: -0.3831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.0037 S13: 0.0161
REMARK 3 S21: -0.0049 S22: 0.0028 S23: 0.0136
REMARK 3 S31: -0.0084 S32: -0.0049 S33: 0.0017
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|79 - A|116}
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9167 2.2793 55.9669
REMARK 3 T TENSOR
REMARK 3 T11: -0.0718 T22: -0.0249
REMARK 3 T33: 0.0831 T12: -0.0223
REMARK 3 T13: -0.0176 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 0.6432 L22: 0.3152
REMARK 3 L33: 0.1289 L12: -0.7435
REMARK 3 L13: 0.1003 L23: 0.0061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0065 S12: -0.0238 S13: 0.0286
REMARK 3 S21: -0.0355 S22: -0.0096 S23: 0.0432
REMARK 3 S31: -0.0279 S32: -0.0614 S33: 0.0161
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|117 - A|143}
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1631 7.2560 54.4065
REMARK 3 T TENSOR
REMARK 3 T11: -0.0203 T22: -0.0610
REMARK 3 T33: 0.0641 T12: -0.0478
REMARK 3 T13: -0.0224 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: -0.1127 L22: 1.2454
REMARK 3 L33: 0.2383 L12: -0.0223
REMARK 3 L13: 0.5699 L23: -0.1621
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: 0.0263 S13: 0.0172
REMARK 3 S21: 0.0009 S22: 0.0046 S23: 0.0006
REMARK 3 S31: -0.0210 S32: 0.0084 S33: -0.0003
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|144 - A|170}
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0008 0.8761 62.6405
REMARK 3 T TENSOR
REMARK 3 T11: -0.0169 T22: -0.0552
REMARK 3 T33: 0.0690 T12: -0.0139
REMARK 3 T13: -0.0176 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.1781 L22: 0.7314
REMARK 3 L33: -0.0244 L12: 0.1222
REMARK 3 L13: -0.0910 L23: 0.2227
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.0268 S13: 0.0318
REMARK 3 S21: 0.0027 S22: 0.0056 S23: 0.0051
REMARK 3 S31: -0.0077 S32: -0.0239 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|171 - A|206}
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7746 -6.5396 57.8107
REMARK 3 T TENSOR
REMARK 3 T11: -0.0158 T22: -0.0931
REMARK 3 T33: 0.1035 T12: -0.0186
REMARK 3 T13: -0.0188 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: -0.0172 L22: 0.5340
REMARK 3 L33: 0.2538 L12: -0.6909
REMARK 3 L13: 0.5029 L23: -0.4173
REMARK 3 S TENSOR
REMARK 3 S11: -0.0078 S12: 0.0405 S13: -0.0179
REMARK 3 S21: 0.0060 S22: 0.0169 S23: -0.0200
REMARK 3 S31: 0.0201 S32: -0.0104 S33: -0.0090
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {A|207 - A|236}
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2995 -4.1079 42.2856
REMARK 3 T TENSOR
REMARK 3 T11: -0.0115 T22: 0.0297
REMARK 3 T33: -0.0231 T12: -0.0785
REMARK 3 T13: -0.0033 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.1275 L22: 0.2111
REMARK 3 L33: 0.6524 L12: -0.2047
REMARK 3 L13: 0.3909 L23: -0.0655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: 0.0243 S13: -0.0187
REMARK 3 S21: -0.0090 S22: 0.0050 S23: 0.0129
REMARK 3 S31: 0.0191 S32: 0.0089 S33: 0.0002
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {A|237 - A|249}
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6826 -10.4820 58.6250
REMARK 3 T TENSOR
REMARK 3 T11: -0.0373 T22: 0.0064
REMARK 3 T33: 0.0315 T12: -0.0554
REMARK 3 T13: -0.0016 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.0789 L22: 0.0334
REMARK 3 L33: 0.0128 L12: 0.4091
REMARK 3 L13: 0.0545 L23: -0.1322
REMARK 3 S TENSOR
REMARK 3 S11: -0.0037 S12: -0.0037 S13: -0.0010
REMARK 3 S21: -0.0015 S22: 0.0032 S23: 0.0084
REMARK 3 S31: 0.0038 S32: -0.0012 S33: 0.0005
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {B|31 - B|43}
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0164 7.2065 24.0143
REMARK 3 T TENSOR
REMARK 3 T11: -0.0009 T22: 0.0060
REMARK 3 T33: 0.0010 T12: 0.0014
REMARK 3 T13: 0.0011 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.0206 L22: 0.0000
REMARK 3 L33: -0.0045 L12: -0.0083
REMARK 3 L13: -0.0164 L23: -0.0210
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: -0.0001 S13: 0.0007
REMARK 3 S21: -0.0005 S22: -0.0003 S23: 0.0004
REMARK 3 S31: -0.0014 S32: -0.0005 S33: 0.0004
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {B|44 - B|55}
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5824 17.4497 28.9564
REMARK 3 T TENSOR
REMARK 3 T11: 0.0098 T22: 0.0087
REMARK 3 T33: 0.0043 T12: 0.0012
REMARK 3 T13: -0.0008 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.0170 L22: 0.0179
REMARK 3 L33: 0.0881 L12: 0.0161
REMARK 3 L13: 0.0349 L23: -0.0035
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: 0.0014 S13: -0.0004
REMARK 3 S21: -0.0009 S22: 0.0009 S23: 0.0002
REMARK 3 S31: 0.0023 S32: 0.0017 S33: -0.0007
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {B|56 - B|78}
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4331 11.4108 22.1858
REMARK 3 T TENSOR
REMARK 3 T11: 0.0032 T22: 0.0027
REMARK 3 T33: -0.0085 T12: -0.0040
REMARK 3 T13: 0.0019 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0374 L22: 0.0049
REMARK 3 L33: 0.0323 L12: 0.0851
REMARK 3 L13: 0.0090 L23: -0.0333
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 0.0003 S13: 0.0010
REMARK 3 S21: 0.0017 S22: 0.0011 S23: -0.0032
REMARK 3 S31: -0.0019 S32: 0.0008 S33: -0.0007
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: {B|79 - B|116}
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6154 3.0628 11.8986
REMARK 3 T TENSOR
REMARK 3 T11: 0.0106 T22: 0.0348
REMARK 3 T33: -0.0676 T12: 0.0005
REMARK 3 T13: 0.0196 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.0479 L22: 0.0001
REMARK 3 L33: 0.4647 L12: -0.4767
REMARK 3 L13: 0.0346 L23: -0.6017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0040 S13: -0.0077
REMARK 3 S21: 0.0037 S22: 0.0069 S23: -0.0216
REMARK 3 S31: -0.0084 S32: 0.0014 S33: -0.0074
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: {B|117 - B|143}
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1301 10.2901 12.5877
REMARK 3 T TENSOR
REMARK 3 T11: -0.0001 T22: 0.0121
REMARK 3 T33: -0.0201 T12: 0.0123
REMARK 3 T13: 0.0044 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.0369 L22: 0.0000
REMARK 3 L33: 0.2103 L12: -0.1574
REMARK 3 L13: 0.1295 L23: -0.1595
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: 0.0014 S13: 0.0045
REMARK 3 S21: -0.0072 S22: 0.0000 S23: 0.0038
REMARK 3 S31: -0.0063 S32: 0.0006 S33: 0.0006
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: {B|144 - B|170}
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1207 5.7066 3.8374
REMARK 3 T TENSOR
REMARK 3 T11: 0.0141 T22: 0.0392
REMARK 3 T33: -0.0629 T12: 0.0073
REMARK 3 T13: 0.0071 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.5057 L22: 0.0312
REMARK 3 L33: 0.3796 L12: -0.1191
REMARK 3 L13: 0.5199 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.0142 S13: 0.0135
REMARK 3 S21: -0.0013 S22: 0.0002 S23: -0.0043
REMARK 3 S31: -0.0008 S32: -0.0064 S33: 0.0023
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: {B|171 - B|206}
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5613 -1.6885 5.0006
REMARK 3 T TENSOR
REMARK 3 T11: 0.0175 T22: 0.0261
REMARK 3 T33: -0.0532 T12: -0.0250
REMARK 3 T13: -0.0040 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.1763 L22: 0.0000
REMARK 3 L33: 0.1732 L12: 0.3420
REMARK 3 L13: 0.1979 L23: 0.1382
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: 0.0017 S13: 0.0026
REMARK 3 S21: -0.0003 S22: -0.0012 S23: 0.0100
REMARK 3 S31: 0.0028 S32: -0.0003 S33: 0.0007
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: {B|207 - B|236}
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5394 -5.2055 21.3817
REMARK 3 T TENSOR
REMARK 3 T11: 0.0279 T22: 0.0226
REMARK 3 T33: -0.0610 T12: -0.0213
REMARK 3 T13: 0.0021 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 0.0462 L22: 0.0000
REMARK 3 L33: 0.2273 L12: 0.2698
REMARK 3 L13: 0.0494 L23: 0.0540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: -0.0045 S13: -0.0045
REMARK 3 S21: -0.0019 S22: -0.0022 S23: 0.0038
REMARK 3 S31: 0.0086 S32: -0.0012 S33: 0.0022
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: {B|237 - B|248}
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1261 -8.1966 6.5355
REMARK 3 T TENSOR
REMARK 3 T11: 0.0047 T22: 0.0018
REMARK 3 T33: -0.0077 T12: 0.0054
REMARK 3 T13: 0.0052 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: -0.0011 L22: 0.0174
REMARK 3 L33: 0.0052 L12: -0.0327
REMARK 3 L13: 0.0037 L23: 0.0098
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: 0.0008 S13: -0.0014
REMARK 3 S21: 0.0009 S22: 0.0003 S23: -0.0008
REMARK 3 S31: 0.0004 S32: -0.0003 S33: -0.0005
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PSE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : BENT CYLINDRICAL MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51222
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.86000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.150
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4PSC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXING 300 NL ENZYME AT 10 MG/ML AND
REMARK 280 30 MM BETAOG WITH 100 NL OF PEG3350 (17%), BIS-TRIS (0.1 M), PH
REMARK 280 5.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 18.77200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 ARG A 2
REMARK 465 SER A 3
REMARK 465 LEU A 4
REMARK 465 ALA A 5
REMARK 465 ILE A 6
REMARK 465 LEU A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 LEU A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 13
REMARK 465 HIS A 14
REMARK 465 ALA A 15
REMARK 465 PHE A 16
REMARK 465 ALA A 17
REMARK 465 TYR A 18
REMARK 465 PRO A 19
REMARK 465 LYS A 20
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 PRO A 23
REMARK 465 GLN A 24
REMARK 465 SER A 25
REMARK 465 VAL A 26
REMARK 465 ASN A 27
REMARK 465 ARG A 28
REMARK 465 ARG A 29
REMARK 465 ASP A 30
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 SER B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 ILE B 6
REMARK 465 LEU B 7
REMARK 465 THR B 8
REMARK 465 THR B 9
REMARK 465 LEU B 10
REMARK 465 LEU B 11
REMARK 465 ALA B 12
REMARK 465 GLY B 13
REMARK 465 HIS B 14
REMARK 465 ALA B 15
REMARK 465 PHE B 16
REMARK 465 ALA B 17
REMARK 465 TYR B 18
REMARK 465 PRO B 19
REMARK 465 LYS B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 PRO B 23
REMARK 465 GLN B 24
REMARK 465 SER B 25
REMARK 465 VAL B 26
REMARK 465 ASN B 27
REMARK 465 ARG B 28
REMARK 465 ARG B 29
REMARK 465 ASP B 30
REMARK 465 HIS B 250
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 47 CD1
REMARK 470 ASP A 49 CG OD1 OD2
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 HIS A 249 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 47 CD1
REMARK 470 ASP B 49 CG OD1 OD2
REMARK 470 ILE B 51 CG1 CG2 CD1
REMARK 470 GLU B 73 CG CD OE1 OE2
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 HIS A 250 O HOH A 463 2546 1.97
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 PRO A 46 -84.53 -119.20
REMARK 500 ASN A 76 45.16 -147.87
REMARK 500 VAL A 100 -59.58 -128.83
REMARK 500 SER A 164 -117.73 54.81
REMARK 500 SER A 248 -162.18 96.86
REMARK 500 HIS A 249 158.63 72.57
REMARK 500 PRO B 46 -74.63 -90.31
REMARK 500 ILE B 47 -77.00 -38.04
REMARK 500 ILE B 51 12.74 -68.56
REMARK 500 THR B 52 -89.51 -118.02
REMARK 500 ALA B 53 -13.02 -42.73
REMARK 500 ASN B 76 44.82 -147.00
REMARK 500 VAL B 100 -59.27 -127.83
REMARK 500 SER B 164 -117.67 53.84
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 VAL A 244 23.0 L L OUTSIDE RANGE
REMARK 500 VAL A 247 24.5 L L OUTSIDE RANGE
REMARK 500 SER A 248 24.5 L L OUTSIDE RANGE
REMARK 500 HIS A 249 20.7 L L OUTSIDE RANGE
REMARK 500 ARG B 115 24.0 L L OUTSIDE RANGE
REMARK 500 VAL B 244 23.4 L L OUTSIDE RANGE
REMARK 500 HIS B 249 24.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 496 DISTANCE = 7.15 ANGSTROMS
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 C11 B 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C11 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C11 B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PSC RELATED DB: PDB
REMARK 900 NATIVE ORTHOGONAL CRYSTAL
REMARK 900 RELATED ID: 4PSD RELATED DB: PDB
REMARK 900 NATIVE OHEXAGONAL CRYSTAL
DBREF 4PSE A 45 248 UNP G0RH85 G0RH85_HYPJQ 1 204
DBREF 4PSE B 45 248 UNP G0RH85 G0RH85_HYPJQ 1 204
SEQADV 4PSE MET A 1 UNP G0RH85 INITIATING METHIONINE
SEQADV 4PSE ARG A 2 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER A 3 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU A 4 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA A 5 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ILE A 6 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU A 7 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE THR A 8 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE THR A 9 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU A 10 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU A 11 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA A 12 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLY A 13 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS A 14 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA A 15 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PHE A 16 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA A 17 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE TYR A 18 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO A 19 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LYS A 20 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO A 21 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA A 22 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO A 23 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLN A 24 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER A 25 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE VAL A 26 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ASN A 27 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ARG A 28 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ARG A 29 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ASP A 30 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE TRP A 31 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO A 32 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER A 33 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ILE A 34 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ASN A 35 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLU A 36 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PHE A 37 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU A 38 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER A 39 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLU A 40 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU A 41 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA A 42 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LYS A 43 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE VAL A 44 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS A 249 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS A 250 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS A 251 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS A 252 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS A 253 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS A 254 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE MET B 1 UNP G0RH85 INITIATING METHIONINE
SEQADV 4PSE ARG B 2 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER B 3 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU B 4 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA B 5 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ILE B 6 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU B 7 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE THR B 8 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE THR B 9 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU B 10 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU B 11 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA B 12 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLY B 13 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS B 14 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA B 15 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PHE B 16 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA B 17 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE TYR B 18 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO B 19 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LYS B 20 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO B 21 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA B 22 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO B 23 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLN B 24 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER B 25 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE VAL B 26 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ASN B 27 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ARG B 28 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ARG B 29 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ASP B 30 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE TRP B 31 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PRO B 32 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER B 33 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ILE B 34 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ASN B 35 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLU B 36 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE PHE B 37 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU B 38 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE SER B 39 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE GLU B 40 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LEU B 41 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE ALA B 42 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE LYS B 43 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE VAL B 44 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS B 249 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS B 250 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS B 251 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS B 252 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS B 253 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSE HIS B 254 UNP G0RH85 EXPRESSION TAG
SEQRES 1 A 254 MET ARG SER LEU ALA ILE LEU THR THR LEU LEU ALA GLY
SEQRES 2 A 254 HIS ALA PHE ALA TYR PRO LYS PRO ALA PRO GLN SER VAL
SEQRES 3 A 254 ASN ARG ARG ASP TRP PRO SER ILE ASN GLU PHE LEU SER
SEQRES 4 A 254 GLU LEU ALA LYS VAL MET PRO ILE GLY ASP THR ILE THR
SEQRES 5 A 254 ALA ALA CYS ASP LEU ILE SER ASP GLY GLU ASP ALA ALA
SEQRES 6 A 254 ALA SER LEU PHE GLY ILE SER GLU THR GLU ASN ASP PRO
SEQRES 7 A 254 CYS GLY ASP VAL THR VAL LEU PHE ALA ARG GLY THR CYS
SEQRES 8 A 254 ASP PRO GLY ASN VAL GLY VAL LEU VAL GLY PRO TRP PHE
SEQRES 9 A 254 PHE ASP SER LEU GLN THR ALA LEU GLY SER ARG THR LEU
SEQRES 10 A 254 GLY VAL LYS GLY VAL PRO TYR PRO ALA SER VAL GLN ASP
SEQRES 11 A 254 PHE LEU SER GLY SER VAL GLN ASN GLY ILE ASN MET ALA
SEQRES 12 A 254 ASN GLN ILE LYS SER VAL LEU GLN SER CYS PRO ASN THR
SEQRES 13 A 254 LYS LEU VAL LEU GLY GLY TYR SER GLN GLY SER MET VAL
SEQRES 14 A 254 VAL HIS ASN ALA ALA SER ASN LEU ASP ALA ALA THR MET
SEQRES 15 A 254 SER LYS ILE SER ALA VAL VAL LEU PHE GLY ASP PRO TYR
SEQRES 16 A 254 TYR GLY LYS PRO VAL ALA ASN PHE ASP ALA ALA LYS THR
SEQRES 17 A 254 LEU VAL VAL CYS HIS ASP GLY ASP ASN ILE CYS GLN GLY
SEQRES 18 A 254 GLY ASP ILE ILE LEU LEU PRO HIS LEU THR TYR ALA GLU
SEQRES 19 A 254 ASP ALA ASP THR ALA ALA ALA PHE VAL VAL PRO LEU VAL
SEQRES 20 A 254 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 254 MET ARG SER LEU ALA ILE LEU THR THR LEU LEU ALA GLY
SEQRES 2 B 254 HIS ALA PHE ALA TYR PRO LYS PRO ALA PRO GLN SER VAL
SEQRES 3 B 254 ASN ARG ARG ASP TRP PRO SER ILE ASN GLU PHE LEU SER
SEQRES 4 B 254 GLU LEU ALA LYS VAL MET PRO ILE GLY ASP THR ILE THR
SEQRES 5 B 254 ALA ALA CYS ASP LEU ILE SER ASP GLY GLU ASP ALA ALA
SEQRES 6 B 254 ALA SER LEU PHE GLY ILE SER GLU THR GLU ASN ASP PRO
SEQRES 7 B 254 CYS GLY ASP VAL THR VAL LEU PHE ALA ARG GLY THR CYS
SEQRES 8 B 254 ASP PRO GLY ASN VAL GLY VAL LEU VAL GLY PRO TRP PHE
SEQRES 9 B 254 PHE ASP SER LEU GLN THR ALA LEU GLY SER ARG THR LEU
SEQRES 10 B 254 GLY VAL LYS GLY VAL PRO TYR PRO ALA SER VAL GLN ASP
SEQRES 11 B 254 PHE LEU SER GLY SER VAL GLN ASN GLY ILE ASN MET ALA
SEQRES 12 B 254 ASN GLN ILE LYS SER VAL LEU GLN SER CYS PRO ASN THR
SEQRES 13 B 254 LYS LEU VAL LEU GLY GLY TYR SER GLN GLY SER MET VAL
SEQRES 14 B 254 VAL HIS ASN ALA ALA SER ASN LEU ASP ALA ALA THR MET
SEQRES 15 B 254 SER LYS ILE SER ALA VAL VAL LEU PHE GLY ASP PRO TYR
SEQRES 16 B 254 TYR GLY LYS PRO VAL ALA ASN PHE ASP ALA ALA LYS THR
SEQRES 17 B 254 LEU VAL VAL CYS HIS ASP GLY ASP ASN ILE CYS GLN GLY
SEQRES 18 B 254 GLY ASP ILE ILE LEU LEU PRO HIS LEU THR TYR ALA GLU
SEQRES 19 B 254 ASP ALA ASP THR ALA ALA ALA PHE VAL VAL PRO LEU VAL
SEQRES 20 B 254 SER HIS HIS HIS HIS HIS HIS
HET C11 A 301 18
HET BOG A 302 20
HET BOG A 303 20
HET C11 B 301 17
HETNAM C11 UNDECYL-PHOSPHINIC ACID BUTYL ESTER
HETNAM BOG B-OCTYLGLUCOSIDE
FORMUL 3 C11 2(C15 H33 O2 P)
FORMUL 4 BOG 2(C14 H28 O6)
FORMUL 7 HOH *194(H2 O)
HELIX 1 1 TRP A 31 ALA A 42 1 12
HELIX 2 2 PRO A 46 GLY A 70 1 25
HELIX 3 3 VAL A 100 GLY A 113 1 14
HELIX 4 4 SER A 127 GLY A 134 1 8
HELIX 5 5 SER A 135 CYS A 153 1 19
HELIX 6 6 SER A 164 ASN A 176 1 13
HELIX 7 7 ASP A 178 SER A 183 1 6
HELIX 8 8 ASP A 204 ALA A 206 5 3
HELIX 9 9 LEU A 226 THR A 231 1 6
HELIX 10 10 TYR A 232 GLU A 234 5 3
HELIX 11 11 ASP A 235 VAL A 247 1 13
HELIX 12 12 PRO B 32 ALA B 42 1 11
HELIX 13 13 ASP B 49 GLY B 70 1 22
HELIX 14 14 VAL B 100 GLY B 113 1 14
HELIX 15 15 SER B 127 GLY B 134 1 8
HELIX 16 16 SER B 135 CYS B 153 1 19
HELIX 17 17 SER B 164 LEU B 177 1 14
HELIX 18 18 ASP B 178 SER B 183 1 6
HELIX 19 19 ASP B 204 ALA B 206 5 3
HELIX 20 20 ASP B 216 GLY B 221 5 6
HELIX 21 21 LEU B 226 THR B 231 1 6
HELIX 22 22 TYR B 232 GLU B 234 5 3
HELIX 23 23 ASP B 235 VAL B 247 1 13
SHEET 1 A 5 LEU A 117 GLY A 121 0
SHEET 2 A 5 VAL A 82 ALA A 87 1 N VAL A 84 O LYS A 120
SHEET 3 A 5 LYS A 157 TYR A 163 1 O VAL A 159 N THR A 83
SHEET 4 A 5 ILE A 185 PHE A 191 1 O PHE A 191 N GLY A 162
SHEET 5 A 5 THR A 208 VAL A 211 1 O VAL A 211 N LEU A 190
SHEET 1 B 5 LEU B 117 GLY B 121 0
SHEET 2 B 5 VAL B 82 ALA B 87 1 N VAL B 84 O LYS B 120
SHEET 3 B 5 LYS B 157 TYR B 163 1 O VAL B 159 N THR B 83
SHEET 4 B 5 ILE B 185 PHE B 191 1 O PHE B 191 N GLY B 162
SHEET 5 B 5 THR B 208 VAL B 211 1 O VAL B 211 N LEU B 190
SSBOND 1 CYS A 55 CYS A 91 1555 1555 2.05
SSBOND 2 CYS A 79 CYS A 153 1555 1555 2.05
SSBOND 3 CYS A 212 CYS A 219 1555 1555 2.06
SSBOND 4 CYS B 55 CYS B 91 1555 1555 2.05
SSBOND 5 CYS B 79 CYS B 153 1555 1555 2.04
SSBOND 6 CYS B 212 CYS B 219 1555 1555 2.03
LINK OG SER B 164 P C11 B 301 1555 1555 1.53
LINK OG SER A 164 P C11 A 301 1555 1555 1.63
CISPEP 1 SER A 248 HIS A 249 0 -17.08
CISPEP 2 HIS A 249 HIS A 250 0 -5.10
SITE 1 AC1 9 ILE A 58 GLU A 62 THR A 90 PHE A 131
SITE 2 AC1 9 SER A 164 GLN A 165 ILE A 225 HIS A 229
SITE 3 AC1 9 BOG A 302
SITE 1 AC2 7 ASP A 223 ILE A 225 C11 A 301 HOH A 553
SITE 2 AC2 7 ASP B 223 ILE B 225 C11 B 301
SITE 1 AC3 7 TRP A 103 LEU A 230 ALA A 233 GLU A 234
SITE 2 AC3 7 HOH A 456 HOH A 478 HOH A 511
SITE 1 AC4 8 BOG A 302 THR B 90 PHE B 131 SER B 164
SITE 2 AC4 8 GLN B 165 ILE B 218 ILE B 225 HIS B 229
CRYST1 49.043 37.544 133.009 90.00 97.38 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020390 0.000000 0.002641 0.00000
SCALE2 0.000000 0.026635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007581 0.00000
TER 1596 HIS A 250
TER 3192 HIS B 249
MASTER 710 0 4 23 10 0 9 6 3451 2 89 40
END |