HEADER HYDROLASE 25-DEC-17 6FDK
TITLE STRUCTURE OF CHLAMYDIA TRACHOMATIS EFFECTOR PROTEIN CDU1 BOUND TO
TITLE 2 UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEUBIQUITINASE AND DENEDDYLASE DUB1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHLADUB1;
COMPND 5 EC: 3.4.22.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: POLYUBIQUITIN-B;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDIA TRACHOMATIS 434/BU;
SOURCE 3 ORGANISM_TAXID: 471472;
SOURCE 4 GENE: CDU1, CTL0247;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: UBB;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS CHLADUB1, CE PROTEASE, DUB, UBIQUITIN., HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.RAMIREZ,C.KISKER
REVDAT 4 07-FEB-24 6FDK 1 REMARK
REVDAT 3 15-MAR-23 6FDK 1 COMPND SOURCE REMARK DBREF
REVDAT 3 2 1 SEQRES LINK ATOM
REVDAT 2 17-OCT-18 6FDK 1 JRNL
REVDAT 1 15-AUG-18 6FDK 0
JRNL AUTH Y.A.RAMIREZ,T.B.ADLER,E.ALTMANN,T.KLEMM,C.TIESMEYER,F.SAUER,
JRNL AUTH 2 S.G.KATHMAN,A.V.STATSYUK,C.SOTRIFFER,C.KISKER
JRNL TITL STRUCTURAL BASIS OF SUBSTRATE RECOGNITION AND COVALENT
JRNL TITL 2 INHIBITION OF CDU1 FROM CHLAMYDIA TRACHOMATIS.
JRNL REF CHEMMEDCHEM V. 13 2014 2018
JRNL REFN ESSN 1860-7187
JRNL PMID 30028574
JRNL DOI 10.1002/CMDC.201800364
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 39198
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2021
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2895
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.6290
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.6760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2543
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 423
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : 0.12000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.092
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.092
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.352
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2642 ; 0.030 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2501 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3594 ; 2.530 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5833 ; 1.287 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 6.224 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 116 ;35.692 ;24.569
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 473 ;14.169 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;14.026 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 403 ; 0.190 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2881 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 517 ; 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): 1276 ; 1.640 ; 1.778
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1275 ; 1.638 ; 1.778
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1594 ; 2.301 ; 2.665
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1595 ; 2.300 ; 2.665
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1366 ; 3.047 ; 2.091
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1367 ; 3.046 ; 2.091
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1996 ; 4.544 ; 2.998
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2953 ; 6.377 ;22.952
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2954 ; 6.376 ;22.948
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 : 12
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 162 A 198
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1819 -61.2663 73.2128
REMARK 3 T TENSOR
REMARK 3 T11: 0.0503 T22: 0.0396
REMARK 3 T33: 0.0132 T12: 0.0034
REMARK 3 T13: -0.0034 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.9189 L22: 0.3147
REMARK 3 L33: 0.0099 L12: 0.2247
REMARK 3 L13: -0.0019 L23: -0.0209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: 0.0772 S13: 0.0951
REMARK 3 S21: -0.0119 S22: 0.0028 S23: 0.0218
REMARK 3 S31: -0.0013 S32: 0.0170 S33: -0.0082
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 199 A 282
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8426 -71.6318 71.0511
REMARK 3 T TENSOR
REMARK 3 T11: 0.0494 T22: 0.0266
REMARK 3 T33: 0.0018 T12: 0.0089
REMARK 3 T13: -0.0026 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.5858 L22: 0.1195
REMARK 3 L33: 0.1634 L12: -0.0586
REMARK 3 L13: 0.2468 L23: -0.1068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.0267 S13: -0.0284
REMARK 3 S21: -0.0079 S22: -0.0033 S23: -0.0030
REMARK 3 S31: 0.0097 S32: 0.0144 S33: -0.0062
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 283 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2645 -77.3230 79.6119
REMARK 3 T TENSOR
REMARK 3 T11: 0.0358 T22: 0.0303
REMARK 3 T33: 0.0217 T12: -0.0004
REMARK 3 T13: -0.0083 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.7425 L22: 0.4890
REMARK 3 L33: 0.9708 L12: -0.5264
REMARK 3 L13: 0.7170 L23: -0.3827
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: -0.0272 S13: -0.0983
REMARK 3 S21: 0.0130 S22: 0.0520 S23: 0.0786
REMARK 3 S31: 0.0123 S32: -0.0266 S33: -0.0736
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 332 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2576 -56.8461 77.3477
REMARK 3 T TENSOR
REMARK 3 T11: 0.0510 T22: 0.0076
REMARK 3 T33: 0.0512 T12: 0.0121
REMARK 3 T13: 0.0176 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.7947 L22: 0.2925
REMARK 3 L33: 0.1185 L12: 0.0694
REMARK 3 L13: 0.0390 L23: -0.1418
REMARK 3 S TENSOR
REMARK 3 S11: 0.0630 S12: -0.0168 S13: 0.1355
REMARK 3 S21: 0.0396 S22: -0.0113 S23: 0.0625
REMARK 3 S31: -0.0119 S32: -0.0070 S33: -0.0516
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 155 B 198
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 199 B 215
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 216 B 238
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 239 B 254
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 : B 255 B 282
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 : B 283 B 331
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 : B 332 B 371
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 : B 372 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0269
REMARK 3 T33: 0.0269 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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
REMARK 4
REMARK 4 6FDK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1200008135.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : 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) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41326
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 46.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.320
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: 5B5Q
REMARK 200
REMARK 200 REMARK: BLADE LIKE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 12% PEG 20000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 28.46850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 136
REMARK 465 LYS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 HIS A 141
REMARK 465 HIS A 142
REMARK 465 HIS A 143
REMARK 465 SER A 144
REMARK 465 ALA A 145
REMARK 465 GLY A 146
REMARK 465 LEU A 147
REMARK 465 GLU A 148
REMARK 465 VAL A 149
REMARK 465 LEU A 150
REMARK 465 PHE A 151
REMARK 465 GLN A 152
REMARK 465 GLY A 153
REMARK 465 PRO A 154
REMARK 465 ARG A 155
REMARK 465 ARG A 156
REMARK 465 GLN A 157
REMARK 465 THR A 158
REMARK 465 ILE A 159
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NE2 GLN A 237 O HOH A 601 2.07
REMARK 500 O HOH A 649 O HOH A 834 2.10
REMARK 500 O HOH A 609 O HOH A 750 2.11
REMARK 500 O HOH A 614 O HOH A 754 2.13
REMARK 500 O HOH A 697 O HOH A 834 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 189 CD GLU A 189 OE1 0.102
REMARK 500 GLU A 217 CD GLU A 217 OE1 0.075
REMARK 500 TYR A 232 CZ TYR A 232 CE2 0.078
REMARK 500 SER A 256 CA SER A 256 CB 0.103
REMARK 500 LEU A 288 C LEU A 288 O 0.117
REMARK 500 SER A 324 N SER A 324 CA 0.450
REMARK 500 SER A 324 CA SER A 324 CB 0.141
REMARK 500 SER A 324 CB SER A 324 OG 0.091
REMARK 500 ASP A 367 CB ASP A 367 CG 0.133
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 ASP A 169 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 PHE A 191 CB - CG - CD2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 LEU A 277 CB - CG - CD1 ANGL. DEV. = 18.8 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 287 CD - NE - CZ ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG A 287 NE - CZ - NH1 ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG A 287 NE - CZ - NH2 ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASP A 323 O - C - N ANGL. DEV. = -12.7 DEGREES
REMARK 500 SER A 324 C - N - CA ANGL. DEV. = -29.2 DEGREES
REMARK 500 SER A 324 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 SER A 324 N - CA - CB ANGL. DEV. = 22.8 DEGREES
REMARK 500 ASP A 359 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 367 CB - CG - OD1 ANGL. DEV. = 6.9 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 TYR A 295 -50.66 72.68
REMARK 500 ASN A 296 34.38 -142.71
REMARK 500 SER A 324 -23.98 99.14
REMARK 500 ASP A 359 108.87 -162.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 287 0.09 SIDE CHAIN
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 CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AYE A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5B5Q RELATED DB: PDB
REMARK 900 LIGAND-FREE PROTEIN
REMARK 900 RELATED ID: 5HAG RELATED DB: PDB
REMARK 900 LIGAND-FREE PROTEIN
DBREF 6FDK A 155 401 UNP B0B9A0 CDUB1_CHLT2 155 401
DBREF 6FDK B 1 75 UNP P0CG47 UBB_HUMAN 1 75
SEQADV 6FDK MET A 136 UNP B0B9A0 INITIATING METHIONINE
SEQADV 6FDK LYS A 137 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK HIS A 138 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK HIS A 139 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK HIS A 140 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK HIS A 141 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK HIS A 142 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK HIS A 143 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK SER A 144 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK ALA A 145 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK GLY A 146 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK LEU A 147 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK GLU A 148 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK VAL A 149 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK LEU A 150 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK PHE A 151 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK GLN A 152 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK GLY A 153 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK PRO A 154 UNP B0B9A0 EXPRESSION TAG
SEQADV 6FDK ALA A 174 UNP B0B9A0 CYS 174 ENGINEERED MUTATION
SEQADV 6FDK SER A 226 UNP B0B9A0 CYS 226 ENGINEERED MUTATION
SEQADV 6FDK ALA A 386 UNP B0B9A0 CYS 386 ENGINEERED MUTATION
SEQRES 1 A 266 MET LYS HIS HIS HIS HIS HIS HIS SER ALA GLY LEU GLU
SEQRES 2 A 266 VAL LEU PHE GLN GLY PRO ARG ARG GLN THR ILE GLU ALA
SEQRES 3 A 266 LEU VAL PRO ALA TRP ASP SER ASP ILE ILE PHE LYS ALA
SEQRES 4 A 266 LEU CYS TYR PHE HIS THR LEU TYR PRO GLY LEU ILE PRO
SEQRES 5 A 266 LEU GLU THR PHE PRO PRO ALA THR ILE PHE ASN PHE LYS
SEQRES 6 A 266 GLN LYS ILE ILE SER ILE LEU GLU ASP LYS LYS ALA VAL
SEQRES 7 A 266 LEU ARG GLY GLU PRO ILE LYS GLY PRO LEU PRO ILE SER
SEQRES 8 A 266 CYS SER LYS GLU ASN TYR ARG ARG HIS LEU GLN ARG THR
SEQRES 9 A 266 THR LEU LEU PRO VAL PHE MET TRP TYR HIS PRO THR PRO
SEQRES 10 A 266 LYS THR LEU SER ASP THR MET GLN THR MET LYS GLN LEU
SEQRES 11 A 266 ALA ILE LYS GLY SER VAL GLY ALA SER HIS TRP LEU LEU
SEQRES 12 A 266 VAL ILE VAL ASP ILE GLN ALA ARG ARG LEU VAL TYR PHE
SEQRES 13 A 266 ASP SER LEU TYR ASN TYR VAL MET PRO PRO GLU ASN MET
SEQRES 14 A 266 LYS LYS GLU LEU GLN SER PHE ALA GLN GLN LEU ASP GLN
SEQRES 15 A 266 VAL TYR PRO ALA TYR ASP SER LYS LYS PHE SER VAL LYS
SEQRES 16 A 266 ILE ALA ALA LYS GLU VAL ILE GLN ARG GLY SER GLY SER
SEQRES 17 A 266 SER CYS GLY ALA TRP CYS CYS GLN PHE LEU HIS TRP TYR
SEQRES 18 A 266 LEU LYS ASP PRO LEU THR ASP ALA LEU ASN ASP LEU PRO
SEQRES 19 A 266 VAL ASP SER VAL GLU ARG HIS GLU ASN LEU ALA SER PHE
SEQRES 20 A 266 VAL GLN ALA ALA GLU ALA ALA VAL GLN ASP LEU PRO GLU
SEQRES 21 A 266 LEU SER TRP PRO GLU ALA
SEQRES 1 B 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
HET CL A 501 1
HET AYE A 502 4
HETNAM CL CHLORIDE ION
HETNAM AYE PROP-2-EN-1-AMINE
HETSYN AYE ALLYLAMINE
FORMUL 3 CL CL 1-
FORMUL 4 AYE C3 H7 N
FORMUL 5 HOH *423(H2 O)
HELIX 1 AA1 ASP A 167 TYR A 182 1 16
HELIX 2 AA2 ASN A 198 ARG A 215 1 18
HELIX 3 AA3 SER A 228 THR A 239 1 12
HELIX 4 AA4 THR A 254 GLY A 269 1 16
HELIX 5 AA5 PRO A 300 TYR A 319 1 20
HELIX 6 AA6 SER A 344 ASP A 359 1 16
HELIX 7 AA7 ASP A 363 ASP A 367 5 5
HELIX 8 AA8 ASP A 371 GLN A 391 1 21
HELIX 9 AA9 THR B 22 GLY B 35 1 14
HELIX 10 AB1 PRO B 37 GLN B 41 5 5
HELIX 11 AB2 THR B 55 ASN B 60 5 6
SHEET 1 AA1 4 LEU A 241 TYR A 248 0
SHEET 2 AA1 4 HIS A 275 ASP A 282 -1 O LEU A 277 N MET A 246
SHEET 3 AA1 4 ARG A 287 PHE A 291 -1 O ARG A 287 N ASP A 282
SHEET 4 AA1 4 SER A 328 ILE A 331 1 O LYS A 330 N LEU A 288
SHEET 1 AA2 5 THR B 12 GLU B 16 0
SHEET 2 AA2 5 GLN B 2 LYS B 6 -1 N VAL B 5 O ILE B 13
SHEET 3 AA2 5 THR B 66 VAL B 70 1 O LEU B 67 N PHE B 4
SHEET 4 AA2 5 ARG B 42 PHE B 45 -1 N ARG B 42 O VAL B 70
SHEET 5 AA2 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
LINK SG CYS A 345 C2 AYE A 502 1555 1555 1.76
LINK N1 AYE A 502 C GLY B 75 1555 1555 1.36
CISPEP 1 PHE A 191 PRO A 192 0 5.97
CISPEP 2 GLY A 221 PRO A 222 0 3.37
SITE 1 AC1 5 PRO A 183 LEU A 185 ILE A 186 HIS A 235
SITE 2 AC1 5 THR A 239
SITE 1 AC2 6 VAL A 271 SER A 274 HIS A 275 GLY A 342
SITE 2 AC2 6 CYS A 345 GLY B 75
CRYST1 47.815 56.937 60.695 90.00 104.86 90.00 P 1 21 1 2
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 0.020914 0.000000 0.005550 0.00000
SCALE2 0.000000 0.017563 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017046 0.00000
(ATOM LINES ARE NOT SHOWN.)
END