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HEADER HYDROLASE 23-MAY-13 4BP8
TITLE OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI - OPEN FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGOPEPTIDASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.83;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PRARE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYDROLASE, PROLYL OLIGOPEPTIDASE, CATALYTIC REGULATION, INDUCED FIT
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CANNING,D.REA,R.MORTY,V.FULOP
REVDAT 1 12-FEB-14 4BP8 0
JRNL AUTH P.CANNING,D.REA,R.E.MORTY,V.FULOP
JRNL TITL CRYSTAL STRUCTURES OF TRYPANOSOMA BRUCEI OLIGOPEPTIDASE B
JRNL TITL 2 BROADEN THE PARADIGM OF CATALYTIC REGULATION IN PROLYL
JRNL TITL 3 OLIGOPEPTIDASE FAMILY ENZYMES.
JRNL REF PLOS ONE V. 8E79349 2013
JRNL REFN ISSN 1932-6203
JRNL PMID 24265767
JRNL DOI 10.1371/JOURNAL.PONE.0079349
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.31
REMARK 3 NUMBER OF REFLECTIONS : 83463
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) : 0.18625
REMARK 3 R VALUE (WORKING SET) : 0.18402
REMARK 3 FREE R VALUE : 0.23885
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3521
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) : 2.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.462
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5723
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.333
REMARK 3 BIN FREE R VALUE SET COUNT : 237
REMARK 3 BIN FREE R VALUE : 0.382
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11030
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 272
REMARK 3 SOLVENT ATOMS : 778
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.311
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.95
REMARK 3 B22 (A**2) : 1.95
REMARK 3 B33 (A**2) : -2.93
REMARK 3 B12 (A**2) : 0.98
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.263
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.257
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11578 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15712 ; 1.721 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1422 ; 7.639 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 540 ;34.226 ;23.259
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1944 ;18.324 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;19.688 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1708 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8880 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 7092 ; 0.677 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11486 ; 1.325 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4486 ; 2.322 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4226 ; 3.754 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 86
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1824 34.5650 57.5539
REMARK 3 T TENSOR
REMARK 3 T11: 0.2023 T22: 0.1962
REMARK 3 T33: 0.2001 T12: -0.0261
REMARK 3 T13: -0.0689 T23: 0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 0.7157 L22: 1.4880
REMARK 3 L33: 1.4322 L12: 0.3085
REMARK 3 L13: 0.1191 L23: -0.4252
REMARK 3 S TENSOR
REMARK 3 S11: 0.2286 S12: -0.0920 S13: -0.2765
REMARK 3 S21: 0.0937 S22: -0.0380 S23: 0.1160
REMARK 3 S31: 0.3832 S32: -0.1460 S33: -0.1906
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 87 A 441
REMARK 3 ORIGIN FOR THE GROUP (A): 41.5583 72.0457 76.7906
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: 0.1556
REMARK 3 T33: 0.0737 T12: -0.0972
REMARK 3 T13: 0.0295 T23: -0.0906
REMARK 3 L TENSOR
REMARK 3 L11: 2.3549 L22: 0.3787
REMARK 3 L33: 0.8422 L12: -0.2039
REMARK 3 L13: 0.0982 L23: -0.0661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0742 S12: -0.3533 S13: 0.2363
REMARK 3 S21: 0.0849 S22: -0.0427 S23: -0.0440
REMARK 3 S31: -0.0802 S32: -0.0016 S33: -0.0316
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 442 A 714
REMARK 3 ORIGIN FOR THE GROUP (A): 62.3927 49.8037 59.5682
REMARK 3 T TENSOR
REMARK 3 T11: 0.0430 T22: 0.1541
REMARK 3 T33: 0.0390 T12: -0.0299
REMARK 3 T13: -0.0115 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 0.7439 L22: 0.6689
REMARK 3 L33: 0.8146 L12: 0.2446
REMARK 3 L13: 0.1104 L23: 0.0587
REMARK 3 S TENSOR
REMARK 3 S11: 0.1538 S12: -0.1333 S13: -0.0120
REMARK 3 S21: 0.1251 S22: -0.0952 S23: -0.0470
REMARK 3 S31: 0.0303 S32: -0.0120 S33: -0.0585
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 : B 3 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): 66.2990 40.4327 20.2049
REMARK 3 T TENSOR
REMARK 3 T11: 0.0993 T22: 0.1429
REMARK 3 T33: 0.0527 T12: 0.0387
REMARK 3 T13: -0.0305 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.0354 L22: 0.9160
REMARK 3 L33: 2.0705 L12: -0.2444
REMARK 3 L13: 0.4892 L23: 0.1954
REMARK 3 S TENSOR
REMARK 3 S11: 0.1912 S12: 0.1663 S13: -0.1731
REMARK 3 S21: -0.1258 S22: -0.0566 S23: 0.0014
REMARK 3 S31: 0.3694 S32: 0.0465 S33: -0.1345
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 87 B 441
REMARK 3 ORIGIN FOR THE GROUP (A): 78.9573 82.2872 13.9637
REMARK 3 T TENSOR
REMARK 3 T11: 0.1897 T22: 0.1038
REMARK 3 T33: 0.1227 T12: 0.0929
REMARK 3 T13: 0.0495 T23: 0.0936
REMARK 3 L TENSOR
REMARK 3 L11: 2.2018 L22: 0.6163
REMARK 3 L33: 0.9038 L12: 0.2871
REMARK 3 L13: -0.1250 L23: -0.0688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0342 S12: 0.1278 S13: 0.2793
REMARK 3 S21: -0.0945 S22: 0.0288 S23: 0.0794
REMARK 3 S31: -0.1938 S32: -0.0160 S33: -0.0630
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 442 B 714
REMARK 3 ORIGIN FOR THE GROUP (A): 58.2224 55.7647 22.9658
REMARK 3 T TENSOR
REMARK 3 T11: 0.0514 T22: 0.1777
REMARK 3 T33: 0.0723 T12: 0.0621
REMARK 3 T13: -0.0189 T23: 0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 0.7719 L22: 0.7067
REMARK 3 L33: 0.9041 L12: -0.3627
REMARK 3 L13: 0.1377 L23: -0.0072
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: 0.1770 S13: 0.0664
REMARK 3 S21: -0.0869 S22: -0.0764 S23: 0.0841
REMARK 3 S31: -0.0364 S32: -0.0502 S33: -0.0295
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4BP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-13.
REMARK 100 THE PDBE ID CODE IS EBI-56991.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86984
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 66.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 34.6
REMARK 200 R MERGE (I) : 0.17
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 22.2
REMARK 200 R MERGE FOR SHELL (I) : 1.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE,RESOLVE
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% (W/V) POLYETHYLENE GLYCOL
REMARK 280 6000, 1M LITHIUM CHLORIDE, 100MM BIS-TRIS PROPANE, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 166.09333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.04667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 83.04667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 166.09333
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 MSE A 1
REMARK 465 GLN A 2
REMARK 465 MSE B 1
REMARK 465 GLN B 2
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 LYS A 715 CA C O CB CG CD CE NZ
REMARK 470 LYS B 715 CA C O CB CG CD CE NZ
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 NH2 ARG A 354 OE2 GLU A 490 2.19
REMARK 500 O HOH A 2114 O HOH A 2116 2.07
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 CYS A 151 CB CYS A 151 SG -0.109
REMARK 500 ASP B 209 CB ASP B 209 CG 0.162
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 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PRO A 157 C - N - CA ANGL. DEV. = 23.2 DEGREES
REMARK 500 PRO A 157 C - N - CD ANGL. DEV. = -31.4 DEGREES
REMARK 500 CYS A 169 CA - CB - SG ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG A 213 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 213 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 354 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 354 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LEU A 463 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 ARG A 576 NE - CZ - NH1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 576 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 49 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 49 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 PRO B 157 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 PRO B 157 C - N - CD ANGL. DEV. = -20.6 DEGREES
REMARK 500 LEU B 463 CA - CB - CG ANGL. DEV. = 22.2 DEGREES
REMARK 500 TYR B 482 CA - C - N ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG B 710 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASN A 29 51.54 -149.78
REMARK 500 ASP A 99 -122.74 48.67
REMARK 500 ALA A 121 -57.58 -18.20
REMARK 500 CYS A 151 134.76 -174.91
REMARK 500 PRO A 156 173.52 -59.42
REMARK 500 PRO A 157 -69.42 35.74
REMARK 500 VAL A 179 108.71 -45.43
REMARK 500 ASP A 185 132.07 -34.20
REMARK 500 ASP A 209 -106.28 -124.47
REMARK 500 VAL A 282 -90.49 -84.10
REMARK 500 ARG A 285 114.36 -4.40
REMARK 500 PRO A 368 18.75 -65.00
REMARK 500 LEU A 377 113.22 -38.53
REMARK 500 PHE A 387 -174.65 -172.80
REMARK 500 VAL A 392 77.87 -112.21
REMARK 500 ASP A 400 46.56 -106.47
REMARK 500 TYR A 482 -75.84 -102.44
REMARK 500 TYR A 485 12.53 55.77
REMARK 500 PRO A 491 46.37 -73.80
REMARK 500 TYR A 523 -61.71 -94.67
REMARK 500 TYR A 529 -120.52 50.07
REMARK 500 SER A 563 -116.19 69.57
REMARK 500 VAL A 587 60.44 29.38
REMARK 500 ASP A 591 57.40 -96.58
REMARK 500 GLU A 610 -60.45 -104.96
REMARK 500 SER A 687 -89.93 -20.48
REMARK 500 ASP A 688 -13.33 109.27
REMARK 500 ARG A 689 -49.44 79.74
REMARK 500 ASN A 708 42.02 70.41
REMARK 500 ASP B 99 -128.84 46.60
REMARK 500 ARG B 118 140.44 -170.97
REMARK 500 ALA B 121 -38.94 -31.79
REMARK 500 GLU B 142 110.42 -34.67
REMARK 500 PRO B 156 166.77 -46.12
REMARK 500 PRO B 157 -64.44 33.11
REMARK 500 ARG B 180 94.56 -53.82
REMARK 500 ASP B 209 -121.44 -103.25
REMARK 500 PRO B 238 -8.79 -55.72
REMARK 500 VAL B 282 -90.45 -81.90
REMARK 500 ARG B 285 111.38 -13.48
REMARK 500 ASN B 370 27.96 83.94
REMARK 500 PHE B 372 136.02 -38.16
REMARK 500 PHE B 387 -178.96 -176.68
REMARK 500 TYR B 482 -76.18 -96.90
REMARK 500 TYR B 485 -0.67 68.97
REMARK 500 ASP B 502 -1.57 -55.67
REMARK 500 TYR B 529 -129.36 46.12
REMARK 500 SER B 563 -112.45 62.22
REMARK 500 VAL B 587 59.06 26.12
REMARK 500 ASP B 591 56.79 -100.71
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 156 PRO A 157 -120.28
REMARK 500 TYR A 482 GLY A 483 -53.60
REMARK 500 PRO B 156 PRO B 157 -123.48
REMARK 500 VAL B 179 ARG B 180 -117.33
REMARK 500 TYR B 482 GLY B 483 -53.65
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 ASP A 209 15.2 L L OUTSIDE RANGE
REMARK 500 VAL A 315 21.0 L L OUTSIDE RANGE
REMARK 500 ASP A 341 19.7 L L OUTSIDE RANGE
REMARK 500 GLN A 556 24.2 L L OUTSIDE RANGE
REMARK 500 ASP A 688 22.2 L L OUTSIDE RANGE
REMARK 500 ARG B 180 22.6 L L OUTSIDE RANGE
REMARK 500 ASP B 209 19.7 L L OUTSIDE RANGE
REMARK 500 VAL B 315 24.2 L L OUTSIDE RANGE
REMARK 500 ASP B 341 23.3 L L OUTSIDE RANGE
REMARK 500 ASP B 688 22.4 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BP9 RELATED DB: PDB
REMARK 900 OLIGOPEPTIDASE B FROM TRYPANOSOMA BRUCEI WITH COVALENTLY
REMARK 900 BOUND ANTIPAIN - CLOSED FORM
DBREF 4BP8 A 1 715 UNP O76728 O76728_TRYBB 1 715
DBREF 4BP8 B 1 715 UNP O76728 O76728_TRYBB 1 715
SEQRES 1 A 715 MSE GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 A 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 A 715 GLY ALA ASN PRO MSE ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 A 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 A 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 A 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 A 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 A 715 MSE SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 A 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 A 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 A 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 A 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 A 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 A 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 A 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 A 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 A 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 A 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 A 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 A 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MSE SER SER
SEQRES 21 A 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 A 715 VAL LYS HIS ASN THR LEU GLU MSE VAL ARG PRO ARG GLU
SEQRES 23 A 715 LYS GLY VAL ARG TYR THR VAL GLU MSE HIS GLY THR ASP
SEQRES 24 A 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 A 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 A 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 A 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 A 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 A 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 A 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 A 715 VAL VAL CYS SER GLN MSE LYS THR TYR ASP ALA SER LEU
SEQRES 32 A 715 LEU ARG LEU ARG TYR SER SER MSE THR THR PRO THR VAL
SEQRES 33 A 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 A 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 A 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 A 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 A 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MSE LEU TYR GLY
SEQRES 38 A 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 A 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MSE ILE TYR
SEQRES 40 A 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MSE GLY ARG
SEQRES 41 A 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 A 715 ASN THR PHE MSE ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 A 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 A 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 A 715 LEU ASN MSE ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 A 715 GLY VAL PRO PHE VAL ASP VAL MSE THR THR MSE CYS ASP
SEQRES 47 A 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 A 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MSE ASN
SEQRES 49 A 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 A 715 PRO HIS LEU MSE ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 A 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 A 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 A 715 MSE ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 A 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 A 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
SEQRES 1 B 715 MSE GLN THR GLU ARG GLY PRO ILE ALA ALA HIS ARG PRO
SEQRES 2 B 715 HIS GLU VAL VAL PHE GLY LYS VAL GLU GLY GLU ASP ARG
SEQRES 3 B 715 GLY ALA ASN PRO MSE ASP PRO PRO ARG ARG ARG VAL ASP
SEQRES 4 B 715 PRO LEU PHE TRP LEU ARG ASP ASP ASN ARG ALA ASP PRO
SEQRES 5 B 715 GLU VAL LEU ALA HIS LEU HIS LEU GLU LYS ASP TYR TYR
SEQRES 6 B 715 GLU LYS ARG ALA VAL ASP ILE LYS ASP LEU ALA GLU THR
SEQRES 7 B 715 ILE TYR GLN GLU HIS ILE SER HIS ILE GLU GLU THR ASP
SEQRES 8 B 715 MSE SER ALA PRO TYR VAL TYR ASP ARG PHE LEU TYR TYR
SEQRES 9 B 715 THR ARG ASP VAL LYS GLY LEU SER TYR LYS LEU HIS CYS
SEQRES 10 B 715 ARG VAL PRO ALA GLY LYS THR PRO GLY GLU GLY GLU ASP
SEQRES 11 B 715 GLU GLU ILE VAL LEU ASP GLU ASN LYS LEU ALA GLU GLY
SEQRES 12 B 715 LYS SER PHE CYS VAL VAL GLY CYS VAL ALA PRO ALA PRO
SEQRES 13 B 715 PRO GLU HIS ALA LEU VAL ALA TYR SER VAL ASP TYR CYS
SEQRES 14 B 715 GLY ASP GLU VAL TYR SER ILE ARG PHE VAL ARG ASP VAL
SEQRES 15 B 715 VAL ALA ASP LYS VAL GLU GLY THR ASN GLY SER VAL VAL
SEQRES 16 B 715 TRP GLY PRO ASN ALA GLU CYS PHE PHE TYR ILE THR LYS
SEQRES 17 B 715 ASP ALA SER LYS ARG ASP ASN LYS VAL TRP ARG HIS ILE
SEQRES 18 B 715 ILE GLY GLN PRO GLN SER GLU ASP VAL CYS LEU TYR THR
SEQRES 19 B 715 ASP ASP ASP PRO LEU PHE SER VAL GLY VAL GLY ARG SER
SEQRES 20 B 715 GLY ASP GLY LYS THR LEU ILE ILE CYS SER MSE SER SER
SEQRES 21 B 715 GLU THR SER GLU SER HIS LEU LEU ASP LEU ARG LYS GLY
SEQRES 22 B 715 VAL LYS HIS ASN THR LEU GLU MSE VAL ARG PRO ARG GLU
SEQRES 23 B 715 LYS GLY VAL ARG TYR THR VAL GLU MSE HIS GLY THR ASP
SEQRES 24 B 715 THR LEU ILE VAL LEU THR ASN LYS ASP LYS CYS VAL ASN
SEQRES 25 B 715 GLY LYS VAL VAL LEU THR LYS ARG SER ALA PRO THR ASP
SEQRES 26 B 715 TRP GLY THR VAL LEU ILE PRO HIS ASP ASP LYS VAL THR
SEQRES 27 B 715 ILE ASP ASP VAL ALA VAL PHE ALA LYS PHE ALA VAL LEU
SEQRES 28 B 715 SER GLY ARG ARG ASP GLY LEU THR ARG VAL TRP THR VAL
SEQRES 29 B 715 ARG LEU GLY PRO ASP ASN LEU PHE SER SER ALA THR LEU
SEQRES 30 B 715 LYS GLU LEU HIS PHE ASP GLU PRO VAL PHE THR ALA HIS
SEQRES 31 B 715 VAL VAL CYS SER GLN MSE LYS THR TYR ASP ALA SER LEU
SEQRES 32 B 715 LEU ARG LEU ARG TYR SER SER MSE THR THR PRO THR VAL
SEQRES 33 B 715 TRP TYR ASP GLU ASP VAL LEU SER GLY GLU ARG LYS VAL
SEQRES 34 B 715 VAL LYS ALA ARG LYS VAL GLY GLY GLY PHE GLU SER LYS
SEQRES 35 B 715 ASN TYR VAL CYS ARG ARG GLU LEU ALA THR ALA PRO ASP
SEQRES 36 B 715 GLY THR LYS VAL PRO ILE SER LEU VAL TYR ASP THR SER
SEQRES 37 B 715 ILE ASP LEU LYS LYS PRO ASN PRO THR MSE LEU TYR GLY
SEQRES 38 B 715 TYR GLY SER TYR GLY ILE CYS ILE GLU PRO GLU PHE ASN
SEQRES 39 B 715 SER ARG PHE LEU PRO TYR VAL ASP ARG GLY MSE ILE TYR
SEQRES 40 B 715 ALA ILE ALA HIS VAL ARG GLY GLY GLY GLU MSE GLY ARG
SEQRES 41 B 715 THR TRP TYR GLU VAL GLY GLY LYS TYR LEU THR LYS ARG
SEQRES 42 B 715 ASN THR PHE MSE ASP PHE ILE ALA CYS ALA GLU HIS LEU
SEQRES 43 B 715 ILE SER SER GLY LEU THR THR PRO ALA GLN LEU SER CYS
SEQRES 44 B 715 GLU GLY ARG SER ALA GLY GLY LEU LEU VAL GLY ALA VAL
SEQRES 45 B 715 LEU ASN MSE ARG PRO ASP LEU PHE HIS VAL ALA LEU ALA
SEQRES 46 B 715 GLY VAL PRO PHE VAL ASP VAL MSE THR THR MSE CYS ASP
SEQRES 47 B 715 PRO SER ILE PRO LEU THR THR GLY GLU TRP GLU GLU TRP
SEQRES 48 B 715 GLY ASN PRO ASN GLU TYR LYS PHE PHE ASP TYR MSE ASN
SEQRES 49 B 715 SER TYR SER PRO ILE ASP ASN VAL ARG ALA GLN ASP TYR
SEQRES 50 B 715 PRO HIS LEU MSE ILE GLN ALA GLY LEU HIS ASP PRO ARG
SEQRES 51 B 715 VAL ALA TYR TRP GLU PRO ALA LYS TRP ALA SER LYS LEU
SEQRES 52 B 715 ARG GLU LEU LYS THR ASP SER ASN GLU VAL LEU LEU LYS
SEQRES 53 B 715 MSE ASP LEU GLU SER GLY HIS PHE SER ALA SER ASP ARG
SEQRES 54 B 715 TYR LYS TYR LEU ARG GLU ASN ALA ILE GLN GLN ALA PHE
SEQRES 55 B 715 VAL LEU LYS HIS LEU ASN VAL ARG GLN LEU LEU ARG LYS
MODRES 4BP8 MSE A 31 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 92 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 258 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 281 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 295 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 396 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 411 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 478 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 505 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 518 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 537 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 575 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 593 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 596 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 623 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 641 MET SELENOMETHIONINE
MODRES 4BP8 MSE A 677 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 31 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 92 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 258 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 281 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 295 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 396 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 411 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 478 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 505 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 518 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 537 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 575 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 593 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 596 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 623 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 641 MET SELENOMETHIONINE
MODRES 4BP8 MSE B 677 MET SELENOMETHIONINE
HET MSE A 31 8
HET MSE A 92 8
HET MSE A 258 8
HET MSE A 281 8
HET MSE A 295 8
HET MSE A 396 8
HET MSE A 411 8
HET MSE A 478 8
HET MSE A 505 8
HET MSE A 518 8
HET MSE A 537 8
HET MSE A 575 8
HET MSE A 593 8
HET MSE A 596 8
HET MSE A 623 8
HET MSE A 641 8
HET MSE A 677 8
HET MSE B 31 8
HET MSE B 92 8
HET MSE B 258 8
HET MSE B 281 8
HET MSE B 295 8
HET MSE B 396 8
HET MSE B 411 8
HET MSE B 478 8
HET MSE B 505 8
HET MSE B 518 8
HET MSE B 537 8
HET MSE B 575 8
HET MSE B 593 8
HET MSE B 596 8
HET MSE B 623 8
HET MSE B 641 8
HET MSE B 677 8
HETNAM MSE SELENOMETHIONINE
FORMUL 3 MSE 34(C5 H11 N O2 SE)
FORMUL 4 HOH *778(H2 O)
HELIX 1 1 LEU A 41 ARG A 45 5 5
HELIX 2 2 ASP A 51 ALA A 69 1 19
HELIX 3 3 ILE A 72 SER A 85 1 14
HELIX 4 4 GLU A 137 GLU A 142 1 6
HELIX 5 5 ARG A 180 VAL A 182 5 3
HELIX 6 6 PRO A 198 ALA A 200 5 3
HELIX 7 7 ALA A 210 LYS A 212 5 3
HELIX 8 8 PRO A 225 ASP A 229 5 5
HELIX 9 9 ARG A 271 GLY A 273 5 3
HELIX 10 10 SER A 373 LEU A 377 5 5
HELIX 11 11 CYS A 393 MSE A 396 5 4
HELIX 12 12 GLU A 440 LYS A 442 5 3
HELIX 13 13 ASN A 494 ARG A 496 5 3
HELIX 14 14 PHE A 497 ASP A 502 1 6
HELIX 15 15 GLY A 519 VAL A 525 1 7
HELIX 16 16 LYS A 528 THR A 531 5 4
HELIX 17 17 LYS A 532 SER A 549 1 18
HELIX 18 18 THR A 553 ALA A 555 5 3
HELIX 19 19 ALA A 564 ARG A 576 1 13
HELIX 20 20 PRO A 577 PHE A 580 5 4
HELIX 21 21 ASP A 591 CYS A 597 1 7
HELIX 22 22 LEU A 603 GLY A 612 1 10
HELIX 23 23 PHE A 619 SER A 627 1 9
HELIX 24 24 PRO A 628 VAL A 632 5 5
HELIX 25 25 TYR A 653 LYS A 667 1 15
HELIX 26 26 ARG A 689 ASN A 708 1 20
HELIX 27 27 LEU B 41 ARG B 45 5 5
HELIX 28 28 ASP B 51 ALA B 69 1 19
HELIX 29 29 ILE B 72 HIS B 86 1 15
HELIX 30 30 GLU B 137 GLU B 142 1 6
HELIX 31 31 ARG B 180 VAL B 182 5 3
HELIX 32 32 PRO B 198 ALA B 200 5 3
HELIX 33 33 ALA B 210 LYS B 212 5 3
HELIX 34 34 PRO B 225 ASP B 229 5 5
HELIX 35 35 ARG B 271 GLY B 273 5 3
HELIX 36 36 SER B 373 LEU B 377 5 5
HELIX 37 37 CYS B 393 MSE B 396 5 4
HELIX 38 38 GLU B 440 LYS B 442 5 3
HELIX 39 39 ASN B 494 ARG B 496 5 3
HELIX 40 40 PHE B 497 ASP B 502 1 6
HELIX 41 41 ARG B 520 VAL B 525 1 6
HELIX 42 42 LYS B 528 THR B 531 5 4
HELIX 43 43 LYS B 532 SER B 549 1 18
HELIX 44 44 THR B 553 ALA B 555 5 3
HELIX 45 45 SER B 563 ARG B 576 1 14
HELIX 46 46 PRO B 577 PHE B 580 5 4
HELIX 47 47 ASP B 591 CYS B 597 1 7
HELIX 48 48 LEU B 603 TRP B 608 1 6
HELIX 49 49 PHE B 619 SER B 625 1 7
HELIX 50 50 SER B 627 VAL B 632 1 6
HELIX 51 51 TYR B 653 LYS B 667 1 15
HELIX 52 52 ARG B 689 LEU B 707 1 19
SHEET 1 AA 2 GLU A 15 PHE A 18 0
SHEET 2 AA 2 ARG A 35 VAL A 38 -1 O ARG A 35 N PHE A 18
SHEET 1 AB 2 ASP A 91 MSE A 92 0
SHEET 2 AB 2 PHE A 101 ASP A 107 -1 O ASP A 107 N ASP A 91
SHEET 1 AC 2 TYR A 96 TYR A 98 0
SHEET 2 AC 2 PHE A 101 ASP A 107 -1 O PHE A 101 N TYR A 98
SHEET 1 AD 4 GLU A 132 ASP A 136 0
SHEET 2 AD 4 LEU A 115 PRO A 120 -1 O HIS A 116 N VAL A 134
SHEET 3 AD 4 PHE A 101 ASP A 107 -1 O LEU A 102 N VAL A 119
SHEET 4 AD 4 TYR A 96 TYR A 98 -1 O TYR A 96 N TYR A 103
SHEET 1 AE 4 GLU A 132 ASP A 136 0
SHEET 2 AE 4 LEU A 115 PRO A 120 -1 O HIS A 116 N VAL A 134
SHEET 3 AE 4 PHE A 101 ASP A 107 -1 O LEU A 102 N VAL A 119
SHEET 4 AE 4 ASP A 91 MSE A 92 -1 O ASP A 91 N ASP A 107
SHEET 1 AF 4 VAL A 148 PRO A 154 0
SHEET 2 AF 4 VAL A 162 ASP A 167 -1 O ALA A 163 N ALA A 153
SHEET 3 AF 4 TYR A 174 PHE A 178 -1 O SER A 175 N VAL A 166
SHEET 4 AF 4 VAL A 187 THR A 190 -1 O VAL A 187 N ILE A 176
SHEET 1 AG 4 VAL A 195 TRP A 196 0
SHEET 2 AG 4 CYS A 202 LYS A 208 -1 O PHE A 204 N VAL A 195
SHEET 3 AG 4 ASP A 214 ILE A 221 -1 N ASN A 215 O THR A 207
SHEET 4 AG 4 VAL A 230 THR A 234 -1 O VAL A 230 N ARG A 219
SHEET 1 AH 4 SER A 241 ARG A 246 0
SHEET 2 AH 4 THR A 252 MSE A 258 -1 O ILE A 254 N GLY A 245
SHEET 3 AH 4 SER A 263 ASP A 269 -1 O GLU A 264 N SER A 257
SHEET 4 AH 4 GLU A 280 MSE A 281 -1 O GLU A 280 N LEU A 267
SHEET 1 AI 4 TYR A 291 HIS A 296 0
SHEET 2 AI 4 THR A 300 THR A 305 -1 O THR A 300 N HIS A 296
SHEET 3 AI 4 LYS A 314 LYS A 319 -1 O LYS A 314 N THR A 305
SHEET 4 AI 4 VAL A 329 ILE A 331 -1 N LEU A 330 O VAL A 315
SHEET 1 AJ 4 VAL A 337 VAL A 344 0
SHEET 2 AJ 4 PHE A 348 ARG A 355 -1 O VAL A 350 N ALA A 343
SHEET 3 AJ 4 LEU A 358 ARG A 365 -1 O LEU A 358 N ARG A 355
SHEET 4 AJ 4 LYS A 378 GLU A 379 -1 O LYS A 378 N THR A 363
SHEET 1 AK 4 THR A 388 VAL A 391 0
SHEET 2 AK 4 LEU A 403 SER A 410 -1 O ARG A 407 N HIS A 390
SHEET 3 AK 4 THR A 413 ASP A 421 -1 O THR A 413 N SER A 410
SHEET 4 AK 4 ARG A 427 ALA A 432 -1 O LYS A 428 N ASP A 419
SHEET 1 AL 8 TYR A 444 THR A 452 0
SHEET 2 AL 8 LYS A 458 ASP A 466 -1 O VAL A 459 N ALA A 451
SHEET 3 AL 8 ILE A 506 ALA A 510 -1 O TYR A 507 N VAL A 464
SHEET 4 AL 8 THR A 477 TYR A 480 1 O MSE A 478 N ALA A 508
SHEET 5 AL 8 LEU A 557 ARG A 562 1 O SER A 558 N LEU A 479
SHEET 6 AL 8 VAL A 582 GLY A 586 1 O VAL A 582 N CYS A 559
SHEET 7 AL 8 HIS A 639 GLY A 645 1 O HIS A 639 N ALA A 583
SHEET 8 AL 8 VAL A 673 ASP A 678 1 O LEU A 674 N ILE A 642
SHEET 1 BA 2 GLU B 15 PHE B 18 0
SHEET 2 BA 2 ARG B 35 VAL B 38 -1 O ARG B 35 N PHE B 18
SHEET 1 BB 2 ASP B 91 MSE B 92 0
SHEET 2 BB 2 PHE B 101 ASP B 107 -1 O ASP B 107 N ASP B 91
SHEET 1 BC 2 TYR B 96 TYR B 98 0
SHEET 2 BC 2 PHE B 101 ASP B 107 -1 O PHE B 101 N TYR B 98
SHEET 1 BD 4 GLU B 132 ASP B 136 0
SHEET 2 BD 4 LEU B 115 PRO B 120 -1 O HIS B 116 N LEU B 135
SHEET 3 BD 4 PHE B 101 ASP B 107 -1 O LEU B 102 N VAL B 119
SHEET 4 BD 4 TYR B 96 TYR B 98 -1 O TYR B 96 N TYR B 103
SHEET 1 BE 4 GLU B 132 ASP B 136 0
SHEET 2 BE 4 LEU B 115 PRO B 120 -1 O HIS B 116 N LEU B 135
SHEET 3 BE 4 PHE B 101 ASP B 107 -1 O LEU B 102 N VAL B 119
SHEET 4 BE 4 ASP B 91 MSE B 92 -1 O ASP B 91 N ASP B 107
SHEET 1 BF 4 VAL B 148 PRO B 154 0
SHEET 2 BF 4 VAL B 162 ASP B 167 -1 O ALA B 163 N ALA B 153
SHEET 3 BF 4 TYR B 174 PHE B 178 -1 O SER B 175 N VAL B 166
SHEET 4 BF 4 VAL B 187 THR B 190 -1 O VAL B 187 N ILE B 176
SHEET 1 BG 4 VAL B 195 TRP B 196 0
SHEET 2 BG 4 CYS B 202 LYS B 208 -1 O PHE B 204 N VAL B 195
SHEET 3 BG 4 ASP B 214 ILE B 221 -1 N ASN B 215 O THR B 207
SHEET 4 BG 4 VAL B 230 THR B 234 -1 O VAL B 230 N ARG B 219
SHEET 1 BH 4 SER B 241 ARG B 246 0
SHEET 2 BH 4 THR B 252 MSE B 258 -1 O ILE B 254 N GLY B 245
SHEET 3 BH 4 SER B 263 ASP B 269 -1 O GLU B 264 N SER B 257
SHEET 4 BH 4 GLU B 280 MSE B 281 -1 O GLU B 280 N LEU B 267
SHEET 1 BI 4 TYR B 291 HIS B 296 0
SHEET 2 BI 4 THR B 300 THR B 305 -1 O THR B 300 N HIS B 296
SHEET 3 BI 4 LYS B 314 LYS B 319 -1 O LYS B 314 N THR B 305
SHEET 4 BI 4 THR B 328 ILE B 331 -1 O THR B 328 N LEU B 317
SHEET 1 BJ 4 VAL B 337 VAL B 344 0
SHEET 2 BJ 4 PHE B 348 ARG B 355 -1 O VAL B 350 N ALA B 343
SHEET 3 BJ 4 LEU B 358 ARG B 365 -1 O LEU B 358 N ARG B 355
SHEET 4 BJ 4 LYS B 378 GLU B 379 -1 O LYS B 378 N THR B 363
SHEET 1 BK 4 THR B 388 VAL B 391 0
SHEET 2 BK 4 LEU B 403 SER B 410 -1 O ARG B 407 N HIS B 390
SHEET 3 BK 4 THR B 413 ASP B 421 -1 O THR B 413 N SER B 410
SHEET 4 BK 4 ARG B 427 ALA B 432 -1 O LYS B 428 N ASP B 419
SHEET 1 BL 8 TYR B 444 THR B 452 0
SHEET 2 BL 8 LYS B 458 ASP B 466 -1 O VAL B 459 N ALA B 451
SHEET 3 BL 8 ILE B 506 ALA B 510 -1 O TYR B 507 N VAL B 464
SHEET 4 BL 8 THR B 477 TYR B 480 1 O MSE B 478 N ALA B 508
SHEET 5 BL 8 LEU B 557 ARG B 562 1 O SER B 558 N LEU B 479
SHEET 6 BL 8 VAL B 582 GLY B 586 1 O VAL B 582 N CYS B 559
SHEET 7 BL 8 HIS B 639 GLY B 645 1 O HIS B 639 N ALA B 583
SHEET 8 BL 8 VAL B 673 ASP B 678 1 O LEU B 674 N ILE B 642
LINK N MSE A 31 C PRO A 30 1555 1555 1.33
LINK C MSE A 31 N ASP A 32 1555 1555 1.33
LINK N MSE A 92 C ASP A 91 1555 1555 1.33
LINK C MSE A 92 N SER A 93 1555 1555 1.33
LINK N MSE A 258 C SER A 257 1555 1555 1.33
LINK C MSE A 258 N SER A 259 1555 1555 1.33
LINK N MSE A 281 C GLU A 280 1555 1555 1.32
LINK C MSE A 281 N VAL A 282 1555 1555 1.33
LINK N MSE A 295 C GLU A 294 1555 1555 1.33
LINK C MSE A 295 N HIS A 296 1555 1555 1.33
LINK N MSE A 396 C GLN A 395 1555 1555 1.33
LINK C MSE A 396 N LYS A 397 1555 1555 1.34
LINK N MSE A 411 C SER A 410 1555 1555 1.32
LINK C MSE A 411 N THR A 412 1555 1555 1.32
LINK N MSE A 478 C THR A 477 1555 1555 1.33
LINK C MSE A 478 N LEU A 479 1555 1555 1.33
LINK N MSE A 505 C GLY A 504 1555 1555 1.33
LINK C MSE A 505 N ILE A 506 1555 1555 1.34
LINK N MSE A 518 C GLU A 517 1555 1555 1.33
LINK C MSE A 518 N GLY A 519 1555 1555 1.32
LINK N MSE A 537 C PHE A 536 1555 1555 1.34
LINK C MSE A 537 N ASP A 538 1555 1555 1.34
LINK N MSE A 575 C ASN A 574 1555 1555 1.33
LINK C MSE A 575 N ARG A 576 1555 1555 1.33
LINK N MSE A 593 C VAL A 592 1555 1555 1.33
LINK C MSE A 593 N THR A 594 1555 1555 1.34
LINK N MSE A 596 C THR A 595 1555 1555 1.32
LINK C MSE A 596 N CYS A 597 1555 1555 1.33
LINK N MSE A 623 C TYR A 622 1555 1555 1.33
LINK C MSE A 623 N ASN A 624 1555 1555 1.32
LINK N MSE A 641 C LEU A 640 1555 1555 1.33
LINK C MSE A 641 N ILE A 642 1555 1555 1.33
LINK N MSE A 677 C LYS A 676 1555 1555 1.32
LINK C MSE A 677 N ASP A 678 1555 1555 1.33
LINK C MSE B 31 N ASP B 32 1555 1555 1.33
LINK N MSE B 31 C PRO B 30 1555 1555 1.33
LINK C MSE B 92 N SER B 93 1555 1555 1.34
LINK N MSE B 92 C ASP B 91 1555 1555 1.33
LINK C MSE B 258 N SER B 259 1555 1555 1.33
LINK N MSE B 258 C SER B 257 1555 1555 1.33
LINK C MSE B 281 N VAL B 282 1555 1555 1.33
LINK N MSE B 281 C GLU B 280 1555 1555 1.33
LINK C MSE B 295 N HIS B 296 1555 1555 1.33
LINK N MSE B 295 C GLU B 294 1555 1555 1.33
LINK C MSE B 396 N LYS B 397 1555 1555 1.32
LINK N MSE B 396 C GLN B 395 1555 1555 1.33
LINK C MSE B 411 N THR B 412 1555 1555 1.32
LINK N MSE B 411 C SER B 410 1555 1555 1.32
LINK C MSE B 478 N LEU B 479 1555 1555 1.33
LINK N MSE B 478 C THR B 477 1555 1555 1.33
LINK C MSE B 505 N ILE B 506 1555 1555 1.32
LINK N MSE B 505 C GLY B 504 1555 1555 1.32
LINK C MSE B 518 N GLY B 519 1555 1555 1.33
LINK N MSE B 518 C GLU B 517 1555 1555 1.33
LINK C MSE B 537 N ASP B 538 1555 1555 1.33
LINK N MSE B 537 C PHE B 536 1555 1555 1.34
LINK C MSE B 575 N ARG B 576 1555 1555 1.32
LINK N MSE B 575 C ASN B 574 1555 1555 1.32
LINK C MSE B 593 N THR B 594 1555 1555 1.33
LINK N MSE B 593 C VAL B 592 1555 1555 1.32
LINK C MSE B 596 N CYS B 597 1555 1555 1.34
LINK N MSE B 596 C THR B 595 1555 1555 1.33
LINK C MSE B 623 N ASN B 624 1555 1555 1.32
LINK N MSE B 623 C TYR B 622 1555 1555 1.33
LINK C MSE B 641 N ILE B 642 1555 1555 1.33
LINK N MSE B 641 C LEU B 640 1555 1555 1.33
LINK C MSE B 677 N ASP B 678 1555 1555 1.32
LINK N MSE B 677 C LYS B 676 1555 1555 1.32
CISPEP 1 ASP A 32 PRO A 33 0 7.36
CISPEP 2 ASP B 32 PRO B 33 0 6.56
CRYST1 124.140 124.140 249.140 90.00 90.00 120.00 P 32 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 0.008055 0.004651 0.000000 0.00000
SCALE2 0.000000 0.009302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004014 0.00000
TER 5652 LYS A 715
TER 11304 LYS B 715
MASTER 558 0 34 52 92 0 0 612080 2 340 110
END |