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HEADER HYDROLASE 02-FEB-05 1YR2
TITLE STRUCTURAL AND MECHANISTIC ANALYSIS OF TWO PROLYL
TITLE 2 ENDOPEPTIDASES: ROLE OF INTER-DOMAIN DYNAMICS IN CATALYSIS
TITLE 3 AND SPECIFICITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROLYL ENDOPEPTIDASES;
COMPND 5 EC: 3.4.21.26;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOVOSPHINGOBIUM CAPSULATUM;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: ATCC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS PROLYL ENDOPEPTIDASE, CRYSTAL STRUCTURE, MECHANISTIC STUDY,
KEYWDS 2 CELIAC SPRUE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SHAN,I.I.MATHEWS,C.KHOSLA
REVDAT 1 15-MAR-05 1YR2 0
JRNL AUTH L.SHAN,I.I.MATHEWS,C.KHOSLA
JRNL TITL STRUCTURAL AND MECHANISTIC ANALYSIS OF TWO PROLYL
JRNL TITL 2 ENDOPEPTIDASES: ROLE OF INTERDOMAIN DYNAMICS IN
JRNL TITL 3 CATALYSIS AND SPECIFICITY
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 3599 2005
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.SHAN,T.MARTI,L.M.SOLLID,G.M.GRAY,C.KHOSLA
REMARK 1 TITL COMPARATIVE BIOCHEMICAL ANALYSIS OF THREE
REMARK 1 TITL 2 BACTERIAL PROLYL ENDOPEPTIDASES: IMPLICATIONS FOR
REMARK 1 TITL 3 CELIAC SPRUE
REMARK 1 REF BIOCHEM.J. V. 383 311 2004
REMARK 1 REFN ASTM BIJOAK UK ISSN 0264-6021
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.SHAN,O.MOLBERG,I.PARROIT,F.HAUSCH,F.FILIZ,
REMARK 1 AUTH 2 G.M.GRAY,L.M.SOLLID,C.KHOSLA
REMARK 1 TITL STRUCTURAL BASIS FOR GLUTEN INTOLERANCE IN CELIAC
REMARK 1 TITL 2 SPRUE
REMARK 1 REF SCIENCE V. 297 2275 2002
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.POLGAR
REMARK 1 TITL THE PROLYL OLIGOPEPTIDASE FAMILY
REMARK 1 REF CELL.MOL.LIFE SCI. V. 59 349 2002
REMARK 1 REFN SZ ISSN 1420-682X
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 66171
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3538
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4393
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 237
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5929
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.97000
REMARK 3 B22 (A**2) : 1.93000
REMARK 3 B33 (A**2) : -0.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.111
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.545
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5419 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4839 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7388 ; 1.561 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11222 ; 1.026 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 676 ; 6.281 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 790 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6119 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1155 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 890 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5346 ; 0.262 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3121 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 481 ; 0.143 ; 0.200
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): 9 ; 0.118 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 51 ; 0.301 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.127 ; 0.200
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): 3382 ; 0.988 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5418 ; 1.755 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2037 ; 2.764 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1970 ; 4.352 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 38 A 107
REMARK 3 RESIDUE RANGE : A 453 A 725
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0986 40.9254 -30.0682
REMARK 3 T TENSOR
REMARK 3 T11: 0.0780 T22: 0.0414
REMARK 3 T33: 0.0267 T12: 0.0360
REMARK 3 T13: 0.0242 T23: 0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.8483 L22: 0.3301
REMARK 3 L33: 0.9385 L12: 0.0624
REMARK 3 L13: 0.4636 L23: 0.2463
REMARK 3 S TENSOR
REMARK 3 S11: 0.0516 S12: 0.0856 S13: 0.0228
REMARK 3 S21: -0.0592 S22: -0.0105 S23: -0.0384
REMARK 3 S31: 0.0545 S32: 0.0358 S33: -0.0411
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 726 A 738
REMARK 3 ORIGIN FOR THE GROUP (A): 79.6414 44.0146 -14.2893
REMARK 3 T TENSOR
REMARK 3 T11: 0.0768 T22: 0.0666
REMARK 3 T33: 0.0746 T12: -0.0013
REMARK 3 T13: -0.0486 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 30.0191 L22: 0.3293
REMARK 3 L33: 5.0265 L12: 4.4798
REMARK 3 L13: -8.2204 L23: -3.5080
REMARK 3 S TENSOR
REMARK 3 S11: 0.1958 S12: -0.8422 S13: -0.3150
REMARK 3 S21: 0.1928 S22: -0.1848 S23: -0.1090
REMARK 3 S31: 0.2482 S32: 0.1362 S33: -0.0110
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 108 A 452
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9692 49.8286 8.8530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0384 T22: 0.0175
REMARK 3 T33: 0.0538 T12: -0.0041
REMARK 3 T13: -0.0174 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 1.0595 L22: 0.3179
REMARK 3 L33: 0.7644 L12: -0.0512
REMARK 3 L13: -0.1806 L23: -0.1331
REMARK 3 S TENSOR
REMARK 3 S11: 0.0194 S12: -0.0941 S13: -0.0191
REMARK 3 S21: 0.0122 S22: -0.0204 S23: -0.0287
REMARK 3 S31: -0.0196 S32: -0.0277 S33: 0.0010
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1YR2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-2005.
REMARK 100 THE RCSB ID CODE IS RCSB031832.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68648
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50200
REMARK 200 FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1H2W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRIS, PH 8.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295.0K
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,1/2+Y,-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 45.61200
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 ASN A 3
REMARK 465 ARG A 4
REMARK 465 LEU A 5
REMARK 465 TRP A 6
REMARK 465 LEU A 7
REMARK 465 ALA A 8
REMARK 465 MET A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 PRO A 12
REMARK 465 LEU A 13
REMARK 465 ALA A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 THR A 17
REMARK 465 PRO A 18
REMARK 465 VAL A 19
REMARK 465 ALA A 20
REMARK 465 PHE A 21
REMARK 465 ALA A 22
REMARK 465 GLN A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 PRO A 26
REMARK 465 THR A 27
REMARK 465 LEU A 28
REMARK 465 ALA A 29
REMARK 465 LYS A 30
REMARK 465 ASP A 31
REMARK 465 GLN A 32
REMARK 465 ALA A 33
REMARK 465 MET A 34
REMARK 465 PRO A 35
REMARK 465 SER A 36
REMARK 465 LEU A 37
REMARK 465 ALA A 158
REMARK 465 LYS A 159
REMARK 465 ASP A 160
REMARK 465 GLY A 161
REMARK 465 LYS A 231
REMARK 465 GLU A 232
REMARK 465 GLY A 233
REMARK 465 GLN A 234
REMARK 465 ALA A 235
REMARK 465 PHE A 236
REMARK 465 GLN A 237
REMARK 465 ALA A 238
REMARK 465 THR A 689
REMARK 465 ARG A 690
REMARK 465 ALA A 691
REMARK 465 GLY A 692
REMARK 465 HIS A 693
REMARK 465 GLY A 694
REMARK 465 SER A 695
REMARK 465 GLY A 696
REMARK 465 LYS A 697
REMARK 465 HIS A 739
REMARK 465 HIS A 740
REMARK 465 HIS A 741
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 HIS A 738 CB CG ND1 CD2 CE1 NE2
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 102 CG MET A 102 SD -0.101
REMARK 500 MET A 102 SD MET A 102 CE 0.155
REMARK 500 MET A 511 SD MET A 511 CE -0.133
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 214 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 THR A 290 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 ALA A 612 C - N - CA ANGL. DEV. = 10.4 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 LYS A 341 160.77 78.16
REMARK 500 SER A 575 -118.32 72.31
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICT MAY BE DUE TO A DIFFERENT LAB STRAIN.
DBREF 1YR2 A 1 723 GB 3805974 BAA34052 1 723
SEQADV 1YR2 PHE A 667 GB 3805974 LEU 667 SEE REMARK 999
SEQADV 1YR2 TRP A 724 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 SER A 725 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 SER A 726 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 VAL A 727 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 ASP A 728 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 LYS A 729 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 LEU A 730 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 ALA A 731 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 ALA A 732 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 ALA A 733 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 LEU A 734 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 GLU A 735 GB 3805974 CLONING ARTIFACT
SEQADV 1YR2 HIS A 736 GB 3805974 HIS TAG
SEQADV 1YR2 HIS A 737 GB 3805974 HIS TAG
SEQADV 1YR2 HIS A 738 GB 3805974 HIS TAG
SEQADV 1YR2 HIS A 739 GB 3805974 HIS TAG
SEQADV 1YR2 HIS A 740 GB 3805974 HIS TAG
SEQADV 1YR2 HIS A 741 GB 3805974 HIS TAG
SEQRES 1 A 741 MET LYS ASN ARG LEU TRP LEU ALA MET ALA ALA PRO LEU
SEQRES 2 A 741 ALA LEU ALA THR PRO VAL ALA PHE ALA GLN THR PRO PRO
SEQRES 3 A 741 THR LEU ALA LYS ASP GLN ALA MET PRO SER LEU PRO PRO
SEQRES 4 A 741 TYR PRO ALA SER PRO GLN VAL PRO LEU VAL GLU ASP HIS
SEQRES 5 A 741 PHE GLY GLU LYS VAL SER ASP PRO TRP ARG TRP LEU GLU
SEQRES 6 A 741 ALA ASP VAL ARG THR ASP ALA LYS VAL ALA ALA TRP VAL
SEQRES 7 A 741 GLN ALA GLN SER ALA TYR THR ALA ALA TYR LEU LYS GLN
SEQRES 8 A 741 LEU PRO GLU ARG ALA ALA LEU GLU LYS ARG MET LYS ALA
SEQRES 9 A 741 LEU ILE ASP TYR GLU ARG PHE GLY LEU PRO GLN ARG ARG
SEQRES 10 A 741 GLY ALA SER VAL PHE TYR SER TRP ASN SER GLY LEU MET
SEQRES 11 A 741 ASN GLN SER GLN LEU LEU VAL ARG PRO ALA ASP ALA PRO
SEQRES 12 A 741 VAL GLY THR LYS GLY ARG VAL LEU LEU ASP PRO ASN THR
SEQRES 13 A 741 TRP ALA LYS ASP GLY ALA THR ALA LEU ASP ALA TRP ALA
SEQRES 14 A 741 ALA SER ASP ASP GLY ARG LEU LEU ALA TYR SER VAL GLN
SEQRES 15 A 741 ASP GLY GLY SER ASP TRP ARG THR VAL LYS PHE VAL GLY
SEQRES 16 A 741 VAL ALA ASP GLY LYS PRO LEU ALA ASP GLU LEU LYS TRP
SEQRES 17 A 741 VAL LYS PHE SER GLY LEU ALA TRP LEU GLY ASN ASP ALA
SEQRES 18 A 741 LEU LEU TYR SER ARG PHE ALA GLU PRO LYS GLU GLY GLN
SEQRES 19 A 741 ALA PHE GLN ALA LEU ASN TYR ASN GLN THR VAL TRP LEU
SEQRES 20 A 741 HIS ARG LEU GLY THR PRO GLN SER ALA ASP GLN PRO VAL
SEQRES 21 A 741 PHE ALA THR PRO GLU LEU PRO LYS ARG GLY HIS GLY ALA
SEQRES 22 A 741 SER VAL SER SER ASP GLY ARG TRP VAL VAL ILE THR SER
SEQRES 23 A 741 SER GLU GLY THR ASP PRO VAL ASN THR VAL HIS VAL ALA
SEQRES 24 A 741 ARG VAL THR ASN GLY LYS ILE GLY PRO VAL THR ALA LEU
SEQRES 25 A 741 ILE PRO ASP LEU LYS ALA GLN TRP ASP PHE VAL ASP GLY
SEQRES 26 A 741 VAL GLY ASP GLN LEU TRP PHE VAL SER GLY ASP GLY ALA
SEQRES 27 A 741 PRO LEU LYS LYS ILE VAL ARG VAL ASP LEU SER GLY SER
SEQRES 28 A 741 THR PRO ARG PHE ASP THR VAL VAL PRO GLU SER LYS ASP
SEQRES 29 A 741 ASN LEU GLU SER VAL GLY ILE ALA GLY ASN ARG LEU PHE
SEQRES 30 A 741 ALA SER TYR ILE HIS ASP ALA LYS SER GLN VAL LEU ALA
SEQRES 31 A 741 PHE ASP LEU ASP GLY LYS PRO ALA GLY ALA VAL SER LEU
SEQRES 32 A 741 PRO GLY ILE GLY SER ALA SER GLY LEU SER GLY ARG PRO
SEQRES 33 A 741 GLY ASP ARG HIS ALA TYR LEU SER PHE SER SER PHE THR
SEQRES 34 A 741 GLN PRO ALA THR VAL LEU ALA LEU ASP PRO ALA THR ALA
SEQRES 35 A 741 LYS THR THR PRO TRP GLU PRO VAL HIS LEU THR PHE ASP
SEQRES 36 A 741 PRO ALA ASP PHE ARG VAL GLU GLN VAL PHE TYR PRO SER
SEQRES 37 A 741 LYS ASP GLY THR LYS VAL PRO MET PHE ILE VAL ARG ARG
SEQRES 38 A 741 LYS ASP ALA LYS GLY PRO LEU PRO THR LEU LEU TYR GLY
SEQRES 39 A 741 TYR GLY GLY PHE ASN VAL ALA LEU THR PRO TRP PHE SER
SEQRES 40 A 741 ALA GLY PHE MET THR TRP ILE ASP SER GLY GLY ALA PHE
SEQRES 41 A 741 ALA LEU ALA ASN LEU ARG GLY GLY GLY GLU TYR GLY ASP
SEQRES 42 A 741 ALA TRP HIS ASP ALA GLY ARG ARG ASP LYS LYS GLN ASN
SEQRES 43 A 741 VAL PHE ASP ASP PHE ILE ALA ALA GLY GLU TRP LEU ILE
SEQRES 44 A 741 ALA ASN GLY VAL THR PRO ARG HIS GLY LEU ALA ILE GLU
SEQRES 45 A 741 GLY GLY SER ASN GLY GLY LEU LEU ILE GLY ALA VAL THR
SEQRES 46 A 741 ASN GLN ARG PRO ASP LEU PHE ALA ALA ALA SER PRO ALA
SEQRES 47 A 741 VAL GLY VAL MET ASP MET LEU ARG PHE ASP GLN PHE THR
SEQRES 48 A 741 ALA GLY ARG TYR TRP VAL ASP ASP TYR GLY TYR PRO GLU
SEQRES 49 A 741 LYS GLU ALA ASP TRP ARG VAL LEU ARG ARG TYR SER PRO
SEQRES 50 A 741 TYR HIS ASN VAL ARG SER GLY VAL ASP TYR PRO ALA ILE
SEQRES 51 A 741 LEU VAL THR THR ALA ASP THR ASP ASP ARG VAL VAL PRO
SEQRES 52 A 741 GLY HIS SER PHE LYS TYR THR ALA ALA LEU GLN THR ALA
SEQRES 53 A 741 ALA ILE GLY PRO LYS PRO HIS LEU ILE ARG ILE GLU THR
SEQRES 54 A 741 ARG ALA GLY HIS GLY SER GLY LYS PRO ILE ASP LYS GLN
SEQRES 55 A 741 ILE GLU GLU THR ALA ASP VAL GLN ALA PHE LEU ALA HIS
SEQRES 56 A 741 PHE THR GLY LEU THR PRO ARG PRO TRP SER SER VAL ASP
SEQRES 57 A 741 LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET GOL 750 6
HET GOL 755 6
HETNAM GOL GLYCEROL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 HOH *660(H2 O1)
HELIX 1 1 TRP A 61 ALA A 66 5 6
HELIX 2 2 ASP A 71 LYS A 90 1 20
HELIX 3 3 GLU A 94 ILE A 106 1 13
HELIX 4 4 ASP A 153 TRP A 157 5 5
HELIX 5 5 PRO A 253 ASP A 257 5 5
HELIX 6 6 ASP A 455 ALA A 457 5 3
HELIX 7 7 SER A 507 ASP A 515 1 9
HELIX 8 8 TYR A 531 ALA A 538 1 8
HELIX 9 9 GLY A 539 ASP A 542 5 4
HELIX 10 10 LYS A 543 ASN A 561 1 19
HELIX 11 11 SER A 575 ARG A 588 1 14
HELIX 12 12 PRO A 589 PHE A 592 5 4
HELIX 13 13 ARG A 606 PHE A 610 5 5
HELIX 14 14 ALA A 612 TYR A 615 5 4
HELIX 15 15 TRP A 616 GLY A 621 1 6
HELIX 16 16 LYS A 625 ARG A 634 1 10
HELIX 17 17 SER A 636 ASN A 640 5 5
HELIX 18 18 PRO A 663 ALA A 676 1 14
HELIX 19 19 PRO A 698 GLY A 718 1 21
HELIX 20 20 SER A 725 HIS A 736 1 12
SHEET 1 A 2 VAL A 49 HIS A 52 0
SHEET 2 A 2 GLU A 55 SER A 58 -1 O GLU A 55 N HIS A 52
SHEET 1 B 3 ARG A 110 PHE A 111 0
SHEET 2 B 3 SER A 120 ASN A 126 -1 O ASN A 126 N ARG A 110
SHEET 3 B 3 GLN A 115 ARG A 117 -1 N GLN A 115 O PHE A 122
SHEET 1 C 4 ARG A 110 PHE A 111 0
SHEET 2 C 4 SER A 120 ASN A 126 -1 O ASN A 126 N ARG A 110
SHEET 3 C 4 GLN A 134 PRO A 139 -1 O LEU A 136 N TYR A 123
SHEET 4 C 4 ARG A 149 LEU A 152 -1 O LEU A 151 N LEU A 135
SHEET 1 D 4 THR A 163 ALA A 170 0
SHEET 2 D 4 LEU A 176 ASP A 183 -1 O SER A 180 N ASP A 166
SHEET 3 D 4 TRP A 188 GLY A 195 -1 O LYS A 192 N TYR A 179
SHEET 4 D 4 PRO A 201 LYS A 210 -1 O VAL A 209 N ARG A 189
SHEET 1 E 4 ALA A 215 TRP A 216 0
SHEET 2 E 4 ALA A 221 ARG A 226 -1 O LEU A 223 N ALA A 215
SHEET 3 E 4 THR A 244 ARG A 249 -1 O HIS A 248 N LEU A 222
SHEET 4 E 4 GLN A 258 PHE A 261 -1 O VAL A 260 N VAL A 245
SHEET 1 F 4 GLY A 270 VAL A 275 0
SHEET 2 F 4 TRP A 281 SER A 287 -1 O SER A 287 N GLY A 270
SHEET 3 F 4 THR A 295 THR A 302 -1 O HIS A 297 N ILE A 284
SHEET 4 F 4 LYS A 305 ILE A 306 -1 O LYS A 305 N THR A 302
SHEET 1 G 4 GLY A 270 VAL A 275 0
SHEET 2 G 4 TRP A 281 SER A 287 -1 O SER A 287 N GLY A 270
SHEET 3 G 4 THR A 295 THR A 302 -1 O HIS A 297 N ILE A 284
SHEET 4 G 4 THR A 310 ILE A 313 -1 O THR A 310 N VAL A 298
SHEET 1 H 4 TRP A 320 VAL A 326 0
SHEET 2 H 4 GLN A 329 SER A 334 -1 O TRP A 331 N VAL A 323
SHEET 3 H 4 LYS A 342 ASP A 347 -1 O VAL A 346 N LEU A 330
SHEET 4 H 4 ARG A 354 VAL A 359 -1 O ASP A 356 N ARG A 345
SHEET 1 I 4 ASN A 365 ALA A 372 0
SHEET 2 I 4 ARG A 375 HIS A 382 -1 O SER A 379 N SER A 368
SHEET 3 I 4 LYS A 385 ASP A 392 -1 O PHE A 391 N LEU A 376
SHEET 4 I 4 PRO A 397 ALA A 400 -1 O GLY A 399 N ALA A 390
SHEET 1 J 4 SER A 408 SER A 413 0
SHEET 2 J 4 ALA A 421 SER A 427 -1 O SER A 426 N SER A 408
SHEET 3 J 4 GLN A 430 ASP A 438 -1 O LEU A 435 N LEU A 423
SHEET 4 J 4 LYS A 443 PRO A 446 -1 O THR A 445 N ALA A 436
SHEET 1 K 8 PHE A 459 PRO A 467 0
SHEET 2 K 8 LYS A 473 ARG A 481 -1 O ILE A 478 N GLU A 462
SHEET 3 K 8 ALA A 519 ALA A 523 -1 O PHE A 520 N VAL A 479
SHEET 4 K 8 THR A 490 TYR A 493 1 N TYR A 493 O ALA A 521
SHEET 5 K 8 LEU A 569 GLY A 574 1 O ALA A 570 N THR A 490
SHEET 6 K 8 ALA A 594 ALA A 598 1 O ALA A 598 N GLY A 573
SHEET 7 K 8 ALA A 649 ALA A 655 1 O ALA A 649 N ALA A 595
SHEET 8 K 8 HIS A 683 GLU A 688 1 O ARG A 686 N VAL A 652
CRYST1 53.341 91.224 79.787 90.00 91.00 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 0.018747 0.000000 0.000327 0.00000
SCALE2 0.000000 0.010962 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012535 0.00000
TER 5257 HIS A 738
MASTER 419 0 2 20 45 0 0 6 5929 1 12 57
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