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HEADER HYDROLASE 14-DEC-04 2BKL
TITLE STRUCTURAL AND MECHANISTIC ANALYSIS OF TWO PROLYL
TITLE 2 ENDOPEPTIDASES: ROLE OF INTER-DOMAIN DYNAMICS IN
TITLE 3 CATALYSIS AND SPECIFICITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.26;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: Z-ALA PROLINAL
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 5 ORGANISM_SCIENTIFIC: MYXOCOCCUS XANTHUS;
SOURCE 6 ATCC: 25232
KEYWDS PROLYL ENDOPEPTIDASE, CRYSTAL STRUCTURE, MECHANISTIC STUDY,
KEYWDS 2 CELIAC SPRUE, HYDROLASE, PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.KHOSLA,L.SHAN,I.I.MATHEWS
REVDAT 1 09-MAR-05 2BKL 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 TO BE PUBLISHED
JRNL REFN
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.PARROT,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 ASTM ISSN 1420-682X
REMARK 2
REMARK 2 RESOLUTION. 1.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.90
REMARK 3 NUMBER OF REFLECTIONS : 214057
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) : 0.16077
REMARK 3 R VALUE (WORKING SET) : 0.15964
REMARK 3 FREE R VALUE : 0.18242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 11252
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) : 1.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.539
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15555
REMARK 3 BIN R VALUE (WORKING SET) : 0.224
REMARK 3 BIN FREE R VALUE SET COUNT : 812
REMARK 3 BIN FREE R VALUE : 0.256
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10723
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 1371
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.335
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.57
REMARK 3 B22 (A**2) : 0.47
REMARK 3 B33 (A**2) : 0.09
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.01
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.067
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.062
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
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 (A): 11137 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 9844 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 15138 ; 1.491 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22909 ; 1.235 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1351 ; 6.160 ; 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): 1593 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 12455 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2368 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 1825 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 11376 ; 0.257 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 6418 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 925 ; 0.117 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 7 ; 0.077 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.311 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 30 ; 0.133 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 6733 ; 1.432 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 10824 ; 2.385 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 4404 ; 2.342 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 4312 ; 3.114 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 2 A 68
REMARK 3 RESIDUE RANGE : A 409 A 677
REMARK 3 ORIGIN FOR THE GROUP (A): -37.7448 7.4794 0.8975
REMARK 3 T TENSOR
REMARK 3 T11: 0.0298 T22: 0.0473
REMARK 3 T33: 0.0215 T12: -0.0005
REMARK 3 T13: -0.0019 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.2938 L22: 0.2731
REMARK 3 L33: 0.1752 L12: 0.0352
REMARK 3 L13: -0.0249 L23: -0.0155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: 0.0011 S13: 0.0002
REMARK 3 S21: -0.0126 S22: -0.0082 S23: 0.0128
REMARK 3 S31: -0.0187 S32: 0.0484 S33: -0.0030
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 69 A 408
REMARK 3 ORIGIN FOR THE GROUP (A): -55.2967 -7.1985 21.2116
REMARK 3 T TENSOR
REMARK 3 T11: 0.0271 T22: 0.0239
REMARK 3 T33: 0.0320 T12: -0.0085
REMARK 3 T13: 0.0009 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.3868 L22: 0.1420
REMARK 3 L33: 0.2506 L12: 0.0469
REMARK 3 L13: -0.1521 L23: 0.0100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: -0.0626 S13: -0.0467
REMARK 3 S21: 0.0034 S22: -0.0196 S23: 0.0232
REMARK 3 S31: -0.0052 S32: 0.0184 S33: 0.0052
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 68
REMARK 3 RESIDUE RANGE : B 409 B 678
REMARK 3 ORIGIN FOR THE GROUP (A): -32.5770 3.0250 65.1799
REMARK 3 T TENSOR
REMARK 3 T11: 0.0354 T22: 0.0345
REMARK 3 T33: 0.0264 T12: -0.0014
REMARK 3 T13: -0.0008 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.2407 L22: 0.2100
REMARK 3 L33: 0.3014 L12: -0.0169
REMARK 3 L13: 0.0003 L23: 0.0644
REMARK 3 S TENSOR
REMARK 3 S11: -0.0096 S12: -0.0029 S13: -0.0103
REMARK 3 S21: 0.0118 S22: -0.0258 S23: -0.0049
REMARK 3 S31: -0.0198 S32: -0.0495 S33: 0.0354
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 69 B 408
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7938 -19.4301 51.6331
REMARK 3 T TENSOR
REMARK 3 T11: 0.0380 T22: 0.0058
REMARK 3 T33: 0.0393 T12: 0.0048
REMARK 3 T13: 0.0048 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.1885 L22: 0.2505
REMARK 3 L33: 0.4039 L12: -0.0217
REMARK 3 L13: -0.0444 L23: 0.1194
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: 0.0405 S13: -0.0243
REMARK 3 S21: 0.0334 S22: -0.0012 S23: -0.0086
REMARK 3 S31: 0.0633 S32: 0.0135 S33: 0.0129
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 3 SOME OF THE RESIDUES ARE MODELED WITH ALTERNATE
REMARK 3 CONFORMATIONS.
REMARK 4
REMARK 4 2BKL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 17-FEB-2005.
REMARK 100 THE EBI ID CODE IS EBI-21952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-2003
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS BEAMLINE 8.2.2
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (Q315)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 225366
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.50
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.1
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.0
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1QFS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% METHOXY PEG 5K AND 0.1MES
REMARK 280 (PH 6.01).
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 57.35900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 679
REMARK 465 ALA A 680
REMARK 465 GLN A 681
REMARK 465 GLY A 682
REMARK 465 GLY A 683
REMARK 465 VAL A 684
REMARK 465 ALA A 685
REMARK 465 ALA A 686
REMARK 465 GLN A 687
REMARK 465 GLY A 688
REMARK 465 ARG A 689
REMARK 465 HIS A 690
REMARK 465 HIS A 691
REMARK 465 HIS A 692
REMARK 465 HIS A 693
REMARK 465 HIS A 694
REMARK 465 HIS A 695
REMARK 465 MET B 1
REMARK 465 ALA B 680
REMARK 465 GLN B 681
REMARK 465 GLY B 682
REMARK 465 GLY B 683
REMARK 465 VAL B 684
REMARK 465 ALA B 685
REMARK 465 ALA B 686
REMARK 465 GLN B 687
REMARK 465 GLY B 688
REMARK 465 ARG B 689
REMARK 465 HIS B 690
REMARK 465 HIS B 691
REMARK 465 HIS B 692
REMARK 465 HIS B 693
REMARK 465 HIS B 694
REMARK 465 HIS B 695
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 SER A 2 OG
REMARK 470 GLN A 678 CA C O CB CG CD OE1 NE2
REMARK 470 SER B 2 OG
REMARK 470 GLY B 679 CA C O
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 460 SD MET A 460 CE -0.516
REMARK 500 MET A 543 SD MET A 543 CE -0.263
REMARK 500 MET B 460 SD MET B 460 CE -0.484
REMARK 500 MET B 543 SD MET B 543 CE -0.239
REMARK 500
REMARK 500 REMARK: NULL
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 OD1 ASP B 70 O HOH Y 120 2.20
REMARK 500 O HOH Y 120 OD1 ASP B 70 2.20
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 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 GLN A 295 156.02 76.71
REMARK 500 GLN B 295 156.73 74.03
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (MES): MES BUFFER
REMARK 600 MOLECULE
REMARK 600 SULFATE ION (SO4): SULPHATE ION FROM CRYSTALLIZATION
REMARK 600 MEDIUM.
REMARK 600 Z-ALA PROLINAL (ZAH): Z-ALA PROLINAL IN THE ACID FORM.
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: SER 533 IS THE ACTIVE SITE SERINE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: ZAH BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: ZAH BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: ZAH BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: MES BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: MES BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: MES BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
DBREF 2BKL A 1 689 UNP Q9X5N2 Q9X5N2_MYXXA 1 689
DBREF 2BKL A 690 695 PDB 2BKL 2BKL 690 695
DBREF 2BKL B 1 689 UNP Q9X5N2 Q9X5N2_MYXXA 1 689
DBREF 2BKL B 690 695 PDB 2BKL 2BKL 690 695
SEQRES 1 A 695 MET SER TYR PRO ALA THR ARG ALA GLU GLN VAL VAL ASP
SEQRES 2 A 695 THR LEU HIS GLY VAL GLN VAL ALA ASP PRO TYR ARG TRP
SEQRES 3 A 695 LEU GLU ASP GLU LYS ALA PRO GLU VAL GLN THR TRP MET
SEQRES 4 A 695 THR ALA GLN ASN ALA HIS ALA ARG GLU ALA LEU ALA LYS
SEQRES 5 A 695 PHE PRO GLY ARG GLU ALA LEU ALA ALA ARG PHE LYS GLU
SEQRES 6 A 695 LEU PHE TYR THR ASP SER VAL SER THR PRO SER ARG ARG
SEQRES 7 A 695 ASN GLY ARG PHE PHE TYR VAL ARG THR HIS LYS ASP LYS
SEQRES 8 A 695 GLU LYS ALA ILE LEU TYR TRP ARG GLN GLY GLU SER GLY
SEQRES 9 A 695 GLN GLU LYS VAL LEU LEU ASP PRO ASN GLY TRP SER LYS
SEQRES 10 A 695 ASP GLY THR VAL SER LEU GLY THR TRP ALA VAL SER TRP
SEQRES 11 A 695 ASP GLY LYS LYS VAL ALA PHE ALA GLN LYS PRO ASN ALA
SEQRES 12 A 695 ALA ASP GLU ALA VAL LEU HIS VAL ILE ASP VAL ASP SER
SEQRES 13 A 695 GLY GLU TRP SER LYS VAL ASP VAL ILE GLU GLY GLY LYS
SEQRES 14 A 695 TYR ALA THR PRO LYS TRP THR PRO ASP SER LYS GLY PHE
SEQRES 15 A 695 TYR TYR GLU TRP LEU PRO THR ASP PRO SER ILE LYS VAL
SEQRES 16 A 695 ASP GLU ARG PRO GLY TYR THR THR ILE ARG TYR HIS THR
SEQRES 17 A 695 LEU GLY THR GLU PRO SER LYS ASP THR VAL VAL HIS GLU
SEQRES 18 A 695 ARG THR GLY ASP PRO THR THR PHE LEU GLN SER ASP LEU
SEQRES 19 A 695 SER ARG ASP GLY LYS TYR LEU PHE VAL TYR ILE LEU ARG
SEQRES 20 A 695 GLY TRP SER GLU ASN ASP VAL TYR TRP LYS ARG PRO GLY
SEQRES 21 A 695 GLU LYS ASP PHE ARG LEU LEU VAL LYS GLY VAL GLY ALA
SEQRES 22 A 695 LYS TYR GLU VAL HIS ALA TRP LYS ASP ARG PHE TYR VAL
SEQRES 23 A 695 LEU THR ASP GLU GLY ALA PRO ARG GLN ARG VAL PHE GLU
SEQRES 24 A 695 VAL ASP PRO ALA LYS PRO ALA ARG ALA SER TRP LYS GLU
SEQRES 25 A 695 ILE VAL PRO GLU ASP SER SER ALA SER LEU LEU SER VAL
SEQRES 26 A 695 SER ILE VAL GLY GLY HIS LEU SER LEU GLU TYR LEU LYS
SEQRES 27 A 695 ASP ALA THR SER GLU VAL ARG VAL ALA THR LEU LYS GLY
SEQRES 28 A 695 LYS PRO VAL ARG THR VAL GLN LEU PRO GLY VAL GLY ALA
SEQRES 29 A 695 ALA SER ASN LEU MET GLY LEU GLU ASP LEU ASP ASP ALA
SEQRES 30 A 695 TYR TYR VAL PHE THR SER PHE THR THR PRO ARG GLN ILE
SEQRES 31 A 695 TYR LYS THR SER VAL SER THR GLY LYS SER GLU LEU TRP
SEQRES 32 A 695 ALA LYS VAL ASP VAL PRO MET ASN PRO GLU GLN TYR GLN
SEQRES 33 A 695 VAL GLU GLN VAL PHE TYR ALA SER LYS ASP GLY THR LYS
SEQRES 34 A 695 VAL PRO MET PHE VAL VAL HIS ARG LYS ASP LEU LYS ARG
SEQRES 35 A 695 ASP GLY ASN ALA PRO THR LEU LEU TYR GLY TYR GLY GLY
SEQRES 36 A 695 PHE ASN VAL ASN MET GLU ALA ASN PHE ARG SER SER ILE
SEQRES 37 A 695 LEU PRO TRP LEU ASP ALA GLY GLY VAL TYR ALA VAL ALA
SEQRES 38 A 695 ASN LEU ARG GLY GLY GLY GLU TYR GLY LYS ALA TRP HIS
SEQRES 39 A 695 ASP ALA GLY ARG LEU ASP LYS LYS GLN ASN VAL PHE ASP
SEQRES 40 A 695 ASP PHE HIS ALA ALA ALA GLU TYR LEU VAL GLN GLN LYS
SEQRES 41 A 695 TYR THR GLN PRO LYS ARG LEU ALA ILE TYR GLY GLY SER
SEQRES 42 A 695 ASN GLY GLY LEU LEU VAL GLY ALA ALA MET THR GLN ARG
SEQRES 43 A 695 PRO GLU LEU TYR GLY ALA VAL VAL CYS ALA VAL PRO LEU
SEQRES 44 A 695 LEU ASP MET VAL ARG TYR HIS LEU PHE GLY SER GLY ARG
SEQRES 45 A 695 THR TRP ILE PRO GLU TYR GLY THR ALA GLU LYS PRO GLU
SEQRES 46 A 695 ASP PHE LYS THR LEU HIS ALA TYR SER PRO TYR HIS HIS
SEQRES 47 A 695 VAL ARG PRO ASP VAL ARG TYR PRO ALA LEU LEU MET MET
SEQRES 48 A 695 ALA ALA ASP HIS ASP ASP ARG VAL ASP PRO MET HIS ALA
SEQRES 49 A 695 ARG LYS PHE VAL ALA ALA VAL GLN ASN SER PRO GLY ASN
SEQRES 50 A 695 PRO ALA THR ALA LEU LEU ARG ILE GLU ALA ASN ALA GLY
SEQRES 51 A 695 HIS GLY GLY ALA ASP GLN VAL ALA LYS ALA ILE GLU SER
SEQRES 52 A 695 SER VAL ASP LEU TYR SER PHE LEU PHE GLN VAL LEU ASP
SEQRES 53 A 695 VAL GLN GLY ALA GLN GLY GLY VAL ALA ALA GLN GLY ARG
SEQRES 54 A 695 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 695 MET SER TYR PRO ALA THR ARG ALA GLU GLN VAL VAL ASP
SEQRES 2 B 695 THR LEU HIS GLY VAL GLN VAL ALA ASP PRO TYR ARG TRP
SEQRES 3 B 695 LEU GLU ASP GLU LYS ALA PRO GLU VAL GLN THR TRP MET
SEQRES 4 B 695 THR ALA GLN ASN ALA HIS ALA ARG GLU ALA LEU ALA LYS
SEQRES 5 B 695 PHE PRO GLY ARG GLU ALA LEU ALA ALA ARG PHE LYS GLU
SEQRES 6 B 695 LEU PHE TYR THR ASP SER VAL SER THR PRO SER ARG ARG
SEQRES 7 B 695 ASN GLY ARG PHE PHE TYR VAL ARG THR HIS LYS ASP LYS
SEQRES 8 B 695 GLU LYS ALA ILE LEU TYR TRP ARG GLN GLY GLU SER GLY
SEQRES 9 B 695 GLN GLU LYS VAL LEU LEU ASP PRO ASN GLY TRP SER LYS
SEQRES 10 B 695 ASP GLY THR VAL SER LEU GLY THR TRP ALA VAL SER TRP
SEQRES 11 B 695 ASP GLY LYS LYS VAL ALA PHE ALA GLN LYS PRO ASN ALA
SEQRES 12 B 695 ALA ASP GLU ALA VAL LEU HIS VAL ILE ASP VAL ASP SER
SEQRES 13 B 695 GLY GLU TRP SER LYS VAL ASP VAL ILE GLU GLY GLY LYS
SEQRES 14 B 695 TYR ALA THR PRO LYS TRP THR PRO ASP SER LYS GLY PHE
SEQRES 15 B 695 TYR TYR GLU TRP LEU PRO THR ASP PRO SER ILE LYS VAL
SEQRES 16 B 695 ASP GLU ARG PRO GLY TYR THR THR ILE ARG TYR HIS THR
SEQRES 17 B 695 LEU GLY THR GLU PRO SER LYS ASP THR VAL VAL HIS GLU
SEQRES 18 B 695 ARG THR GLY ASP PRO THR THR PHE LEU GLN SER ASP LEU
SEQRES 19 B 695 SER ARG ASP GLY LYS TYR LEU PHE VAL TYR ILE LEU ARG
SEQRES 20 B 695 GLY TRP SER GLU ASN ASP VAL TYR TRP LYS ARG PRO GLY
SEQRES 21 B 695 GLU LYS ASP PHE ARG LEU LEU VAL LYS GLY VAL GLY ALA
SEQRES 22 B 695 LYS TYR GLU VAL HIS ALA TRP LYS ASP ARG PHE TYR VAL
SEQRES 23 B 695 LEU THR ASP GLU GLY ALA PRO ARG GLN ARG VAL PHE GLU
SEQRES 24 B 695 VAL ASP PRO ALA LYS PRO ALA ARG ALA SER TRP LYS GLU
SEQRES 25 B 695 ILE VAL PRO GLU ASP SER SER ALA SER LEU LEU SER VAL
SEQRES 26 B 695 SER ILE VAL GLY GLY HIS LEU SER LEU GLU TYR LEU LYS
SEQRES 27 B 695 ASP ALA THR SER GLU VAL ARG VAL ALA THR LEU LYS GLY
SEQRES 28 B 695 LYS PRO VAL ARG THR VAL GLN LEU PRO GLY VAL GLY ALA
SEQRES 29 B 695 ALA SER ASN LEU MET GLY LEU GLU ASP LEU ASP ASP ALA
SEQRES 30 B 695 TYR TYR VAL PHE THR SER PHE THR THR PRO ARG GLN ILE
SEQRES 31 B 695 TYR LYS THR SER VAL SER THR GLY LYS SER GLU LEU TRP
SEQRES 32 B 695 ALA LYS VAL ASP VAL PRO MET ASN PRO GLU GLN TYR GLN
SEQRES 33 B 695 VAL GLU GLN VAL PHE TYR ALA SER LYS ASP GLY THR LYS
SEQRES 34 B 695 VAL PRO MET PHE VAL VAL HIS ARG LYS ASP LEU LYS ARG
SEQRES 35 B 695 ASP GLY ASN ALA PRO THR LEU LEU TYR GLY TYR GLY GLY
SEQRES 36 B 695 PHE ASN VAL ASN MET GLU ALA ASN PHE ARG SER SER ILE
SEQRES 37 B 695 LEU PRO TRP LEU ASP ALA GLY GLY VAL TYR ALA VAL ALA
SEQRES 38 B 695 ASN LEU ARG GLY GLY GLY GLU TYR GLY LYS ALA TRP HIS
SEQRES 39 B 695 ASP ALA GLY ARG LEU ASP LYS LYS GLN ASN VAL PHE ASP
SEQRES 40 B 695 ASP PHE HIS ALA ALA ALA GLU TYR LEU VAL GLN GLN LYS
SEQRES 41 B 695 TYR THR GLN PRO LYS ARG LEU ALA ILE TYR GLY GLY SER
SEQRES 42 B 695 ASN GLY GLY LEU LEU VAL GLY ALA ALA MET THR GLN ARG
SEQRES 43 B 695 PRO GLU LEU TYR GLY ALA VAL VAL CYS ALA VAL PRO LEU
SEQRES 44 B 695 LEU ASP MET VAL ARG TYR HIS LEU PHE GLY SER GLY ARG
SEQRES 45 B 695 THR TRP ILE PRO GLU TYR GLY THR ALA GLU LYS PRO GLU
SEQRES 46 B 695 ASP PHE LYS THR LEU HIS ALA TYR SER PRO TYR HIS HIS
SEQRES 47 B 695 VAL ARG PRO ASP VAL ARG TYR PRO ALA LEU LEU MET MET
SEQRES 48 B 695 ALA ALA ASP HIS ASP ASP ARG VAL ASP PRO MET HIS ALA
SEQRES 49 B 695 ARG LYS PHE VAL ALA ALA VAL GLN ASN SER PRO GLY ASN
SEQRES 50 B 695 PRO ALA THR ALA LEU LEU ARG ILE GLU ALA ASN ALA GLY
SEQRES 51 B 695 HIS GLY GLY ALA ASP GLN VAL ALA LYS ALA ILE GLU SER
SEQRES 52 B 695 SER VAL ASP LEU TYR SER PHE LEU PHE GLN VAL LEU ASP
SEQRES 53 B 695 VAL GLN GLY ALA GLN GLY GLY VAL ALA ALA GLN GLY ARG
SEQRES 54 B 695 HIS HIS HIS HIS HIS HIS
HET ZAH A1533 22
HET ZAH B1533 22
HET ZAH B1679 23
HET MES A1678 12
HET MES B1680 12
HET MES A1679 12
HET SO4 A1680 5
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM SO4 SULFATE ION
HETNAM ZAH N-[(BENZYLOXY)CARBONYL]-L-ALANYL-L-PROLINE
HETSYN ZAH Z-ALA PROLINAL
FORMUL 3 MES 3(C6 H13 N1 O4 S1)
FORMUL 4 SO4 O4 S1 2-
FORMUL 5 ZAH 3(C16 H20 N2 O5)
FORMUL 6 HOH *1371(H2 O1)
HELIX 1 1 TYR A 24 ASP A 29 5 6
HELIX 2 2 ALA A 32 LYS A 52 1 21
HELIX 3 3 GLY A 55 TYR A 68 1 14
HELIX 4 4 ASP A 111 TRP A 115 5 5
HELIX 5 5 LYS A 194 THR A 202 5 9
HELIX 6 6 GLU A 212 ASP A 216 5 5
HELIX 7 7 ALA A 306 TRP A 310 5 5
HELIX 8 8 ASN A 411 GLU A 413 5 3
HELIX 9 9 ARG A 465 SER A 467 5 3
HELIX 10 10 ILE A 468 ALA A 474 1 7
HELIX 11 11 GLY A 490 ALA A 496 1 7
HELIX 12 12 GLY A 497 LYS A 501 5 5
HELIX 13 13 LYS A 502 GLN A 519 1 18
HELIX 14 14 GLN A 523 LYS A 525 5 3
HELIX 15 15 ASN A 534 ARG A 546 1 13
HELIX 16 16 PRO A 547 TYR A 550 5 4
HELIX 17 17 ARG A 564 PHE A 568 5 5
HELIX 18 18 SER A 570 THR A 573 5 4
HELIX 19 19 TRP A 574 GLY A 579 1 6
HELIX 20 20 LYS A 583 SER A 594 1 12
HELIX 21 21 PRO A 595 HIS A 598 5 4
HELIX 22 22 PRO A 621 ASN A 633 1 13
HELIX 23 23 GLN A 656 LEU A 675 1 20
HELIX 24 24 TYR B 24 ASP B 29 5 6
HELIX 25 25 ALA B 32 LYS B 52 1 21
HELIX 26 26 GLY B 55 TYR B 68 1 14
HELIX 27 27 ASP B 111 TRP B 115 5 5
HELIX 28 28 GLU B 197 THR B 202 5 6
HELIX 29 29 GLU B 212 ASP B 216 5 5
HELIX 30 30 ALA B 306 TRP B 310 5 5
HELIX 31 31 ASN B 411 GLU B 413 5 3
HELIX 32 32 ARG B 465 SER B 467 5 3
HELIX 33 33 ILE B 468 ALA B 474 1 7
HELIX 34 34 GLY B 490 ALA B 496 1 7
HELIX 35 35 GLY B 497 ASP B 500 5 4
HELIX 36 36 LYS B 501 GLN B 519 1 19
HELIX 37 37 GLN B 523 LYS B 525 5 3
HELIX 38 38 ASN B 534 ARG B 546 1 13
HELIX 39 39 PRO B 547 TYR B 550 5 4
HELIX 40 40 ARG B 564 PHE B 568 5 5
HELIX 41 41 SER B 570 THR B 573 5 4
HELIX 42 42 TRP B 574 GLY B 579 1 6
HELIX 43 43 LYS B 583 SER B 594 1 12
HELIX 44 44 PRO B 595 HIS B 598 5 4
HELIX 45 45 PRO B 621 ASN B 633 1 13
HELIX 46 46 GLN B 656 LEU B 675 1 20
SHEET 1 AA 2 VAL A 12 LEU A 15 0
SHEET 2 AA 2 VAL A 18 ALA A 21 -1 O VAL A 18 N LEU A 15
SHEET 1 AB 3 SER A 71 VAL A 72 0
SHEET 2 AB 3 ARG A 81 THR A 87 -1 O THR A 87 N SER A 71
SHEET 3 AB 3 SER A 76 ARG A 78 -1 O SER A 76 N PHE A 83
SHEET 1 AC 4 SER A 71 VAL A 72 0
SHEET 2 AC 4 ARG A 81 THR A 87 -1 O THR A 87 N SER A 71
SHEET 3 AC 4 ILE A 95 GLN A 100 -1 O ILE A 95 N ARG A 86
SHEET 4 AC 4 LYS A 107 LEU A 110 -1 O LYS A 107 N TRP A 98
SHEET 1 AD 3 VAL A 121 VAL A 128 0
SHEET 2 AD 3 LYS A 134 PRO A 141 -1 O ALA A 136 N ALA A 127
SHEET 3 AD 3 VAL A 148 ASP A 153 -1 O VAL A 148 N GLN A 139
SHEET 1 AE 4 LYS A 174 TRP A 175 0
SHEET 2 AE 4 GLY A 181 TRP A 186 -1 O TYR A 183 N LYS A 174
SHEET 3 AE 4 THR A 203 THR A 208 -1 O THR A 203 N TRP A 186
SHEET 4 AE 4 THR A 217 HIS A 220 -1 O THR A 217 N TYR A 206
SHEET 1 AF 4 PHE A 229 LEU A 234 0
SHEET 2 AF 4 LEU A 241 ARG A 247 -1 O PHE A 242 N ASP A 233
SHEET 3 AF 4 GLU A 251 LYS A 257 -1 O GLU A 251 N ARG A 247
SHEET 4 AF 4 ARG A 265 LYS A 269 -1 O ARG A 265 N TRP A 256
SHEET 1 AG 4 TYR A 275 TRP A 280 0
SHEET 2 AG 4 ARG A 283 THR A 288 -1 O ARG A 283 N TRP A 280
SHEET 3 AG 4 ARG A 296 VAL A 300 -1 O ARG A 296 N THR A 288
SHEET 4 AG 4 LYS A 311 VAL A 314 -1 O LYS A 311 N GLU A 299
SHEET 1 AH 4 SER A 321 VAL A 328 0
SHEET 2 AH 4 HIS A 331 LYS A 338 -1 O HIS A 331 N VAL A 328
SHEET 3 AH 4 THR A 341 THR A 348 -1 O THR A 341 N LYS A 338
SHEET 4 AH 4 PRO A 353 THR A 356 -1 N VAL A 354 O VAL A 346
SHEET 1 AI 4 ALA A 364 ALA A 365 0
SHEET 2 AI 4 ASP A 376 SER A 383 -1 O THR A 382 N ALA A 364
SHEET 3 AI 4 THR A 386 SER A 394 -1 O THR A 386 N SER A 383
SHEET 4 AI 4 SER A 400 LYS A 405 -1 O GLU A 401 N LYS A 392
SHEET 1 AJ 8 TYR A 415 ALA A 423 0
SHEET 2 AJ 8 LYS A 429 ARG A 437 -1 O VAL A 430 N TYR A 422
SHEET 3 AJ 8 VAL A 477 ALA A 481 -1 O TYR A 478 N VAL A 435
SHEET 4 AJ 8 THR A 448 TYR A 451 1 O LEU A 449 N ALA A 479
SHEET 5 AJ 8 LEU A 527 GLY A 531 1 O ALA A 528 N LEU A 450
SHEET 6 AJ 8 ALA A 552 ALA A 556 1 O ALA A 552 N ILE A 529
SHEET 7 AJ 8 ALA A 607 ALA A 613 1 O ALA A 607 N VAL A 553
SHEET 8 AJ 8 ALA A 641 GLU A 646 1 O LEU A 642 N MET A 610
SHEET 1 BA 2 VAL B 12 LEU B 15 0
SHEET 2 BA 2 VAL B 18 ALA B 21 -1 O VAL B 18 N LEU B 15
SHEET 1 BB 3 SER B 71 VAL B 72 0
SHEET 2 BB 3 ARG B 81 THR B 87 -1 O THR B 87 N SER B 71
SHEET 3 BB 3 SER B 76 ARG B 78 -1 O SER B 76 N PHE B 83
SHEET 1 BC 4 SER B 71 VAL B 72 0
SHEET 2 BC 4 ARG B 81 THR B 87 -1 O THR B 87 N SER B 71
SHEET 3 BC 4 ILE B 95 GLN B 100 -1 O ILE B 95 N ARG B 86
SHEET 4 BC 4 LYS B 107 LEU B 110 -1 O LYS B 107 N TRP B 98
SHEET 1 BD 3 VAL B 121 VAL B 128 0
SHEET 2 BD 3 LYS B 134 PRO B 141 -1 O ALA B 136 N ALA B 127
SHEET 3 BD 3 VAL B 148 ASP B 153 -1 O VAL B 148 N GLN B 139
SHEET 1 BE 4 LYS B 174 TRP B 175 0
SHEET 2 BE 4 GLY B 181 TRP B 186 -1 O TYR B 183 N LYS B 174
SHEET 3 BE 4 THR B 203 THR B 208 -1 O THR B 203 N TRP B 186
SHEET 4 BE 4 THR B 217 HIS B 220 -1 O THR B 217 N TYR B 206
SHEET 1 BF 4 PHE B 229 LEU B 234 0
SHEET 2 BF 4 LEU B 241 ARG B 247 -1 O PHE B 242 N ASP B 233
SHEET 3 BF 4 GLU B 251 LYS B 257 -1 O GLU B 251 N ARG B 247
SHEET 4 BF 4 ARG B 265 LYS B 269 -1 O ARG B 265 N TRP B 256
SHEET 1 BG 4 TYR B 275 TRP B 280 0
SHEET 2 BG 4 ARG B 283 THR B 288 -1 O ARG B 283 N TRP B 280
SHEET 3 BG 4 ARG B 296 VAL B 300 -1 O ARG B 296 N THR B 288
SHEET 4 BG 4 LYS B 311 VAL B 314 -1 O LYS B 311 N GLU B 299
SHEET 1 BH 4 SER B 321 VAL B 328 0
SHEET 2 BH 4 HIS B 331 LYS B 338 -1 O HIS B 331 N VAL B 328
SHEET 3 BH 4 THR B 341 THR B 348 -1 O THR B 341 N LYS B 338
SHEET 4 BH 4 PRO B 353 THR B 356 -1 N VAL B 354 O VAL B 346
SHEET 1 BI 4 ALA B 364 ALA B 365 0
SHEET 2 BI 4 ASP B 376 SER B 383 -1 O THR B 382 N ALA B 364
SHEET 3 BI 4 THR B 386 SER B 394 -1 O THR B 386 N SER B 383
SHEET 4 BI 4 SER B 400 LYS B 405 -1 O GLU B 401 N LYS B 392
SHEET 1 BJ 8 TYR B 415 ALA B 423 0
SHEET 2 BJ 8 LYS B 429 ARG B 437 -1 O VAL B 430 N TYR B 422
SHEET 3 BJ 8 VAL B 477 ALA B 481 -1 O TYR B 478 N VAL B 435
SHEET 4 BJ 8 THR B 448 TYR B 451 1 O LEU B 449 N ALA B 479
SHEET 5 BJ 8 LEU B 527 GLY B 531 1 O ALA B 528 N LEU B 450
SHEET 6 BJ 8 ALA B 552 ALA B 556 1 O ALA B 552 N ILE B 529
SHEET 7 BJ 8 ALA B 607 ALA B 613 1 O ALA B 607 N VAL B 553
SHEET 8 BJ 8 ALA B 641 GLU B 646 1 O LEU B 642 N MET B 610
LINK OG SER A 533 C1 ZAH A1533 1555 1555
LINK OG SER B 533 C1 ZAH B1533 1555 1555
SITE 1 CAT 2 SER A 533 SER B 533
SITE 1 AC1 12 LYS A 169 TYR A 170 TRP A 249 TYR A 453
SITE 2 AC1 12 PHE A 456 SER A 533 ASN A 534 TRP A 574
SITE 3 AC1 12 ARG A 618 HIS A 651 HOH Z 568 HOH Z 569
SITE 1 AC2 10 TRP B 249 TYR B 453 PHE B 456 SER B 533
SITE 2 AC2 10 ASN B 534 TRP B 574 ARG B 618 HIS B 651
SITE 3 AC2 10 HOH Y 576 HOH Y 577
SITE 1 AC3 9 ASN A 79 LYS A 133 TYR B 84 ARG B 99
SITE 2 AC3 9 GLU B 102 TRP B 403 HOH Y 169 HOH Y 690
SITE 3 AC3 9 HOH Z 135
SITE 1 AC4 8 ALA A 21 HIS A 591 HIS A 597 ARG A 600
SITE 2 AC4 8 PRO A 601 HOH Z 49 HOH Z 676 HOH Z 677
SITE 1 AC5 8 ALA B 21 HIS B 591 HIS B 597 ARG B 600
SITE 2 AC5 8 HOH Y 41 HOH Y 627 HOH Y 691 HOH Y 692
SITE 1 AC6 7 TYR A 183 THR A 217 LEU A 241 LYS A 257
SITE 2 AC6 7 PRO A 259 GLY A 260 HOH Z 349
SITE 1 AC7 5 THR A 176 PRO A 177 ASP A 178 HOH Z 678
SITE 2 AC7 5 HOH Z 679
CRYST1 65.692 114.718 99.279 90.00 103.60 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015223 0.000000 0.003683 0.00000
SCALE2 0.000000 0.008717 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010363 0.00000
TER 5358 GLN A 678
TER 10725 GLY B 679
MASTER 451 0 7 46 80 0 18 612202 2 110 108
END |