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HEADER HYDROLASE 13-SEP-02 1MPX
TITLE ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH
TITLE 2 SELENOMETHIONINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMINO ACID ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.43;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS CITRI;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PXC
KEYWDS ALPHA/BETA HYDROLASE, JELLYROLL, SELENOMETHIONINE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,C.M.H.HENSGENS,
AUTHOR 2 E.J.DE VRIES,D.B.JANSSEN,B.W.DIJKSTRA
REVDAT 1 15-APR-03 1MPX 0
JRNL AUTH T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,
JRNL AUTH 2 C.M.H.HENSGENS,E.J.DE VRIES,D.B.JANSSEN,
JRNL AUTH 3 B.W.DIJKSTRA
JRNL TITL THE SEQUENCE AND CRYSTAL STRUCTURE OF THE ALPHA
JRNL TITL 2 -AMINO ACID ESTER HYDROLASE FROM XANTHOMONAS CITRI
JRNL TITL 3 DEFINE A NEW FAMILY OF BETA -LACTAM ANTIBIOTIC
JRNL TITL 4 ACYLASES.
JRNL REF J.BIOL.CHEM. 2003
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 209646
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11118
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15490
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 848
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 21702
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.57000
REMARK 3 B22 (A**2) : -0.47000
REMARK 3 B33 (A**2) : 1.03000
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): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.650
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20058 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 17546 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27338 ; 1.143 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): 40910 ; 0.713 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2452 ; 2.712 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2832 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22556 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4196 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3857 ; 0.181 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 21151 ; 0.221 ; 0.300
REMARK 3 NON-BONDED TORSION OTHERS (A): 10952 ; 0.084 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2949 ; 0.158 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.079 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 70 ; 0.220 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 40 ; 0.122 ; 0.500
REMARK 3 SYMMETRY H-BOND 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): 12296 ; 1.552 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19872 ; 2.377 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7762 ; 3.721 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7466 ; 5.463 ; 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 : 0
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 1MPX COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-2002.
REMARK 100 THE RCSB ID CODE IS RCSB017083.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-NOV-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8459, 0.9779, 0.9783, 0.9392
REMARK 200 MONOCHROMATOR : TRIANGULAR
REMARK 200 OPTICS : PREMIRROR, TRIANGULAR
REMARK 200 MONOCHROMATOR, BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 220969
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SNB2.1, SOLVE/RESOLVE, ARP/WARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CACODYLATE, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 63.00800
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 4 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, B, C, D
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 GLN A 23
REMARK 465 GLN B 23
REMARK 465 GLN C 23
REMARK 465 GLN D 23
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 VAL A 453 CB VAL A 453 CG1 -0.084
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 ILE A 31 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ILE A 113 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP A 208 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 GLY A 313 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 ASN A 575 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 PHE A 578 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 LEU A 592 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ASN A 599 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 THR A 602 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ILE B 31 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ILE B 113 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP B 208 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 GLY B 313 N - CA - C ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASN B 575 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 PHE B 578 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 LEU B 592 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 THR B 602 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ILE C 31 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 ILE C 113 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP C 208 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 GLY C 313 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG C 339 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 LEU C 421 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASN C 575 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 LEU C 592 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASN C 599 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 THR C 602 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 ILE D 31 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ILE D 113 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP D 208 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLY D 313 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU D 421 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 LEU D 519 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASN D 575 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 LEU D 592 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASN D 599 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 THR D 602 N - CA - C ANGL. DEV. =-10.2 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 TYR A 123 -115.68 45.59
REMARK 500 SER A 174 -118.32 65.14
REMARK 500 TYR B 123 -115.60 46.88
REMARK 500 TYR C 123 -114.65 47.28
REMARK 500 SER C 174 -118.11 65.55
REMARK 500 TYR D 123 -111.73 49.00
DBREF 1MPX A 23 637 GB 21108589 AAM37193 23 637
DBREF 1MPX B 23 637 GB 21108589 AAM37193 23 637
DBREF 1MPX C 23 637 GB 21108589 AAM37193 23 637
DBREF 1MPX D 23 637 GB 21108589 AAM37193 23 637
SEQADV 1MPX MSE A 27 GB 21108589 MET 27 MODIFIED RESIDUE
SEQADV 1MPX MSE A 51 GB 21108589 MET 51 MODIFIED RESIDUE
SEQADV 1MPX MSE A 54 GB 21108589 MET 54 MODIFIED RESIDUE
SEQADV 1MPX MSE A 96 GB 21108589 MET 96 MODIFIED RESIDUE
SEQADV 1MPX MSE A 131 GB 21108589 MET 131 MODIFIED RESIDUE
SEQADV 1MPX MSE A 170 GB 21108589 MET 170 MODIFIED RESIDUE
SEQADV 1MPX MSE A 182 GB 21108589 MET 182 MODIFIED RESIDUE
SEQADV 1MPX MSE A 200 GB 21108589 MET 200 MODIFIED RESIDUE
SEQADV 1MPX MSE A 205 GB 21108589 MET 205 MODIFIED RESIDUE
SEQADV 1MPX MSE A 290 GB 21108589 MET 290 MODIFIED RESIDUE
SEQADV 1MPX MSE A 300 GB 21108589 MET 300 MODIFIED RESIDUE
SEQADV 1MPX MSE A 311 GB 21108589 MET 311 MODIFIED RESIDUE
SEQADV 1MPX MSE A 321 GB 21108589 MET 321 MODIFIED RESIDUE
SEQADV 1MPX MSE A 335 GB 21108589 MET 335 MODIFIED RESIDUE
SEQADV 1MPX MSE A 464 GB 21108589 MET 464 MODIFIED RESIDUE
SEQADV 1MPX MSE A 527 GB 21108589 MET 527 MODIFIED RESIDUE
SEQADV 1MPX MSE A 533 GB 21108589 MET 533 MODIFIED RESIDUE
SEQADV 1MPX MSE A 585 GB 21108589 MET 585 MODIFIED RESIDUE
SEQADV 1MPX MSE B 27 GB 21108589 MET 27 MODIFIED RESIDUE
SEQADV 1MPX MSE B 51 GB 21108589 MET 51 MODIFIED RESIDUE
SEQADV 1MPX MSE B 54 GB 21108589 MET 54 MODIFIED RESIDUE
SEQADV 1MPX MSE B 96 GB 21108589 MET 96 MODIFIED RESIDUE
SEQADV 1MPX MSE B 131 GB 21108589 MET 131 MODIFIED RESIDUE
SEQADV 1MPX MSE B 170 GB 21108589 MET 170 MODIFIED RESIDUE
SEQADV 1MPX MSE B 182 GB 21108589 MET 182 MODIFIED RESIDUE
SEQADV 1MPX MSE B 200 GB 21108589 MET 200 MODIFIED RESIDUE
SEQADV 1MPX MSE B 205 GB 21108589 MET 205 MODIFIED RESIDUE
SEQADV 1MPX MSE B 290 GB 21108589 MET 290 MODIFIED RESIDUE
SEQADV 1MPX MSE B 300 GB 21108589 MET 300 MODIFIED RESIDUE
SEQADV 1MPX MSE B 311 GB 21108589 MET 311 MODIFIED RESIDUE
SEQADV 1MPX MSE B 321 GB 21108589 MET 321 MODIFIED RESIDUE
SEQADV 1MPX MSE B 335 GB 21108589 MET 335 MODIFIED RESIDUE
SEQADV 1MPX MSE B 464 GB 21108589 MET 464 MODIFIED RESIDUE
SEQADV 1MPX MSE B 527 GB 21108589 MET 527 MODIFIED RESIDUE
SEQADV 1MPX MSE B 533 GB 21108589 MET 533 MODIFIED RESIDUE
SEQADV 1MPX MSE B 585 GB 21108589 MET 585 MODIFIED RESIDUE
SEQADV 1MPX MSE C 27 GB 21108589 MET 27 MODIFIED RESIDUE
SEQADV 1MPX MSE C 51 GB 21108589 MET 51 MODIFIED RESIDUE
SEQADV 1MPX MSE C 54 GB 21108589 MET 54 MODIFIED RESIDUE
SEQADV 1MPX MSE C 96 GB 21108589 MET 96 MODIFIED RESIDUE
SEQADV 1MPX MSE C 131 GB 21108589 MET 131 MODIFIED RESIDUE
SEQADV 1MPX MSE C 170 GB 21108589 MET 170 MODIFIED RESIDUE
SEQADV 1MPX MSE C 182 GB 21108589 MET 182 MODIFIED RESIDUE
SEQADV 1MPX MSE C 200 GB 21108589 MET 200 MODIFIED RESIDUE
SEQADV 1MPX MSE C 205 GB 21108589 MET 205 MODIFIED RESIDUE
SEQADV 1MPX MSE C 290 GB 21108589 MET 290 MODIFIED RESIDUE
SEQADV 1MPX MSE C 300 GB 21108589 MET 300 MODIFIED RESIDUE
SEQADV 1MPX MSE C 311 GB 21108589 MET 311 MODIFIED RESIDUE
SEQADV 1MPX MSE C 321 GB 21108589 MET 321 MODIFIED RESIDUE
SEQADV 1MPX MSE C 335 GB 21108589 MET 335 MODIFIED RESIDUE
SEQADV 1MPX MSE C 464 GB 21108589 MET 464 MODIFIED RESIDUE
SEQADV 1MPX MSE C 527 GB 21108589 MET 527 MODIFIED RESIDUE
SEQADV 1MPX MSE C 533 GB 21108589 MET 533 MODIFIED RESIDUE
SEQADV 1MPX MSE C 585 GB 21108589 MET 585 MODIFIED RESIDUE
SEQADV 1MPX MSE D 27 GB 21108589 MET 27 MODIFIED RESIDUE
SEQADV 1MPX MSE D 51 GB 21108589 MET 51 MODIFIED RESIDUE
SEQADV 1MPX MSE D 54 GB 21108589 MET 54 MODIFIED RESIDUE
SEQADV 1MPX MSE D 96 GB 21108589 MET 96 MODIFIED RESIDUE
SEQADV 1MPX MSE D 131 GB 21108589 MET 131 MODIFIED RESIDUE
SEQADV 1MPX MSE D 170 GB 21108589 MET 170 MODIFIED RESIDUE
SEQADV 1MPX MSE D 182 GB 21108589 MET 182 MODIFIED RESIDUE
SEQADV 1MPX MSE D 200 GB 21108589 MET 200 MODIFIED RESIDUE
SEQADV 1MPX MSE D 205 GB 21108589 MET 205 MODIFIED RESIDUE
SEQADV 1MPX MSE D 290 GB 21108589 MET 290 MODIFIED RESIDUE
SEQADV 1MPX MSE D 300 GB 21108589 MET 300 MODIFIED RESIDUE
SEQADV 1MPX MSE D 311 GB 21108589 MET 311 MODIFIED RESIDUE
SEQADV 1MPX MSE D 321 GB 21108589 MET 321 MODIFIED RESIDUE
SEQADV 1MPX MSE D 335 GB 21108589 MET 335 MODIFIED RESIDUE
SEQADV 1MPX MSE D 464 GB 21108589 MET 464 MODIFIED RESIDUE
SEQADV 1MPX MSE D 527 GB 21108589 MET 527 MODIFIED RESIDUE
SEQADV 1MPX MSE D 533 GB 21108589 MET 533 MODIFIED RESIDUE
SEQADV 1MPX MSE D 585 GB 21108589 MET 585 MODIFIED RESIDUE
SEQRES 1 A 615 GLN THR SER PRO MSE THR PRO ASP ILE THR GLY LYS PRO
SEQRES 2 A 615 PHE VAL ALA ALA ASP ALA SER ASN ASP TYR ILE LYS ARG
SEQRES 3 A 615 GLU VAL MSE ILE PRO MSE ARG ASP GLY VAL LYS LEU HIS
SEQRES 4 A 615 THR VAL ILE VAL LEU PRO LYS GLY ALA LYS ASN ALA PRO
SEQRES 5 A 615 ILE VAL LEU THR ARG THR PRO TYR ASP ALA SER GLY ARG
SEQRES 6 A 615 THR GLU ARG LEU ALA SER PRO HIS MSE LYS ASP LEU LEU
SEQRES 7 A 615 SER ALA GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 8 A 615 ARG VAL PHE GLN ASP VAL ARG GLY LYS TYR GLY SER GLU
SEQRES 9 A 615 GLY ASP TYR VAL MSE THR ARG PRO LEU ARG GLY PRO LEU
SEQRES 10 A 615 ASN PRO SER GLU VAL ASP HIS ALA THR ASP ALA TRP ASP
SEQRES 11 A 615 THR ILE ASP TRP LEU VAL LYS ASN VAL SER GLU SER ASN
SEQRES 12 A 615 GLY LYS VAL GLY MSE ILE GLY SER SER TYR GLU GLY PHE
SEQRES 13 A 615 THR VAL VAL MSE ALA LEU THR ASN PRO HIS PRO ALA LEU
SEQRES 14 A 615 LYS VAL ALA VAL PRO GLU SER PRO MSE ILE ASP GLY TRP
SEQRES 15 A 615 MSE GLY ASP ASP TRP PHE ASN TYR GLY ALA PHE ARG GLN
SEQRES 16 A 615 VAL ASN PHE ASP TYR PHE THR GLY GLN LEU SER LYS ARG
SEQRES 17 A 615 GLY LYS GLY ALA GLY ILE ALA ARG GLN GLY HIS ASP ASP
SEQRES 18 A 615 TYR SER ASN PHE LEU GLN ALA GLY SER ALA GLY ASP PHE
SEQRES 19 A 615 ALA LYS ALA ALA GLY LEU GLU GLN LEU PRO TRP TRP HIS
SEQRES 20 A 615 LYS LEU THR GLU HIS ALA ALA TYR ASP ALA PHE TRP GLN
SEQRES 21 A 615 GLU GLN ALA LEU ASP LYS VAL MSE ALA ARG THR PRO LEU
SEQRES 22 A 615 LYS VAL PRO THR MSE TRP LEU GLN GLY LEU TRP ASP GLN
SEQRES 23 A 615 GLU ASP MSE TRP GLY ALA ILE HIS SER TYR ALA ALA MSE
SEQRES 24 A 615 GLU PRO ARG ASP LYS ARG ASN THR LEU ASN TYR LEU VAL
SEQRES 25 A 615 MSE GLY PRO TRP ARG HIS SER GLN VAL ASN TYR ASP GLY
SEQRES 26 A 615 SER ALA LEU GLY ALA LEU ASN PHE GLU GLY ASP THR ALA
SEQRES 27 A 615 ARG GLN PHE ARG HIS ASP VAL LEU ARG PRO PHE PHE ASP
SEQRES 28 A 615 GLN TYR LEU VAL ASP GLY ALA PRO LYS ALA ASP THR PRO
SEQRES 29 A 615 PRO VAL PHE ILE TYR ASN THR GLY GLU ASN HIS TRP ASP
SEQRES 30 A 615 ARG LEU LYS ALA TRP PRO ARG SER CYS ASP LYS GLY CYS
SEQRES 31 A 615 ALA ALA THR SER LYS PRO LEU TYR LEU GLN ALA GLY GLY
SEQRES 32 A 615 LYS LEU SER PHE GLN PRO PRO VAL ALA GLY GLN ALA GLY
SEQRES 33 A 615 PHE GLU GLU TYR VAL SER ASP PRO ALA LYS PRO VAL PRO
SEQRES 34 A 615 PHE VAL PRO ARG PRO VAL ASP PHE ALA ASP ARG ALA MSE
SEQRES 35 A 615 TRP THR THR TRP LEU VAL HIS ASP GLN ARG PHE VAL ASP
SEQRES 36 A 615 GLY ARG PRO ASP VAL LEU THR PHE VAL THR GLU PRO LEU
SEQRES 37 A 615 THR GLU PRO LEU GLN ILE ALA GLY ALA PRO ASP VAL HIS
SEQRES 38 A 615 LEU GLN ALA SER THR SER GLY SER ASP SER ASP TRP VAL
SEQRES 39 A 615 VAL LYS LEU ILE ASP VAL TYR PRO GLU GLU MSE ALA SER
SEQRES 40 A 615 ASN PRO LYS MSE GLY GLY TYR GLU LEU PRO VAL SER LEU
SEQRES 41 A 615 ALA ILE PHE ARG GLY ARG TYR ARG GLU SER PHE SER THR
SEQRES 42 A 615 PRO LYS PRO LEU THR SER ASN GLN PRO LEU ALA PHE GLN
SEQRES 43 A 615 PHE GLY LEU PRO THR ALA ASN HIS THR PHE GLN PRO GLY
SEQRES 44 A 615 HIS ARG VAL MSE VAL GLN VAL GLN SER SER LEU PHE PRO
SEQRES 45 A 615 LEU TYR ASP ARG ASN PRO GLN THR TYR VAL PRO ASN ILE
SEQRES 46 A 615 PHE PHE ALA LYS PRO GLY ASP TYR GLN LYS ALA THR GLN
SEQRES 47 A 615 ARG VAL TYR VAL SER PRO GLU GLN PRO SER TYR ILE SER
SEQRES 48 A 615 LEU PRO VAL ARG
SEQRES 1 B 615 GLN THR SER PRO MSE THR PRO ASP ILE THR GLY LYS PRO
SEQRES 2 B 615 PHE VAL ALA ALA ASP ALA SER ASN ASP TYR ILE LYS ARG
SEQRES 3 B 615 GLU VAL MSE ILE PRO MSE ARG ASP GLY VAL LYS LEU HIS
SEQRES 4 B 615 THR VAL ILE VAL LEU PRO LYS GLY ALA LYS ASN ALA PRO
SEQRES 5 B 615 ILE VAL LEU THR ARG THR PRO TYR ASP ALA SER GLY ARG
SEQRES 6 B 615 THR GLU ARG LEU ALA SER PRO HIS MSE LYS ASP LEU LEU
SEQRES 7 B 615 SER ALA GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 8 B 615 ARG VAL PHE GLN ASP VAL ARG GLY LYS TYR GLY SER GLU
SEQRES 9 B 615 GLY ASP TYR VAL MSE THR ARG PRO LEU ARG GLY PRO LEU
SEQRES 10 B 615 ASN PRO SER GLU VAL ASP HIS ALA THR ASP ALA TRP ASP
SEQRES 11 B 615 THR ILE ASP TRP LEU VAL LYS ASN VAL SER GLU SER ASN
SEQRES 12 B 615 GLY LYS VAL GLY MSE ILE GLY SER SER TYR GLU GLY PHE
SEQRES 13 B 615 THR VAL VAL MSE ALA LEU THR ASN PRO HIS PRO ALA LEU
SEQRES 14 B 615 LYS VAL ALA VAL PRO GLU SER PRO MSE ILE ASP GLY TRP
SEQRES 15 B 615 MSE GLY ASP ASP TRP PHE ASN TYR GLY ALA PHE ARG GLN
SEQRES 16 B 615 VAL ASN PHE ASP TYR PHE THR GLY GLN LEU SER LYS ARG
SEQRES 17 B 615 GLY LYS GLY ALA GLY ILE ALA ARG GLN GLY HIS ASP ASP
SEQRES 18 B 615 TYR SER ASN PHE LEU GLN ALA GLY SER ALA GLY ASP PHE
SEQRES 19 B 615 ALA LYS ALA ALA GLY LEU GLU GLN LEU PRO TRP TRP HIS
SEQRES 20 B 615 LYS LEU THR GLU HIS ALA ALA TYR ASP ALA PHE TRP GLN
SEQRES 21 B 615 GLU GLN ALA LEU ASP LYS VAL MSE ALA ARG THR PRO LEU
SEQRES 22 B 615 LYS VAL PRO THR MSE TRP LEU GLN GLY LEU TRP ASP GLN
SEQRES 23 B 615 GLU ASP MSE TRP GLY ALA ILE HIS SER TYR ALA ALA MSE
SEQRES 24 B 615 GLU PRO ARG ASP LYS ARG ASN THR LEU ASN TYR LEU VAL
SEQRES 25 B 615 MSE GLY PRO TRP ARG HIS SER GLN VAL ASN TYR ASP GLY
SEQRES 26 B 615 SER ALA LEU GLY ALA LEU ASN PHE GLU GLY ASP THR ALA
SEQRES 27 B 615 ARG GLN PHE ARG HIS ASP VAL LEU ARG PRO PHE PHE ASP
SEQRES 28 B 615 GLN TYR LEU VAL ASP GLY ALA PRO LYS ALA ASP THR PRO
SEQRES 29 B 615 PRO VAL PHE ILE TYR ASN THR GLY GLU ASN HIS TRP ASP
SEQRES 30 B 615 ARG LEU LYS ALA TRP PRO ARG SER CYS ASP LYS GLY CYS
SEQRES 31 B 615 ALA ALA THR SER LYS PRO LEU TYR LEU GLN ALA GLY GLY
SEQRES 32 B 615 LYS LEU SER PHE GLN PRO PRO VAL ALA GLY GLN ALA GLY
SEQRES 33 B 615 PHE GLU GLU TYR VAL SER ASP PRO ALA LYS PRO VAL PRO
SEQRES 34 B 615 PHE VAL PRO ARG PRO VAL ASP PHE ALA ASP ARG ALA MSE
SEQRES 35 B 615 TRP THR THR TRP LEU VAL HIS ASP GLN ARG PHE VAL ASP
SEQRES 36 B 615 GLY ARG PRO ASP VAL LEU THR PHE VAL THR GLU PRO LEU
SEQRES 37 B 615 THR GLU PRO LEU GLN ILE ALA GLY ALA PRO ASP VAL HIS
SEQRES 38 B 615 LEU GLN ALA SER THR SER GLY SER ASP SER ASP TRP VAL
SEQRES 39 B 615 VAL LYS LEU ILE ASP VAL TYR PRO GLU GLU MSE ALA SER
SEQRES 40 B 615 ASN PRO LYS MSE GLY GLY TYR GLU LEU PRO VAL SER LEU
SEQRES 41 B 615 ALA ILE PHE ARG GLY ARG TYR ARG GLU SER PHE SER THR
SEQRES 42 B 615 PRO LYS PRO LEU THR SER ASN GLN PRO LEU ALA PHE GLN
SEQRES 43 B 615 PHE GLY LEU PRO THR ALA ASN HIS THR PHE GLN PRO GLY
SEQRES 44 B 615 HIS ARG VAL MSE VAL GLN VAL GLN SER SER LEU PHE PRO
SEQRES 45 B 615 LEU TYR ASP ARG ASN PRO GLN THR TYR VAL PRO ASN ILE
SEQRES 46 B 615 PHE PHE ALA LYS PRO GLY ASP TYR GLN LYS ALA THR GLN
SEQRES 47 B 615 ARG VAL TYR VAL SER PRO GLU GLN PRO SER TYR ILE SER
SEQRES 48 B 615 LEU PRO VAL ARG
SEQRES 1 C 615 GLN THR SER PRO MSE THR PRO ASP ILE THR GLY LYS PRO
SEQRES 2 C 615 PHE VAL ALA ALA ASP ALA SER ASN ASP TYR ILE LYS ARG
SEQRES 3 C 615 GLU VAL MSE ILE PRO MSE ARG ASP GLY VAL LYS LEU HIS
SEQRES 4 C 615 THR VAL ILE VAL LEU PRO LYS GLY ALA LYS ASN ALA PRO
SEQRES 5 C 615 ILE VAL LEU THR ARG THR PRO TYR ASP ALA SER GLY ARG
SEQRES 6 C 615 THR GLU ARG LEU ALA SER PRO HIS MSE LYS ASP LEU LEU
SEQRES 7 C 615 SER ALA GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 8 C 615 ARG VAL PHE GLN ASP VAL ARG GLY LYS TYR GLY SER GLU
SEQRES 9 C 615 GLY ASP TYR VAL MSE THR ARG PRO LEU ARG GLY PRO LEU
SEQRES 10 C 615 ASN PRO SER GLU VAL ASP HIS ALA THR ASP ALA TRP ASP
SEQRES 11 C 615 THR ILE ASP TRP LEU VAL LYS ASN VAL SER GLU SER ASN
SEQRES 12 C 615 GLY LYS VAL GLY MSE ILE GLY SER SER TYR GLU GLY PHE
SEQRES 13 C 615 THR VAL VAL MSE ALA LEU THR ASN PRO HIS PRO ALA LEU
SEQRES 14 C 615 LYS VAL ALA VAL PRO GLU SER PRO MSE ILE ASP GLY TRP
SEQRES 15 C 615 MSE GLY ASP ASP TRP PHE ASN TYR GLY ALA PHE ARG GLN
SEQRES 16 C 615 VAL ASN PHE ASP TYR PHE THR GLY GLN LEU SER LYS ARG
SEQRES 17 C 615 GLY LYS GLY ALA GLY ILE ALA ARG GLN GLY HIS ASP ASP
SEQRES 18 C 615 TYR SER ASN PHE LEU GLN ALA GLY SER ALA GLY ASP PHE
SEQRES 19 C 615 ALA LYS ALA ALA GLY LEU GLU GLN LEU PRO TRP TRP HIS
SEQRES 20 C 615 LYS LEU THR GLU HIS ALA ALA TYR ASP ALA PHE TRP GLN
SEQRES 21 C 615 GLU GLN ALA LEU ASP LYS VAL MSE ALA ARG THR PRO LEU
SEQRES 22 C 615 LYS VAL PRO THR MSE TRP LEU GLN GLY LEU TRP ASP GLN
SEQRES 23 C 615 GLU ASP MSE TRP GLY ALA ILE HIS SER TYR ALA ALA MSE
SEQRES 24 C 615 GLU PRO ARG ASP LYS ARG ASN THR LEU ASN TYR LEU VAL
SEQRES 25 C 615 MSE GLY PRO TRP ARG HIS SER GLN VAL ASN TYR ASP GLY
SEQRES 26 C 615 SER ALA LEU GLY ALA LEU ASN PHE GLU GLY ASP THR ALA
SEQRES 27 C 615 ARG GLN PHE ARG HIS ASP VAL LEU ARG PRO PHE PHE ASP
SEQRES 28 C 615 GLN TYR LEU VAL ASP GLY ALA PRO LYS ALA ASP THR PRO
SEQRES 29 C 615 PRO VAL PHE ILE TYR ASN THR GLY GLU ASN HIS TRP ASP
SEQRES 30 C 615 ARG LEU LYS ALA TRP PRO ARG SER CYS ASP LYS GLY CYS
SEQRES 31 C 615 ALA ALA THR SER LYS PRO LEU TYR LEU GLN ALA GLY GLY
SEQRES 32 C 615 LYS LEU SER PHE GLN PRO PRO VAL ALA GLY GLN ALA GLY
SEQRES 33 C 615 PHE GLU GLU TYR VAL SER ASP PRO ALA LYS PRO VAL PRO
SEQRES 34 C 615 PHE VAL PRO ARG PRO VAL ASP PHE ALA ASP ARG ALA MSE
SEQRES 35 C 615 TRP THR THR TRP LEU VAL HIS ASP GLN ARG PHE VAL ASP
SEQRES 36 C 615 GLY ARG PRO ASP VAL LEU THR PHE VAL THR GLU PRO LEU
SEQRES 37 C 615 THR GLU PRO LEU GLN ILE ALA GLY ALA PRO ASP VAL HIS
SEQRES 38 C 615 LEU GLN ALA SER THR SER GLY SER ASP SER ASP TRP VAL
SEQRES 39 C 615 VAL LYS LEU ILE ASP VAL TYR PRO GLU GLU MSE ALA SER
SEQRES 40 C 615 ASN PRO LYS MSE GLY GLY TYR GLU LEU PRO VAL SER LEU
SEQRES 41 C 615 ALA ILE PHE ARG GLY ARG TYR ARG GLU SER PHE SER THR
SEQRES 42 C 615 PRO LYS PRO LEU THR SER ASN GLN PRO LEU ALA PHE GLN
SEQRES 43 C 615 PHE GLY LEU PRO THR ALA ASN HIS THR PHE GLN PRO GLY
SEQRES 44 C 615 HIS ARG VAL MSE VAL GLN VAL GLN SER SER LEU PHE PRO
SEQRES 45 C 615 LEU TYR ASP ARG ASN PRO GLN THR TYR VAL PRO ASN ILE
SEQRES 46 C 615 PHE PHE ALA LYS PRO GLY ASP TYR GLN LYS ALA THR GLN
SEQRES 47 C 615 ARG VAL TYR VAL SER PRO GLU GLN PRO SER TYR ILE SER
SEQRES 48 C 615 LEU PRO VAL ARG
SEQRES 1 D 615 GLN THR SER PRO MSE THR PRO ASP ILE THR GLY LYS PRO
SEQRES 2 D 615 PHE VAL ALA ALA ASP ALA SER ASN ASP TYR ILE LYS ARG
SEQRES 3 D 615 GLU VAL MSE ILE PRO MSE ARG ASP GLY VAL LYS LEU HIS
SEQRES 4 D 615 THR VAL ILE VAL LEU PRO LYS GLY ALA LYS ASN ALA PRO
SEQRES 5 D 615 ILE VAL LEU THR ARG THR PRO TYR ASP ALA SER GLY ARG
SEQRES 6 D 615 THR GLU ARG LEU ALA SER PRO HIS MSE LYS ASP LEU LEU
SEQRES 7 D 615 SER ALA GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 8 D 615 ARG VAL PHE GLN ASP VAL ARG GLY LYS TYR GLY SER GLU
SEQRES 9 D 615 GLY ASP TYR VAL MSE THR ARG PRO LEU ARG GLY PRO LEU
SEQRES 10 D 615 ASN PRO SER GLU VAL ASP HIS ALA THR ASP ALA TRP ASP
SEQRES 11 D 615 THR ILE ASP TRP LEU VAL LYS ASN VAL SER GLU SER ASN
SEQRES 12 D 615 GLY LYS VAL GLY MSE ILE GLY SER SER TYR GLU GLY PHE
SEQRES 13 D 615 THR VAL VAL MSE ALA LEU THR ASN PRO HIS PRO ALA LEU
SEQRES 14 D 615 LYS VAL ALA VAL PRO GLU SER PRO MSE ILE ASP GLY TRP
SEQRES 15 D 615 MSE GLY ASP ASP TRP PHE ASN TYR GLY ALA PHE ARG GLN
SEQRES 16 D 615 VAL ASN PHE ASP TYR PHE THR GLY GLN LEU SER LYS ARG
SEQRES 17 D 615 GLY LYS GLY ALA GLY ILE ALA ARG GLN GLY HIS ASP ASP
SEQRES 18 D 615 TYR SER ASN PHE LEU GLN ALA GLY SER ALA GLY ASP PHE
SEQRES 19 D 615 ALA LYS ALA ALA GLY LEU GLU GLN LEU PRO TRP TRP HIS
SEQRES 20 D 615 LYS LEU THR GLU HIS ALA ALA TYR ASP ALA PHE TRP GLN
SEQRES 21 D 615 GLU GLN ALA LEU ASP LYS VAL MSE ALA ARG THR PRO LEU
SEQRES 22 D 615 LYS VAL PRO THR MSE TRP LEU GLN GLY LEU TRP ASP GLN
SEQRES 23 D 615 GLU ASP MSE TRP GLY ALA ILE HIS SER TYR ALA ALA MSE
SEQRES 24 D 615 GLU PRO ARG ASP LYS ARG ASN THR LEU ASN TYR LEU VAL
SEQRES 25 D 615 MSE GLY PRO TRP ARG HIS SER GLN VAL ASN TYR ASP GLY
SEQRES 26 D 615 SER ALA LEU GLY ALA LEU ASN PHE GLU GLY ASP THR ALA
SEQRES 27 D 615 ARG GLN PHE ARG HIS ASP VAL LEU ARG PRO PHE PHE ASP
SEQRES 28 D 615 GLN TYR LEU VAL ASP GLY ALA PRO LYS ALA ASP THR PRO
SEQRES 29 D 615 PRO VAL PHE ILE TYR ASN THR GLY GLU ASN HIS TRP ASP
SEQRES 30 D 615 ARG LEU LYS ALA TRP PRO ARG SER CYS ASP LYS GLY CYS
SEQRES 31 D 615 ALA ALA THR SER LYS PRO LEU TYR LEU GLN ALA GLY GLY
SEQRES 32 D 615 LYS LEU SER PHE GLN PRO PRO VAL ALA GLY GLN ALA GLY
SEQRES 33 D 615 PHE GLU GLU TYR VAL SER ASP PRO ALA LYS PRO VAL PRO
SEQRES 34 D 615 PHE VAL PRO ARG PRO VAL ASP PHE ALA ASP ARG ALA MSE
SEQRES 35 D 615 TRP THR THR TRP LEU VAL HIS ASP GLN ARG PHE VAL ASP
SEQRES 36 D 615 GLY ARG PRO ASP VAL LEU THR PHE VAL THR GLU PRO LEU
SEQRES 37 D 615 THR GLU PRO LEU GLN ILE ALA GLY ALA PRO ASP VAL HIS
SEQRES 38 D 615 LEU GLN ALA SER THR SER GLY SER ASP SER ASP TRP VAL
SEQRES 39 D 615 VAL LYS LEU ILE ASP VAL TYR PRO GLU GLU MSE ALA SER
SEQRES 40 D 615 ASN PRO LYS MSE GLY GLY TYR GLU LEU PRO VAL SER LEU
SEQRES 41 D 615 ALA ILE PHE ARG GLY ARG TYR ARG GLU SER PHE SER THR
SEQRES 42 D 615 PRO LYS PRO LEU THR SER ASN GLN PRO LEU ALA PHE GLN
SEQRES 43 D 615 PHE GLY LEU PRO THR ALA ASN HIS THR PHE GLN PRO GLY
SEQRES 44 D 615 HIS ARG VAL MSE VAL GLN VAL GLN SER SER LEU PHE PRO
SEQRES 45 D 615 LEU TYR ASP ARG ASN PRO GLN THR TYR VAL PRO ASN ILE
SEQRES 46 D 615 PHE PHE ALA LYS PRO GLY ASP TYR GLN LYS ALA THR GLN
SEQRES 47 D 615 ARG VAL TYR VAL SER PRO GLU GLN PRO SER TYR ILE SER
SEQRES 48 D 615 LEU PRO VAL ARG
MODRES 1MPX MSE A 27 MET SELENOMETHIONINE
MODRES 1MPX MSE A 51 MET SELENOMETHIONINE
MODRES 1MPX MSE A 54 MET SELENOMETHIONINE
MODRES 1MPX MSE A 96 MET SELENOMETHIONINE
MODRES 1MPX MSE A 131 MET SELENOMETHIONINE
MODRES 1MPX MSE A 170 MET SELENOMETHIONINE
MODRES 1MPX MSE A 182 MET SELENOMETHIONINE
MODRES 1MPX MSE A 200 MET SELENOMETHIONINE
MODRES 1MPX MSE A 205 MET SELENOMETHIONINE
MODRES 1MPX MSE A 290 MET SELENOMETHIONINE
MODRES 1MPX MSE A 300 MET SELENOMETHIONINE
MODRES 1MPX MSE A 311 MET SELENOMETHIONINE
MODRES 1MPX MSE A 321 MET SELENOMETHIONINE
MODRES 1MPX MSE A 335 MET SELENOMETHIONINE
MODRES 1MPX MSE A 464 MET SELENOMETHIONINE
MODRES 1MPX MSE A 527 MET SELENOMETHIONINE
MODRES 1MPX MSE A 533 MET SELENOMETHIONINE
MODRES 1MPX MSE A 585 MET SELENOMETHIONINE
MODRES 1MPX MSE B 27 MET SELENOMETHIONINE
MODRES 1MPX MSE B 51 MET SELENOMETHIONINE
MODRES 1MPX MSE B 54 MET SELENOMETHIONINE
MODRES 1MPX MSE B 96 MET SELENOMETHIONINE
MODRES 1MPX MSE B 131 MET SELENOMETHIONINE
MODRES 1MPX MSE B 170 MET SELENOMETHIONINE
MODRES 1MPX MSE B 182 MET SELENOMETHIONINE
MODRES 1MPX MSE B 200 MET SELENOMETHIONINE
MODRES 1MPX MSE B 205 MET SELENOMETHIONINE
MODRES 1MPX MSE B 290 MET SELENOMETHIONINE
MODRES 1MPX MSE B 300 MET SELENOMETHIONINE
MODRES 1MPX MSE B 311 MET SELENOMETHIONINE
MODRES 1MPX MSE B 321 MET SELENOMETHIONINE
MODRES 1MPX MSE B 335 MET SELENOMETHIONINE
MODRES 1MPX MSE B 464 MET SELENOMETHIONINE
MODRES 1MPX MSE B 527 MET SELENOMETHIONINE
MODRES 1MPX MSE B 533 MET SELENOMETHIONINE
MODRES 1MPX MSE B 585 MET SELENOMETHIONINE
MODRES 1MPX MSE C 27 MET SELENOMETHIONINE
MODRES 1MPX MSE C 51 MET SELENOMETHIONINE
MODRES 1MPX MSE C 54 MET SELENOMETHIONINE
MODRES 1MPX MSE C 96 MET SELENOMETHIONINE
MODRES 1MPX MSE C 131 MET SELENOMETHIONINE
MODRES 1MPX MSE C 170 MET SELENOMETHIONINE
MODRES 1MPX MSE C 182 MET SELENOMETHIONINE
MODRES 1MPX MSE C 200 MET SELENOMETHIONINE
MODRES 1MPX MSE C 205 MET SELENOMETHIONINE
MODRES 1MPX MSE C 290 MET SELENOMETHIONINE
MODRES 1MPX MSE C 300 MET SELENOMETHIONINE
MODRES 1MPX MSE C 311 MET SELENOMETHIONINE
MODRES 1MPX MSE C 321 MET SELENOMETHIONINE
MODRES 1MPX MSE C 335 MET SELENOMETHIONINE
MODRES 1MPX MSE C 464 MET SELENOMETHIONINE
MODRES 1MPX MSE C 527 MET SELENOMETHIONINE
MODRES 1MPX MSE C 533 MET SELENOMETHIONINE
MODRES 1MPX MSE C 585 MET SELENOMETHIONINE
MODRES 1MPX MSE D 27 MET SELENOMETHIONINE
MODRES 1MPX MSE D 51 MET SELENOMETHIONINE
MODRES 1MPX MSE D 54 MET SELENOMETHIONINE
MODRES 1MPX MSE D 96 MET SELENOMETHIONINE
MODRES 1MPX MSE D 131 MET SELENOMETHIONINE
MODRES 1MPX MSE D 170 MET SELENOMETHIONINE
MODRES 1MPX MSE D 182 MET SELENOMETHIONINE
MODRES 1MPX MSE D 200 MET SELENOMETHIONINE
MODRES 1MPX MSE D 205 MET SELENOMETHIONINE
MODRES 1MPX MSE D 290 MET SELENOMETHIONINE
MODRES 1MPX MSE D 300 MET SELENOMETHIONINE
MODRES 1MPX MSE D 311 MET SELENOMETHIONINE
MODRES 1MPX MSE D 321 MET SELENOMETHIONINE
MODRES 1MPX MSE D 335 MET SELENOMETHIONINE
MODRES 1MPX MSE D 464 MET SELENOMETHIONINE
MODRES 1MPX MSE D 527 MET SELENOMETHIONINE
MODRES 1MPX MSE D 533 MET SELENOMETHIONINE
MODRES 1MPX MSE D 585 MET SELENOMETHIONINE
HET MSE A 27 8
HET MSE A 51 8
HET MSE A 54 8
HET MSE A 96 8
HET MSE A 131 8
HET MSE A 170 8
HET MSE A 182 8
HET MSE A 200 8
HET MSE A 205 8
HET MSE A 290 8
HET MSE A 300 8
HET MSE A 311 8
HET MSE A 321 8
HET MSE A 335 8
HET MSE A 464 8
HET MSE A 527 8
HET MSE A 533 8
HET MSE A 585 8
HET MSE B 27 8
HET MSE B 51 8
HET MSE B 54 8
HET MSE B 96 8
HET MSE B 131 8
HET MSE B 170 8
HET MSE B 182 8
HET MSE B 200 8
HET MSE B 205 8
HET MSE B 290 8
HET MSE B 300 8
HET MSE B 311 8
HET MSE B 321 8
HET MSE B 335 8
HET MSE B 464 8
HET MSE B 527 8
HET MSE B 533 8
HET MSE B 585 8
HET MSE C 27 8
HET MSE C 51 8
HET MSE C 54 8
HET MSE C 96 8
HET MSE C 131 8
HET MSE C 170 8
HET MSE C 182 8
HET MSE C 200 8
HET MSE C 205 8
HET MSE C 290 8
HET MSE C 300 8
HET MSE C 311 8
HET MSE C 321 8
HET MSE C 335 8
HET MSE C 464 8
HET MSE C 527 8
HET MSE C 533 8
HET MSE C 585 8
HET MSE D 27 8
HET MSE D 51 8
HET MSE D 54 8
HET MSE D 96 8
HET MSE D 131 8
HET MSE D 170 8
HET MSE D 182 8
HET MSE D 200 8
HET MSE D 205 8
HET MSE D 290 8
HET MSE D 300 8
HET MSE D 311 8
HET MSE D 321 8
HET MSE D 335 8
HET MSE D 464 8
HET MSE D 527 8
HET MSE D 533 8
HET MSE D 585 8
HET CA A 638 1
HET CA B 638 1
HET CA C 638 1
HET CA D 638 1
HET GOL 3001 6
HET GOL 3002 6
HET GOL 3004 6
HET GOL 3005 6
HET GOL 3006 6
HET GOL 3007 6
HET GOL 3008 6
HET GOL 3009 6
HET GOL 3010 6
HET GOL 3011 6
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
FORMUL 1 MSE 72(C5 H11 N1 O2 SE1)
FORMUL 5 CA 4(CA1 2+)
FORMUL 9 GOL 10(C3 H8 O3)
FORMUL 19 HOH *2246(H2 O1)
HELIX 1 1 ASP A 83 THR A 88 1 6
HELIX 2 2 HIS A 95 LEU A 100 1 6
HELIX 3 3 SER A 101 GLY A 103 5 3
HELIX 4 4 ASP A 104 GLY A 110 1 7
HELIX 5 5 ASP A 145 VAL A 161 1 17
HELIX 6 6 SER A 174 THR A 185 1 12
HELIX 7 7 ASN A 219 SER A 228 1 10
HELIX 8 8 ASP A 242 GLY A 251 1 10
HELIX 9 9 SER A 252 ALA A 260 1 9
HELIX 10 10 GLY A 261 GLN A 264 5 4
HELIX 11 11 LEU A 265 HIS A 274 1 10
HELIX 12 12 ASP A 278 GLU A 283 1 6
HELIX 13 13 ALA A 285 ARG A 292 1 8
HELIX 14 14 TRP A 312 GLU A 322 1 11
HELIX 15 15 PRO A 323 ASP A 325 5 3
HELIX 16 16 SER A 341 TYR A 345 5 5
HELIX 17 17 ASP A 358 VAL A 367 1 10
HELIX 18 18 VAL A 367 VAL A 377 1 11
HELIX 19 19 ASP A 461 TRP A 468 1 8
HELIX 20 20 LEU A 469 HIS A 471 5 3
HELIX 21 21 ASP A 472 VAL A 476 5 5
HELIX 22 22 ASN A 530 GLY A 534 5 5
HELIX 23 23 ARG A 548 ARG A 550 5 3
HELIX 24 24 ASN A 606 ALA A 610 5 5
HELIX 25 25 LYS A 611 TYR A 615 5 5
HELIX 26 26 ASP B 83 THR B 88 1 6
HELIX 27 27 HIS B 95 LEU B 100 1 6
HELIX 28 28 SER B 101 GLY B 103 5 3
HELIX 29 29 ASP B 104 GLY B 110 1 7
HELIX 30 30 ASP B 145 VAL B 161 1 17
HELIX 31 31 SER B 174 THR B 185 1 12
HELIX 32 32 ASN B 219 SER B 228 1 10
HELIX 33 33 ASP B 242 GLY B 251 1 10
HELIX 34 34 SER B 252 ALA B 260 1 9
HELIX 35 35 GLY B 261 GLN B 264 5 4
HELIX 36 36 LEU B 265 HIS B 274 1 10
HELIX 37 37 ASP B 278 GLU B 283 1 6
HELIX 38 38 ALA B 285 ARG B 292 1 8
HELIX 39 39 TRP B 312 GLU B 322 1 11
HELIX 40 40 PRO B 323 ASP B 325 5 3
HELIX 41 41 SER B 341 TYR B 345 5 5
HELIX 42 42 ASP B 358 VAL B 367 1 10
HELIX 43 43 VAL B 367 VAL B 377 1 11
HELIX 44 44 ASP B 461 TRP B 468 1 8
HELIX 45 45 LEU B 469 HIS B 471 5 3
HELIX 46 46 ASP B 472 VAL B 476 5 5
HELIX 47 47 ASN B 530 GLY B 534 5 5
HELIX 48 48 ARG B 548 ARG B 550 5 3
HELIX 49 49 ASN B 606 ALA B 610 5 5
HELIX 50 50 LYS B 611 TYR B 615 5 5
HELIX 51 51 ASP C 83 THR C 88 1 6
HELIX 52 52 HIS C 95 LEU C 100 1 6
HELIX 53 53 SER C 101 GLY C 103 5 3
HELIX 54 54 ASP C 104 GLY C 110 1 7
HELIX 55 55 ASP C 145 VAL C 161 1 17
HELIX 56 56 SER C 174 THR C 185 1 12
HELIX 57 57 ASN C 219 SER C 228 1 10
HELIX 58 58 ASP C 242 GLY C 251 1 10
HELIX 59 59 SER C 252 GLY C 261 1 10
HELIX 60 60 LEU C 262 GLN C 264 5 3
HELIX 61 61 LEU C 265 HIS C 274 1 10
HELIX 62 62 ASP C 278 GLU C 283 1 6
HELIX 63 63 ALA C 285 ARG C 292 1 8
HELIX 64 64 TRP C 312 GLU C 322 1 11
HELIX 65 65 PRO C 323 ASP C 325 5 3
HELIX 66 66 SER C 341 TYR C 345 5 5
HELIX 67 67 ASP C 358 VAL C 367 1 10
HELIX 68 68 VAL C 367 VAL C 377 1 11
HELIX 69 69 ASP C 461 TRP C 468 1 8
HELIX 70 70 LEU C 469 HIS C 471 5 3
HELIX 71 71 ASP C 472 VAL C 476 5 5
HELIX 72 72 ASN C 530 GLY C 534 5 5
HELIX 73 73 ARG C 548 ARG C 550 5 3
HELIX 74 74 ASN C 606 ALA C 610 5 5
HELIX 75 75 LYS C 611 TYR C 615 5 5
HELIX 76 76 ASP D 83 THR D 88 1 6
HELIX 77 77 HIS D 95 LEU D 100 1 6
HELIX 78 78 SER D 101 GLY D 103 5 3
HELIX 79 79 ASP D 104 GLY D 110 1 7
HELIX 80 80 ASP D 145 VAL D 161 1 17
HELIX 81 81 SER D 174 THR D 185 1 12
HELIX 82 82 ASN D 219 SER D 228 1 10
HELIX 83 83 ASP D 242 GLY D 251 1 10
HELIX 84 84 SER D 252 GLY D 261 1 10
HELIX 85 85 LEU D 262 GLN D 264 5 3
HELIX 86 86 LEU D 265 HIS D 274 1 10
HELIX 87 87 ASP D 278 GLU D 283 1 6
HELIX 88 88 ALA D 285 ALA D 291 1 7
HELIX 89 89 TRP D 312 GLU D 322 1 11
HELIX 90 90 PRO D 323 ASP D 325 5 3
HELIX 91 91 SER D 341 TYR D 345 5 5
HELIX 92 92 ASP D 358 VAL D 367 1 10
HELIX 93 93 VAL D 367 VAL D 377 1 11
HELIX 94 94 ASP D 461 TRP D 468 1 8
HELIX 95 95 LEU D 469 HIS D 471 5 3
HELIX 96 96 ASP D 472 VAL D 476 5 5
HELIX 97 97 ASN D 530 GLY D 534 5 5
HELIX 98 98 ARG D 548 ARG D 550 5 3
HELIX 99 99 ASN D 606 ALA D 610 5 5
HELIX 100 100 LYS D 611 TYR D 615 5 5
SHEET 1 A 6 TYR A 45 PRO A 53 0
SHEET 2 A 6 LYS A 59 PRO A 67 -1 O ILE A 64 N ARG A 48
SHEET 3 A 6 ILE A 113 ASP A 118 -1 O PHE A 116 N VAL A 63
SHEET 4 A 6 ALA A 73 THR A 80 1 N THR A 80 O GLN A 117
SHEET 5 A 6 SER A 164 SER A 173 1 O GLY A 169 N LEU A 77
SHEET 6 A 6 LEU A 191 GLU A 197 1 O GLU A 197 N GLY A 172
SHEET 1 B 2 PHE A 210 ASN A 211 0
SHEET 2 B 2 ALA A 214 PHE A 215 -1 O ALA A 214 N ASN A 211
SHEET 1 C 4 THR A 299 GLY A 304 0
SHEET 2 C 4 ASN A 331 GLY A 336 1 O TYR A 332 N THR A 299
SHEET 3 C 4 VAL A 388 ASN A 392 1 O PHE A 389 N LEU A 333
SHEET 4 C 4 HIS A 397 LEU A 401 -1 O HIS A 397 N ASN A 392
SHEET 1 D 2 ALA A 349 LEU A 350 0
SHEET 2 D 2 LEU A 353 ASN A 354 -1 O LEU A 353 N LEU A 350
SHEET 1 E 2 SER A 407 CYS A 408 0
SHEET 2 E 2 ALA A 414 THR A 415 1 O ALA A 414 N CYS A 408
SHEET 1 F 4 PHE A 439 SER A 444 0
SHEET 2 F 4 ALA A 618 TYR A 623 -1 O GLN A 620 N TYR A 442
SHEET 3 F 4 ASP A 501 THR A 508 -1 N SER A 507 O ARG A 621
SHEET 4 F 4 LEU A 565 GLY A 570 -1 O PHE A 567 N LEU A 504
SHEET 1 G 6 PHE A 439 SER A 444 0
SHEET 2 G 6 ALA A 618 TYR A 623 -1 O GLN A 620 N TYR A 442
SHEET 3 G 6 ASP A 501 THR A 508 -1 N SER A 507 O ARG A 621
SHEET 4 G 6 TYR A 631 LEU A 634 -1 O SER A 633 N ASP A 501
SHEET 5 G 6 LYS A 417 GLN A 422 -1 N LYS A 417 O LEU A 634
SHEET 6 G 6 LYS A 426 SER A 428 -1 O LYS A 426 N GLN A 422
SHEET 1 H 4 VAL A 482 VAL A 486 0
SHEET 2 H 4 ARG A 583 GLN A 589 -1 O VAL A 588 N LEU A 483
SHEET 3 H 4 ASP A 514 VAL A 522 -1 N ILE A 520 O MSE A 585
SHEET 4 H 4 GLU A 537 ARG A 546 -1 O SER A 541 N LEU A 519
SHEET 1 I 2 LEU A 494 GLY A 498 0
SHEET 2 I 2 ALA A 574 PHE A 578 -1 O PHE A 578 N LEU A 494
SHEET 1 J 6 TYR B 45 PRO B 53 0
SHEET 2 J 6 LYS B 59 PRO B 67 -1 O ILE B 64 N ARG B 48
SHEET 3 J 6 ILE B 113 ASP B 118 -1 O PHE B 116 N VAL B 63
SHEET 4 J 6 ALA B 73 THR B 80 1 N THR B 80 O GLN B 117
SHEET 5 J 6 SER B 164 SER B 173 1 O GLY B 169 N LEU B 77
SHEET 6 J 6 LEU B 191 GLU B 197 1 O GLU B 197 N GLY B 172
SHEET 1 K 2 PHE B 210 ASN B 211 0
SHEET 2 K 2 ALA B 214 PHE B 215 -1 O ALA B 214 N ASN B 211
SHEET 1 L 4 THR B 299 GLY B 304 0
SHEET 2 L 4 ASN B 331 GLY B 336 1 O TYR B 332 N THR B 299
SHEET 3 L 4 VAL B 388 ASN B 392 1 O PHE B 389 N LEU B 333
SHEET 4 L 4 HIS B 397 LEU B 401 -1 O HIS B 397 N ASN B 392
SHEET 1 M 2 ALA B 349 LEU B 350 0
SHEET 2 M 2 LEU B 353 ASN B 354 -1 O LEU B 353 N LEU B 350
SHEET 1 N 2 SER B 407 CYS B 408 0
SHEET 2 N 2 ALA B 414 THR B 415 1 O ALA B 414 N CYS B 408
SHEET 1 O 4 PHE B 439 SER B 444 0
SHEET 2 O 4 ALA B 618 TYR B 623 -1 O GLN B 620 N TYR B 442
SHEET 3 O 4 ASP B 501 THR B 508 -1 N SER B 507 O ARG B 621
SHEET 4 O 4 LEU B 565 GLY B 570 -1 O PHE B 567 N LEU B 504
SHEET 1 P 6 PHE B 439 SER B 444 0
SHEET 2 P 6 ALA B 618 TYR B 623 -1 O GLN B 620 N TYR B 442
SHEET 3 P 6 ASP B 501 THR B 508 -1 N SER B 507 O ARG B 621
SHEET 4 P 6 TYR B 631 LEU B 634 -1 O SER B 633 N ASP B 501
SHEET 5 P 6 LYS B 417 GLN B 422 -1 N LYS B 417 O LEU B 634
SHEET 6 P 6 LYS B 426 SER B 428 -1 O LYS B 426 N GLN B 422
SHEET 1 Q 4 VAL B 482 VAL B 486 0
SHEET 2 Q 4 ARG B 583 GLN B 589 -1 O VAL B 588 N LEU B 483
SHEET 3 Q 4 ASP B 514 VAL B 522 -1 N ILE B 520 O MSE B 585
SHEET 4 Q 4 GLU B 537 ARG B 546 -1 O SER B 541 N LEU B 519
SHEET 1 R 2 LEU B 494 GLY B 498 0
SHEET 2 R 2 ALA B 574 PHE B 578 -1 O PHE B 578 N LEU B 494
SHEET 1 S 6 TYR C 45 PRO C 53 0
SHEET 2 S 6 LYS C 59 PRO C 67 -1 O ILE C 64 N ARG C 48
SHEET 3 S 6 ILE C 113 ASP C 118 -1 O PHE C 116 N VAL C 63
SHEET 4 S 6 ALA C 73 THR C 80 1 N THR C 80 O GLN C 117
SHEET 5 S 6 SER C 164 SER C 173 1 O GLY C 169 N LEU C 77
SHEET 6 S 6 LEU C 191 GLU C 197 1 O GLU C 197 N GLY C 172
SHEET 1 T 2 PHE C 210 ASN C 211 0
SHEET 2 T 2 ALA C 214 PHE C 215 -1 O ALA C 214 N ASN C 211
SHEET 1 U 4 THR C 299 GLY C 304 0
SHEET 2 U 4 ASN C 331 GLY C 336 1 O TYR C 332 N THR C 299
SHEET 3 U 4 VAL C 388 ASN C 392 1 O PHE C 389 N LEU C 333
SHEET 4 U 4 HIS C 397 LEU C 401 -1 O HIS C 397 N ASN C 392
SHEET 1 V 2 ALA C 349 LEU C 350 0
SHEET 2 V 2 LEU C 353 ASN C 354 -1 O LEU C 353 N LEU C 350
SHEET 1 W 2 SER C 407 CYS C 408 0
SHEET 2 W 2 ALA C 414 THR C 415 1 O ALA C 414 N CYS C 408
SHEET 1 X 4 PHE C 439 SER C 444 0
SHEET 2 X 4 ALA C 618 TYR C 623 -1 O GLN C 620 N TYR C 442
SHEET 3 X 4 ASP C 501 THR C 508 -1 N SER C 507 O ARG C 621
SHEET 4 X 4 LEU C 565 GLY C 570 -1 O PHE C 567 N LEU C 504
SHEET 1 Y 6 PHE C 439 SER C 444 0
SHEET 2 Y 6 ALA C 618 TYR C 623 -1 O GLN C 620 N TYR C 442
SHEET 3 Y 6 ASP C 501 THR C 508 -1 N SER C 507 O ARG C 621
SHEET 4 Y 6 TYR C 631 LEU C 634 -1 O SER C 633 N ASP C 501
SHEET 5 Y 6 LYS C 417 GLN C 422 -1 N LEU C 419 O ILE C 632
SHEET 6 Y 6 LYS C 426 SER C 428 -1 O LYS C 426 N GLN C 422
SHEET 1 Z 4 LEU C 483 VAL C 486 0
SHEET 2 Z 4 ARG C 583 GLN C 589 -1 O VAL C 588 N LEU C 483
SHEET 3 Z 4 ASP C 514 VAL C 522 -1 N ILE C 520 O MSE C 585
SHEET 4 Z 4 GLU C 537 ARG C 546 -1 O SER C 541 N LEU C 519
SHEET 1 AA 2 LEU C 494 GLY C 498 0
SHEET 2 AA 2 ALA C 574 PHE C 578 -1 O PHE C 578 N LEU C 494
SHEET 1 AB 6 TYR D 45 PRO D 53 0
SHEET 2 AB 6 LYS D 59 PRO D 67 -1 O ILE D 64 N ARG D 48
SHEET 3 AB 6 ILE D 113 ASP D 118 -1 O ARG D 114 N VAL D 65
SHEET 4 AB 6 ALA D 73 THR D 80 1 N THR D 80 O GLN D 117
SHEET 5 AB 6 SER D 164 SER D 173 1 O GLY D 169 N LEU D 77
SHEET 6 AB 6 LEU D 191 GLU D 197 1 O GLU D 197 N GLY D 172
SHEET 1 AC 2 PHE D 210 ASN D 211 0
SHEET 2 AC 2 ALA D 214 PHE D 215 -1 O ALA D 214 N ASN D 211
SHEET 1 AD 4 THR D 299 GLY D 304 0
SHEET 2 AD 4 ASN D 331 GLY D 336 1 O TYR D 332 N THR D 299
SHEET 3 AD 4 VAL D 388 ASN D 392 1 O PHE D 389 N LEU D 333
SHEET 4 AD 4 HIS D 397 LEU D 401 -1 O HIS D 397 N ASN D 392
SHEET 1 AE 2 ALA D 349 LEU D 350 0
SHEET 2 AE 2 LEU D 353 ASN D 354 -1 O LEU D 353 N LEU D 350
SHEET 1 AF 2 SER D 407 CYS D 408 0
SHEET 2 AF 2 ALA D 414 THR D 415 1 O ALA D 414 N CYS D 408
SHEET 1 AG 4 PHE D 439 SER D 444 0
SHEET 2 AG 4 ALA D 618 TYR D 623 -1 O GLN D 620 N TYR D 442
SHEET 3 AG 4 ASP D 501 THR D 508 -1 N SER D 507 O ARG D 621
SHEET 4 AG 4 LEU D 565 GLY D 570 -1 O PHE D 567 N LEU D 504
SHEET 1 AH 6 PHE D 439 SER D 444 0
SHEET 2 AH 6 ALA D 618 TYR D 623 -1 O GLN D 620 N TYR D 442
SHEET 3 AH 6 ASP D 501 THR D 508 -1 N SER D 507 O ARG D 621
SHEET 4 AH 6 TYR D 631 LEU D 634 -1 O SER D 633 N ASP D 501
SHEET 5 AH 6 LYS D 417 GLN D 422 -1 N LEU D 419 O ILE D 632
SHEET 6 AH 6 LYS D 426 SER D 428 -1 O LYS D 426 N GLN D 422
SHEET 1 AI 4 LEU D 483 VAL D 486 0
SHEET 2 AI 4 ARG D 583 GLN D 589 -1 O VAL D 588 N LEU D 483
SHEET 3 AI 4 ASP D 514 VAL D 522 -1 N ILE D 520 O MSE D 585
SHEET 4 AI 4 GLU D 537 ARG D 546 -1 O SER D 541 N LEU D 519
SHEET 1 AJ 2 LEU D 494 GLY D 498 0
SHEET 2 AJ 2 ALA D 574 PHE D 578 -1 O PHE D 578 N LEU D 494
SSBOND 1 CYS A 408 CYS A 412
SSBOND 2 CYS B 408 CYS B 412
SSBOND 3 CYS C 408 CYS C 412
SSBOND 4 CYS D 408 CYS D 412
CISPEP 1 TRP A 404 PRO A 405 0 0.36
CISPEP 2 ARG A 455 PRO A 456 0 -1.60
CISPEP 3 PHE A 593 PRO A 594 0 -0.37
CISPEP 4 TRP B 404 PRO B 405 0 -0.13
CISPEP 5 ARG B 455 PRO B 456 0 -0.99
CISPEP 6 PHE B 593 PRO B 594 0 -1.24
CISPEP 7 TRP C 404 PRO C 405 0 0.71
CISPEP 8 ARG C 455 PRO C 456 0 -1.53
CISPEP 9 PHE C 593 PRO C 594 0 -0.76
CISPEP 10 TRP D 404 PRO D 405 0 0.75
CISPEP 11 ARG D 455 PRO D 456 0 -1.82
CISPEP 12 PHE D 593 PRO D 594 0 -0.02
CRYST1 89.772 126.016 132.291 90.00 91.06 90.00 P 1 21 1 8
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 0.011139 0.000000 0.000206 0.00000
SCALE2 0.000000 0.007935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007560 0.00000
TER 4849 ARG A 637
TER 9698 ARG B 637
MASTER 305 0 86 100 128 0 0 621702 4 644 192
END |