HEADER MEMBRANE PROTEIN 04-APR-13 3W9H
TITLE STRUCTURAL BASIS FOR THE INHIBITION OF BACTERIAL MULTIDRUG EXPORTERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACRIFLAVINE RESISTANCE PROTEIN B;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 1-1033;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: ACRB, ACRE, B0462, JW0451;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC118
KEYWDS ACRB, EFFLUX PUMP, TRANSPORTER, MULTIDRUG EFFLUX PUMP, ACRA, TOLC,
KEYWDS 2 INNER MEMBRANE, TRANSPORT PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SAKURAI,C.NAGATA,R.NAKASHIMA,A.YAMAGUCHI
REVDAT 4 08-NOV-23 3W9H 1 REMARK
REVDAT 3 22-NOV-17 3W9H 1 REMARK
REVDAT 2 07-AUG-13 3W9H 1 JRNL
REVDAT 1 03-JUL-13 3W9H 0
JRNL AUTH R.NAKASHIMA,K.SAKURAI,S.YAMASAKI,K.HAYASHI,C.NAGATA,
JRNL AUTH 2 K.HOSHINO,Y.ONODERA,K.NISHINO,A.YAMAGUCHI
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITION OF BACTERIAL MULTIDRUG
JRNL TITL 2 EXPORTERS
JRNL REF NATURE V. 500 102 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 23812586
JRNL DOI 10.1038/NATURE12300
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 88240
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.317
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4430
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) : 3.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5908
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE SET COUNT : 312
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23550
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 15
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 105.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.528
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.444
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.799
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24053 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32672 ; 1.679 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3096 ; 7.008 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 939 ;39.931 ;24.537
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4041 ;22.621 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 111 ;19.232 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3840 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17864 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3W9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000096054.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89374
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.62200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2V50
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM SODIUM PHOSPHATE, 100MM NACL, 14%
REMARK 280 PEG 4000, 32UG/ML ABI-PP, PH 6.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 113.13950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.08000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 113.13950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 67.08000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 115180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 88 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 LEU A 177 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 LEU A 702 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU A 713 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU B 293 CA - CB - CG ANGL. DEV. = 18.2 DEGREES
REMARK 500 LEU B 578 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 LEU B 713 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 34 -91.93 -77.88
REMARK 500 THR A 37 91.46 45.22
REMARK 500 TYR A 49 85.86 -154.72
REMARK 500 VAL A 61 -81.44 -132.96
REMARK 500 SER A 82 67.46 -119.92
REMARK 500 THR A 85 -75.03 -67.93
REMARK 500 MET A 162 -50.67 -145.46
REMARK 500 SER A 170 127.84 -31.98
REMARK 500 ALA A 236 -143.04 -119.22
REMARK 500 THR A 241 15.80 -151.49
REMARK 500 LYS A 248 14.19 -69.52
REMARK 500 ALA A 266 135.00 -176.61
REMARK 500 GLU A 280 118.78 -162.28
REMARK 500 ASN A 282 48.52 33.74
REMARK 500 PRO A 285 120.38 -37.28
REMARK 500 LEU A 293 125.48 -30.23
REMARK 500 PRO A 315 -13.37 -42.35
REMARK 500 LEU A 321 100.42 -35.64
REMARK 500 TYR A 325 51.25 -114.90
REMARK 500 TYR A 327 124.75 -175.32
REMARK 500 TYR A 356 -70.18 -106.14
REMARK 500 LEU A 357 -36.32 -25.14
REMARK 500 LEU A 359 -32.16 -136.76
REMARK 500 GLN A 360 12.14 56.70
REMARK 500 PHE A 362 -75.38 -37.50
REMARK 500 ALA A 364 -13.36 -171.90
REMARK 500 LEU A 366 -7.24 -52.68
REMARK 500 ALA A 371 42.17 -94.88
REMARK 500 VAL A 372 -48.02 -131.87
REMARK 500 LEU A 377 -9.95 -50.09
REMARK 500 THR A 392 -62.69 -20.67
REMARK 500 ASP A 408 -7.86 -55.09
REMARK 500 ASN A 415 2.46 -66.02
REMARK 500 ALA A 421 -72.36 -85.04
REMARK 500 GLU A 422 10.06 -58.75
REMARK 500 GLU A 423 -41.90 -140.96
REMARK 500 PRO A 427 -73.95 -39.23
REMARK 500 LYS A 428 -72.41 -38.56
REMARK 500 GLN A 437 -75.61 -81.78
REMARK 500 GLN A 439 -61.95 -5.49
REMARK 500 THR A 463 -82.10 -17.76
REMARK 500 MET A 496 -22.74 -145.99
REMARK 500 LYS A 502 139.18 -37.49
REMARK 500 ASP A 504 94.15 -54.94
REMARK 500 HIS A 505 45.58 -78.91
REMARK 500 TRP A 515 -49.06 -28.67
REMARK 500 SER A 537 -64.33 -100.60
REMARK 500 THR A 538 42.31 33.49
REMARK 500 MET A 552 -71.50 -102.55
REMARK 500 TYR A 554 -70.56 -61.10
REMARK 500
REMARK 500 THIS ENTRY HAS 356 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY C 996 SER C 997 145.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P9D B 2000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W9I RELATED DB: PDB
REMARK 900 RELATED ID: 3W9J RELATED DB: PDB
DBREF 3W9H A 1 1033 UNP P31224 ACRB_ECOLI 1 1033
DBREF 3W9H B 1 1033 UNP P31224 ACRB_ECOLI 1 1033
DBREF 3W9H C 1 1033 UNP P31224 ACRB_ECOLI 1 1033
SEQRES 1 A 1033 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 A 1033 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 A 1033 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 A 1033 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 A 1033 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 A 1033 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 A 1033 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 A 1033 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 A 1033 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 A 1033 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 A 1033 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 A 1033 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 A 1033 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 A 1033 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 A 1033 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 A 1033 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 A 1033 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 A 1033 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 A 1033 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 A 1033 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 A 1033 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 A 1033 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 A 1033 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 A 1033 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 A 1033 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 A 1033 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 A 1033 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 A 1033 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 A 1033 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 A 1033 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 A 1033 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 A 1033 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 A 1033 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 A 1033 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 A 1033 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 A 1033 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 A 1033 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 A 1033 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 A 1033 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 A 1033 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 A 1033 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 A 1033 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 A 1033 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 A 1033 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 A 1033 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 A 1033 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 A 1033 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 A 1033 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 A 1033 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 A 1033 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 A 1033 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 A 1033 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 A 1033 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 A 1033 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 A 1033 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 A 1033 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 A 1033 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 A 1033 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 A 1033 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 A 1033 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 A 1033 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 A 1033 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 A 1033 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 A 1033 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 A 1033 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 A 1033 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 A 1033 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 A 1033 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 A 1033 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 A 1033 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 A 1033 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 A 1033 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 A 1033 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 A 1033 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 A 1033 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 A 1033 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 A 1033 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 A 1033 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 A 1033 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 A 1033 VAL VAL ARG ARG ARG PHE
SEQRES 1 B 1033 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 B 1033 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 B 1033 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 B 1033 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 B 1033 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 B 1033 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 B 1033 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 B 1033 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 B 1033 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 B 1033 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 B 1033 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 B 1033 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 B 1033 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 B 1033 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 B 1033 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 B 1033 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 B 1033 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 B 1033 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 B 1033 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 B 1033 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 B 1033 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 B 1033 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 B 1033 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 B 1033 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 B 1033 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 B 1033 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 B 1033 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 B 1033 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 B 1033 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 B 1033 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 B 1033 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 B 1033 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 B 1033 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 B 1033 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 B 1033 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 B 1033 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 B 1033 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 B 1033 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 B 1033 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 B 1033 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 B 1033 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 B 1033 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 B 1033 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 B 1033 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 B 1033 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 B 1033 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 B 1033 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 B 1033 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 B 1033 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 B 1033 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 B 1033 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 B 1033 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 B 1033 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 B 1033 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 B 1033 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 B 1033 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 B 1033 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 B 1033 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 B 1033 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 B 1033 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 B 1033 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 B 1033 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 B 1033 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 B 1033 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 B 1033 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 B 1033 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 B 1033 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 B 1033 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 B 1033 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 B 1033 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 B 1033 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 B 1033 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 B 1033 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 B 1033 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 B 1033 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 B 1033 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 B 1033 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 B 1033 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 B 1033 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 B 1033 VAL VAL ARG ARG ARG PHE
SEQRES 1 C 1033 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 C 1033 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 C 1033 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 C 1033 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 C 1033 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 C 1033 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 C 1033 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 C 1033 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 C 1033 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 C 1033 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 C 1033 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 C 1033 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 C 1033 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 C 1033 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 C 1033 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 C 1033 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 C 1033 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 C 1033 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 C 1033 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 C 1033 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 C 1033 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 C 1033 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 C 1033 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 C 1033 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 C 1033 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 C 1033 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 C 1033 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 C 1033 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 C 1033 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 C 1033 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 C 1033 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 C 1033 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 C 1033 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 C 1033 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 C 1033 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 C 1033 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 C 1033 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 C 1033 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 C 1033 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 C 1033 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 C 1033 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 C 1033 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 C 1033 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 C 1033 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 C 1033 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 C 1033 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 C 1033 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 C 1033 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 C 1033 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 C 1033 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 C 1033 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 C 1033 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 C 1033 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 C 1033 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 C 1033 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 C 1033 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 C 1033 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 C 1033 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 C 1033 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 C 1033 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 C 1033 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 C 1033 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 C 1033 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 C 1033 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 C 1033 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 C 1033 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 C 1033 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 C 1033 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 C 1033 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 C 1033 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 C 1033 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 C 1033 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 C 1033 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 C 1033 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 C 1033 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 C 1033 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 C 1033 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 C 1033 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 C 1033 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 C 1033 VAL VAL ARG ARG ARG PHE
HET P9D B2000 49
HETNAM P9D [{2-[({[(3R)-1-{8-[(4-TERT-BUTYL-1,3-THIAZOL-2-YL)
HETNAM 2 P9D CARBAMOYL]-4-OXO-3-[(E)-2-(1H-TETRAZOL-5-YL)ETHENYL]-
HETNAM 3 P9D 4H-PYRIDO[1,2-A]PYRIMIDIN-2-YL}PIPERIDIN-3-
HETNAM 4 P9D YL]OXY}CARBONYL)AMINO]ETHYL}(DIMETHYL)AMMONIO]ACETATE
FORMUL 4 P9D C31 H39 N11 O6 S
FORMUL 5 HOH *15(H2 O)
HELIX 1 1 MET A 1 ASP A 7 1 7
HELIX 2 2 ARG A 8 LEU A 30 1 23
HELIX 3 3 ASP A 53 VAL A 61 1 9
HELIX 4 4 VAL A 61 MET A 69 1 9
HELIX 5 5 ASP A 99 MET A 115 1 17
HELIX 6 6 PRO A 116 LEU A 118 5 3
HELIX 7 7 PRO A 119 GLN A 124 1 6
HELIX 8 8 THR A 150 MET A 162 1 13
HELIX 9 9 MET A 162 ARG A 168 1 7
HELIX 10 10 ASN A 189 PHE A 196 1 8
HELIX 11 11 THR A 199 ASN A 211 1 13
HELIX 12 12 SER A 242 LYS A 248 1 7
HELIX 13 13 ASN A 298 GLU A 314 1 17
HELIX 14 14 PRO A 315 PHE A 317 5 3
HELIX 15 15 THR A 329 LEU A 350 1 22
HELIX 16 16 LEU A 353 PHE A 358 1 6
HELIX 17 17 ASN A 361 ALA A 371 1 11
HELIX 18 18 VAL A 372 PHE A 386 1 15
HELIX 19 19 MET A 395 GLU A 422 1 28
HELIX 20 20 PRO A 426 ILE A 438 1 13
HELIX 21 21 GLN A 439 LEU A 449 1 11
HELIX 22 22 VAL A 454 PHE A 459 5 6
HELIX 23 23 SER A 462 ILE A 466 5 5
HELIX 24 24 TYR A 467 LEU A 486 1 20
HELIX 25 25 ILE A 487 THR A 495 1 9
HELIX 26 26 GLY A 511 ARG A 536 1 26
HELIX 27 27 VAL A 543 GLY A 551 1 9
HELIX 28 28 MET A 552 LEU A 559 1 8
HELIX 29 29 THR A 583 LYS A 601 1 19
HELIX 30 30 GLY A 639 ASN A 642 5 4
HELIX 31 31 LYS A 643 SER A 656 1 14
HELIX 32 32 GLY A 691 ALA A 706 1 16
HELIX 33 33 ASP A 732 LEU A 739 1 8
HELIX 34 34 SER A 742 GLY A 756 1 15
HELIX 35 35 ALA A 777 MET A 781 5 5
HELIX 36 36 LEU A 782 ASP A 788 5 7
HELIX 37 37 SER A 836 ALA A 848 1 13
HELIX 38 38 GLY A 861 GLU A 866 1 6
HELIX 39 39 GLN A 872 TYR A 892 1 21
HELIX 40 40 ILE A 897 LEU A 903 5 7
HELIX 41 41 VAL A 904 ARG A 919 1 16
HELIX 42 42 ASP A 924 ALA A 949 1 26
HELIX 43 43 GLY A 959 ARG A 971 1 13
HELIX 44 44 ARG A 971 VAL A 986 1 16
HELIX 45 45 VAL A 986 ILE A 991 1 6
HELIX 46 46 SER A 997 THR A 1005 1 9
HELIX 47 47 VAL A 1007 PHE A 1020 1 14
HELIX 48 48 PHE A 1020 ARG A 1031 1 12
HELIX 49 49 PRO B 2 ARG B 8 1 7
HELIX 50 50 ARG B 8 ALA B 26 1 19
HELIX 51 51 ASP B 53 VAL B 61 1 9
HELIX 52 52 VAL B 61 GLN B 67 1 7
HELIX 53 53 ASP B 99 LEU B 113 1 15
HELIX 54 54 ALA B 114 LEU B 118 5 5
HELIX 55 55 PRO B 119 GLY B 126 1 8
HELIX 56 56 THR B 150 MET B 162 1 13
HELIX 57 57 MET B 162 THR B 169 1 8
HELIX 58 58 ASN B 189 PHE B 196 1 8
HELIX 59 59 THR B 199 GLN B 210 1 12
HELIX 60 60 SER B 242 ILE B 249 1 8
HELIX 61 61 ASN B 298 LYS B 312 1 15
HELIX 62 62 THR B 329 GLU B 339 1 11
HELIX 63 63 GLU B 339 LEU B 357 1 19
HELIX 64 64 ILE B 367 ILE B 370 5 4
HELIX 65 65 ALA B 371 LEU B 383 1 13
HELIX 66 66 ALA B 384 GLY B 387 5 4
HELIX 67 67 ASN B 391 GLY B 397 1 7
HELIX 68 68 ALA B 401 MET B 420 1 20
HELIX 69 69 ALA B 430 ILE B 438 1 9
HELIX 70 70 ILE B 438 VAL B 454 1 17
HELIX 71 71 PRO B 455 ALA B 457 5 3
HELIX 72 72 GLY B 460 ALA B 494 1 35
HELIX 73 73 GLY B 511 ARG B 536 1 26
HELIX 74 74 ARG B 540 ILE B 547 1 8
HELIX 75 75 ILE B 548 LEU B 555 1 8
HELIX 76 76 THR B 583 LEU B 599 1 17
HELIX 77 77 ASP B 633 ARG B 637 5 5
HELIX 78 78 LYS B 643 ARG B 653 1 11
HELIX 79 79 ALA B 654 GLN B 657 5 4
HELIX 80 80 GLY B 691 ALA B 707 1 17
HELIX 81 81 ASP B 732 GLY B 740 1 9
HELIX 82 82 SER B 742 GLY B 756 1 15
HELIX 83 83 ALA B 777 ARG B 780 5 4
HELIX 84 84 LEU B 782 ASP B 788 5 7
HELIX 85 85 SER B 802 PHE B 804 5 3
HELIX 86 86 SER B 836 SER B 849 1 14
HELIX 87 87 GLY B 861 GLY B 870 1 10
HELIX 88 88 GLN B 872 TYR B 892 1 21
HELIX 89 89 PRO B 898 LEU B 903 1 6
HELIX 90 90 VAL B 904 PHE B 918 1 15
HELIX 91 91 ASP B 924 LEU B 952 1 29
HELIX 92 92 ILE B 961 SER B 992 1 32
HELIX 93 93 GLY B 996 VAL B 1016 1 21
HELIX 94 94 LEU B 1017 ARG B 1031 1 15
HELIX 95 95 ARG B 1032 PHE B 1033 5 2
HELIX 96 96 MET C 1 MET C 1 5 1
HELIX 97 97 PRO C 2 ASP C 7 1 6
HELIX 98 98 ARG C 8 LEU C 30 1 23
HELIX 99 99 ASP C 53 VAL C 61 1 9
HELIX 100 100 VAL C 61 ASN C 68 1 8
HELIX 101 101 ASP C 99 MET C 115 1 17
HELIX 102 102 PRO C 116 LEU C 118 5 3
HELIX 103 103 PRO C 119 GLY C 126 1 8
HELIX 104 104 THR C 150 SER C 167 1 18
HELIX 105 105 ASN C 189 PHE C 196 1 8
HELIX 106 106 THR C 199 ASN C 211 1 13
HELIX 107 107 SER C 242 LYS C 248 1 7
HELIX 108 108 LEU C 262 VAL C 265 1 4
HELIX 109 109 ASN C 298 GLU C 314 1 17
HELIX 110 110 THR C 330 LEU C 350 1 21
HELIX 111 111 ILE C 370 PHE C 386 1 17
HELIX 112 112 ASN C 391 ALA C 401 1 11
HELIX 113 113 ALA C 401 VAL C 406 1 6
HELIX 114 114 VAL C 406 ALA C 421 1 16
HELIX 115 115 PRO C 426 VAL C 454 1 29
HELIX 116 116 GLY C 460 ALA C 485 1 26
HELIX 117 117 ILE C 487 LEU C 497 1 11
HELIX 118 118 GLY C 511 SER C 537 1 27
HELIX 119 119 VAL C 543 LEU C 559 1 17
HELIX 120 120 THR C 583 THR C 600 1 18
HELIX 121 121 ASP C 633 ARG C 637 5 5
HELIX 122 122 GLY C 639 ASN C 642 5 4
HELIX 123 123 LYS C 643 PHE C 655 1 13
HELIX 124 124 GLY C 691 LYS C 708 1 18
HELIX 125 125 ASP C 732 GLY C 740 1 9
HELIX 126 126 SER C 742 GLY C 755 1 14
HELIX 127 127 GLU C 776 ARG C 780 5 5
HELIX 128 128 ASP C 784 TRP C 789 5 6
HELIX 129 129 PRO C 800 PHE C 804 5 5
HELIX 130 130 SER C 836 LYS C 850 1 15
HELIX 131 131 THR C 860 TYR C 892 1 33
HELIX 132 132 SER C 896 MET C 902 1 7
HELIX 133 133 VAL C 904 PHE C 918 1 15
HELIX 134 134 ASP C 924 GLU C 947 1 24
HELIX 135 135 PHE C 948 GLU C 956 1 9
HELIX 136 136 GLY C 959 ARG C 971 1 13
HELIX 137 137 LEU C 972 VAL C 986 1 15
HELIX 138 138 GLY C 996 THR C 1013 1 18
HELIX 139 139 THR C 1015 PHE C 1033 1 19
SHEET 1 A 2 VAL A 32 ALA A 33 0
SHEET 2 A 2 ILE A 390 ASN A 391 1 O ILE A 390 N ALA A 33
SHEET 1 B 6 SER A 128 LYS A 131 0
SHEET 2 B 6 ALA A 42 SER A 48 -1 N THR A 44 O GLU A 130
SHEET 3 B 6 THR A 87 PHE A 94 -1 O LEU A 92 N VAL A 43
SHEET 4 B 6 LEU A 75 ASP A 83 -1 N SER A 79 O THR A 91
SHEET 5 B 6 ARG A 818 TYR A 819 -1 O ARG A 818 N SER A 80
SHEET 6 B 6 LEU A 822 PRO A 823 -1 O LEU A 822 N TYR A 819
SHEET 1 C 4 VAL A 172 LEU A 177 0
SHEET 2 C 4 GLN A 284 LEU A 293 -1 O LYS A 292 N ASP A 174
SHEET 3 C 4 MET A 138 ILE A 143 -1 N MET A 138 O ILE A 291
SHEET 4 C 4 LYS A 322 ASP A 328 -1 O VAL A 324 N GLY A 141
SHEET 1 D 7 VAL A 172 LEU A 177 0
SHEET 2 D 7 GLN A 284 LEU A 293 -1 O LYS A 292 N ASP A 174
SHEET 3 D 7 ILE A 278 PHE A 281 -1 N PHE A 281 O GLN A 284
SHEET 4 D 7 VAL A 606 PHE A 615 -1 O ALA A 611 N GLU A 280
SHEET 5 D 7 ARG A 620 LEU A 631 -1 O ILE A 626 N VAL A 612
SHEET 6 D 7 VAL A 571 VAL A 576 -1 N PHE A 572 O VAL A 629
SHEET 7 D 7 VAL A 663 PHE A 666 -1 O PHE A 666 N MET A 573
SHEET 1 E 4 ALA A 266 GLY A 272 0
SHEET 2 E 4 TYR A 182 MET A 188 -1 N ARG A 185 O GLU A 269
SHEET 3 E 4 ARG A 767 SER A 775 1 O MET A 774 N MET A 188
SHEET 4 E 4 SER A 757 ASP A 764 -1 N SER A 757 O VAL A 773
SHEET 1 F 4 GLN A 218 LEU A 219 0
SHEET 2 F 4 ALA A 232 ILE A 235 -1 O ALA A 232 N LEU A 219
SHEET 3 F 4 GLN B 726 LYS B 728 1 O PHE B 727 N SER A 233
SHEET 4 F 4 TRP B 809 GLU B 810 -1 O GLU B 810 N GLN B 726
SHEET 1 G 2 LEU A 250 VAL A 253 0
SHEET 2 G 2 ARG A 259 LEU A 261 -1 O VAL A 260 N LYS A 252
SHEET 1 H 4 LEU A 713 PRO A 718 0
SHEET 2 H 4 GLU A 826 ALA A 831 -1 O LEU A 828 N ARG A 717
SHEET 3 H 4 GLY A 679 ASP A 686 -1 N PHE A 682 O ILE A 827
SHEET 4 H 4 VAL A 855 TRP A 859 -1 O ASP A 858 N GLU A 683
SHEET 1 I 4 SER A 805 GLY A 812 0
SHEET 2 I 4 THR A 724 ILE A 731 -1 N GLN A 726 O GLU A 810
SHEET 3 I 4 ALA C 232 ILE C 235 1 O ILE C 235 N ILE A 729
SHEET 4 I 4 GLN C 218 LEU C 219 -1 N LEU C 219 O ALA C 232
SHEET 1 J 2 TYR A 790 VAL A 791 0
SHEET 2 J 2 VAL A 799 PRO A 800 -1 O VAL A 799 N VAL A 791
SHEET 1 K 7 SER B 128 LYS B 131 0
SHEET 2 K 7 ALA B 42 SER B 48 -1 N THR B 44 O GLU B 130
SHEET 3 K 7 THR B 87 PHE B 94 -1 O ILE B 90 N ILE B 45
SHEET 4 K 7 LEU B 75 ASP B 83 -1 N MET B 76 O THR B 93
SHEET 5 K 7 ARG B 815 TYR B 819 -1 O ARG B 818 N SER B 80
SHEET 6 K 7 LEU B 822 GLN B 830 -1 O SER B 824 N GLU B 817
SHEET 7 K 7 THR B 714 PRO B 718 -1 N ARG B 717 O LEU B 828
SHEET 1 L 8 SER B 128 LYS B 131 0
SHEET 2 L 8 ALA B 42 SER B 48 -1 N THR B 44 O GLU B 130
SHEET 3 L 8 THR B 87 PHE B 94 -1 O ILE B 90 N ILE B 45
SHEET 4 L 8 LEU B 75 ASP B 83 -1 N MET B 76 O THR B 93
SHEET 5 L 8 ARG B 815 TYR B 819 -1 O ARG B 818 N SER B 80
SHEET 6 L 8 LEU B 822 GLN B 830 -1 O SER B 824 N GLU B 817
SHEET 7 L 8 GLY B 679 ASP B 686 -1 N PHE B 682 O ILE B 827
SHEET 8 L 8 VAL B 855 TRP B 859 -1 O GLY B 856 N ILE B 685
SHEET 1 M 4 VAL B 172 LEU B 177 0
SHEET 2 M 4 LEU B 289 LEU B 293 -1 O LYS B 292 N GLY B 173
SHEET 3 M 4 MET B 138 VAL B 142 -1 N MET B 138 O ILE B 291
SHEET 4 M 4 ILE B 323 ASP B 328 -1 O VAL B 324 N GLY B 141
SHEET 1 N 4 ALA B 266 GLU B 269 0
SHEET 2 N 4 MET B 184 MET B 188 -1 N TRP B 187 O LYS B 267
SHEET 3 N 4 VAL B 768 SER B 775 1 O MET B 774 N ILE B 186
SHEET 4 N 4 SER B 757 ILE B 763 -1 N VAL B 759 O VAL B 771
SHEET 1 O 4 GLY B 217 LEU B 219 0
SHEET 2 O 4 ALA B 232 ILE B 234 -1 O ALA B 232 N LEU B 219
SHEET 3 O 4 GLN C 726 PHE C 727 1 O PHE C 727 N SER B 233
SHEET 4 O 4 TRP C 809 GLU C 810 -1 O GLU C 810 N GLN C 726
SHEET 1 P 2 LEU B 250 LYS B 252 0
SHEET 2 P 2 VAL B 260 LEU B 261 -1 O VAL B 260 N LYS B 252
SHEET 1 Q 6 GLN B 284 PRO B 285 0
SHEET 2 Q 6 ILE B 278 PHE B 281 -1 N PHE B 281 O GLN B 284
SHEET 3 Q 6 VAL B 606 PHE B 615 -1 O ASN B 613 N ILE B 278
SHEET 4 Q 6 ARG B 620 LEU B 631 -1 O PHE B 628 N PHE B 610
SHEET 5 Q 6 VAL B 571 GLN B 577 -1 N VAL B 576 O GLY B 625
SHEET 6 Q 6 ALA B 665 PHE B 666 -1 O PHE B 666 N MET B 573
SHEET 1 R 2 TYR B 790 ARG B 792 0
SHEET 2 R 2 MET B 798 PRO B 800 -1 O VAL B 799 N VAL B 791
SHEET 1 S 7 SER C 128 LYS C 131 0
SHEET 2 S 7 ALA C 42 ALA C 47 -1 N THR C 44 O GLU C 130
SHEET 3 S 7 VAL C 88 PHE C 94 -1 O LEU C 92 N VAL C 43
SHEET 4 S 7 LEU C 75 ASP C 83 -1 N TYR C 77 O THR C 93
SHEET 5 S 7 ARG C 815 TYR C 819 -1 O ARG C 818 N SER C 80
SHEET 6 S 7 LEU C 822 ALA C 831 -1 O SER C 824 N GLU C 817
SHEET 7 S 7 LEU C 713 PRO C 718 -1 N ARG C 717 O LEU C 828
SHEET 1 T 8 SER C 128 LYS C 131 0
SHEET 2 T 8 ALA C 42 ALA C 47 -1 N THR C 44 O GLU C 130
SHEET 3 T 8 VAL C 88 PHE C 94 -1 O LEU C 92 N VAL C 43
SHEET 4 T 8 LEU C 75 ASP C 83 -1 N TYR C 77 O THR C 93
SHEET 5 T 8 ARG C 815 TYR C 819 -1 O ARG C 818 N SER C 80
SHEET 6 T 8 LEU C 822 ALA C 831 -1 O SER C 824 N GLU C 817
SHEET 7 T 8 PHE C 680 LEU C 684 -1 N PHE C 682 O ILE C 827
SHEET 8 T 8 ASP C 858 TRP C 859 -1 O ASP C 858 N GLU C 683
SHEET 1 U 4 VAL C 172 PHE C 178 0
SHEET 2 U 4 SER C 287 LEU C 293 -1 O GLY C 290 N GLN C 176
SHEET 3 U 4 VAL C 140 ASN C 144 -1 N VAL C 142 O SER C 287
SHEET 4 U 4 LEU C 321 VAL C 324 -1 O VAL C 324 N GLY C 141
SHEET 1 V 2 TYR C 182 MET C 188 0
SHEET 2 V 2 ALA C 266 GLY C 272 -1 O GLY C 271 N ALA C 183
SHEET 1 W 2 LEU C 250 VAL C 253 0
SHEET 2 W 2 ARG C 259 LEU C 261 -1 O VAL C 260 N LYS C 252
SHEET 1 X 6 GLN C 284 PRO C 285 0
SHEET 2 X 6 ILE C 278 PHE C 281 -1 N PHE C 281 O GLN C 284
SHEET 3 X 6 VAL C 606 ASN C 613 -1 O ASN C 613 N ILE C 278
SHEET 4 X 6 GLY C 625 LEU C 631 -1 O ILE C 626 N VAL C 612
SHEET 5 X 6 VAL C 571 GLN C 577 -1 N VAL C 576 O GLY C 625
SHEET 6 X 6 MET C 662 PHE C 666 -1 O PHE C 664 N MET C 575
SHEET 1 Y 2 SER C 757 TYR C 758 0
SHEET 2 Y 2 TYR C 772 VAL C 773 -1 O VAL C 773 N SER C 757
SHEET 1 Z 2 PHE C 762 ASP C 764 0
SHEET 2 Z 2 ARG C 767 LYS C 769 -1 O LYS C 769 N PHE C 762
CISPEP 1 THR A 222 PRO A 223 0 -0.97
CISPEP 2 THR B 222 PRO B 223 0 -4.93
CISPEP 3 THR C 222 PRO C 223 0 -1.17
SITE 1 AC1 14 VAL B 139 GLN B 176 LEU B 177 PHE B 178
SITE 2 AC1 14 GLY B 179 ILE B 277 ALA B 279 TYR B 327
SITE 3 AC1 14 PHE B 610 VAL B 612 PHE B 615 ARG B 620
SITE 4 AC1 14 PHE B 628 LEU B 668
CRYST1 226.279 134.160 162.202 90.00 97.83 90.00 C 1 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004419 0.000000 0.000607 0.00000
SCALE2 0.000000 0.007454 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006223 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
