HEADER TRANSPORT PROTEIN 29-APR-16 5JMN
TITLE FUSIDIC ACID BOUND ACRB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDRUG EFFLUX PUMP SUBUNIT ACRB;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ACRAB-TOLC MULTIDRUG EFFLUX PUMP SUBUNIT ACRB,ACRIDINE
COMPND 5 RESISTANCE PROTEIN B;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DARPIN;
COMPND 9 CHAIN: D, E;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: ACRB, ACRE, B0462, JW0451;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: C43;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 GENE: ARTIFICIAL GENE;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: XL1 BLUE;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS MULTIDRUG EFFLUX PROTEIN, MEMBRANE PROTEIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.OSWALD,H.K.TAM,K.M.POS
REVDAT 4 10-JAN-24 5JMN 1 REMARK
REVDAT 3 11-JAN-17 5JMN 1 JRNL
REVDAT 2 28-DEC-16 5JMN 1 JRNL
REVDAT 1 21-DEC-16 5JMN 0
JRNL AUTH C.OSWALD,H.K.TAM,K.M.POS
JRNL TITL TRANSPORT OF LIPOPHILIC CARBOXYLATES IS MEDIATED BY
JRNL TITL 2 TRANSMEMBRANE HELIX 2 IN MULTIDRUG TRANSPORTER ACRB.
JRNL REF NAT COMMUN V. 7 13819 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27982032
JRNL DOI 10.1038/NCOMMS13819
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 192130
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10113
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14058
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3940
REMARK 3 BIN FREE R VALUE SET COUNT : 740
REMARK 3 BIN FREE R VALUE : 0.4080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 25920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 874
REMARK 3 SOLVENT ATOMS : 815
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.15000
REMARK 3 B22 (A**2) : 4.55000
REMARK 3 B33 (A**2) : -0.40000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.333
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.252
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.269
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.800
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 27306 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 27131 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 36971 ; 1.105 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): 62427 ; 0.838 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3418 ; 5.025 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1056 ;34.018 ;24.688
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4445 ;12.779 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;13.667 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4368 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30139 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5847 ; 0.001 ; 0.020
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): 13657 ; 1.512 ; 6.169
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 13656 ; 1.512 ; 6.169
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17065 ; 2.636 ; 9.252
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 17066 ; 2.636 ; 9.252
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13649 ; 1.422 ; 6.632
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 13650 ; 1.422 ; 6.632
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 19902 ; 2.539 ; 9.827
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 29766 ; 4.818 ;49.438
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 29767 ; 4.817 ;49.439
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 : NULL
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5JMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 259156
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 49.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 4DX7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M ADA, PH 6.9, 0.15-0.25M AMMONIUM
REMARK 280 SULFATE, 5% GLYCEROL, 5-10% PEG4000, 0.004M FUSIDIC ACID, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 72.82700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 123.02100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.62400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 123.02100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 72.82700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.62400
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 44600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 125520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 ARG A 1035
REMARK 465 LYS A 1036
REMARK 465 ASN A 1037
REMARK 465 GLU A 1038
REMARK 465 ASP A 1039
REMARK 465 ILE A 1040
REMARK 465 GLU A 1041
REMARK 465 HIS A 1042
REMARK 465 SER A 1043
REMARK 465 HIS A 1044
REMARK 465 THR A 1045
REMARK 465 VAL A 1046
REMARK 465 ASP A 1047
REMARK 465 HIS A 1048
REMARK 465 HIS A 1049
REMARK 465 LEU A 1050
REMARK 465 GLU A 1051
REMARK 465 HIS A 1052
REMARK 465 HIS A 1053
REMARK 465 HIS A 1054
REMARK 465 HIS A 1055
REMARK 465 HIS A 1056
REMARK 465 HIS A 1057
REMARK 465 ARG B 1035
REMARK 465 LYS B 1036
REMARK 465 ASN B 1037
REMARK 465 GLU B 1038
REMARK 465 ASP B 1039
REMARK 465 ILE B 1040
REMARK 465 GLU B 1041
REMARK 465 HIS B 1042
REMARK 465 SER B 1043
REMARK 465 HIS B 1044
REMARK 465 THR B 1045
REMARK 465 VAL B 1046
REMARK 465 ASP B 1047
REMARK 465 HIS B 1048
REMARK 465 HIS B 1049
REMARK 465 LEU B 1050
REMARK 465 GLU B 1051
REMARK 465 HIS B 1052
REMARK 465 HIS B 1053
REMARK 465 HIS B 1054
REMARK 465 HIS B 1055
REMARK 465 HIS B 1056
REMARK 465 HIS B 1057
REMARK 465 SER C 1034
REMARK 465 ARG C 1035
REMARK 465 LYS C 1036
REMARK 465 ASN C 1037
REMARK 465 GLU C 1038
REMARK 465 ASP C 1039
REMARK 465 ILE C 1040
REMARK 465 GLU C 1041
REMARK 465 HIS C 1042
REMARK 465 SER C 1043
REMARK 465 HIS C 1044
REMARK 465 THR C 1045
REMARK 465 VAL C 1046
REMARK 465 ASP C 1047
REMARK 465 HIS C 1048
REMARK 465 HIS C 1049
REMARK 465 LEU C 1050
REMARK 465 GLU C 1051
REMARK 465 HIS C 1052
REMARK 465 HIS C 1053
REMARK 465 HIS C 1054
REMARK 465 HIS C 1055
REMARK 465 HIS C 1056
REMARK 465 HIS C 1057
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 GLY D 3
REMARK 465 SER D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 ASN D 169
REMARK 465 MET E 1
REMARK 465 ARG E 2
REMARK 465 GLY E 3
REMARK 465 SER E 4
REMARK 465 HIS E 5
REMARK 465 HIS E 6
REMARK 465 HIS E 7
REMARK 465 HIS E 8
REMARK 465 HIS E 9
REMARK 465 HIS E 10
REMARK 465 GLY E 11
REMARK 465 SER E 12
REMARK 465 LYS E 167
REMARK 465 LEU E 168
REMARK 465 ASN E 169
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 O4 FUA A 1101 O HOH A 1201 2.19
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 VAL A 61 -67.09 -128.76
REMARK 500 MET A 162 -50.54 -129.72
REMARK 500 ALA A 236 -136.72 -103.31
REMARK 500 ILE A 487 -65.17 -95.81
REMARK 500 GLU A 507 -66.96 67.07
REMARK 500 LYS A 509 106.19 -160.21
REMARK 500 THR A 538 -73.93 60.68
REMARK 500 PHE A 563 -69.49 -100.88
REMARK 500 ALA A 677 -70.08 63.24
REMARK 500 ALA A 688 34.01 -145.39
REMARK 500 PRO A 852 170.08 -59.14
REMARK 500 SER A 869 167.56 65.64
REMARK 500 LEU A 972 -58.87 -122.86
REMARK 500 SER A 992 130.36 -36.18
REMARK 500 MET B 69 46.78 -86.12
REMARK 500 MET B 162 -54.83 -139.67
REMARK 500 ALA B 216 -97.81 -110.28
REMARK 500 ALA B 236 -140.49 -97.53
REMARK 500 ILE B 487 -63.53 -121.79
REMARK 500 SER B 537 67.85 -108.39
REMARK 500 PHE B 563 -64.54 -94.05
REMARK 500 THR B 600 -63.46 -97.10
REMARK 500 ASP B 660 77.55 17.50
REMARK 500 ALA B 677 64.11 60.22
REMARK 500 ALA B 688 41.11 -151.06
REMARK 500 ARG B 780 39.88 -141.64
REMARK 500 SER B 869 60.13 -101.18
REMARK 500 ARG C 8 75.02 -114.77
REMARK 500 VAL C 61 -58.22 -122.19
REMARK 500 MET C 69 50.84 -92.67
REMARK 500 ASP C 146 18.85 -143.71
REMARK 500 ASN C 211 78.14 -115.89
REMARK 500 ALA C 236 -140.12 -106.10
REMARK 500 GLN C 360 -55.77 72.39
REMARK 500 ILE C 487 -66.43 -108.26
REMARK 500 PHE C 563 -71.81 -96.86
REMARK 500 PRO C 579 170.96 -58.39
REMARK 500 THR C 600 -70.35 -106.42
REMARK 500 ALA C 688 27.14 -142.69
REMARK 500 HIS C 709 66.05 -117.21
REMARK 500 ASN D 69 36.41 -93.60
REMARK 500 ASN E 36 32.76 -98.51
REMARK 500 ASN E 69 35.12 -96.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1423 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH C1467 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH C1468 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH C1469 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH C1470 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH C1471 DISTANCE = 8.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUA A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT A 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ETE A 1107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ETE A 1108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUA B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PTY B 1107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D12 B 1108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P3G B 1110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D10 B 1112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUA C 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT C 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT C 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT C 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT C 1105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PTY C 1109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PTY C 1110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PTY C 1111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D12 C 1112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D12 C 1113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ETE C 1115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEX C 1117
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 202
DBREF 5JMN A 1 1049 UNP P31224 ACRB_ECOLI 1 1049
DBREF 5JMN B 1 1049 UNP P31224 ACRB_ECOLI 1 1049
DBREF 5JMN C 1 1049 UNP P31224 ACRB_ECOLI 1 1049
DBREF 5JMN D 1 169 PDB 5JMN 5JMN 1 169
DBREF 5JMN E 1 169 PDB 5JMN 5JMN 1 169
SEQADV 5JMN LEU A 1050 UNP P31224 EXPRESSION TAG
SEQADV 5JMN GLU A 1051 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS A 1052 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS A 1053 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS A 1054 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS A 1055 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS A 1056 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS A 1057 UNP P31224 EXPRESSION TAG
SEQADV 5JMN LEU B 1050 UNP P31224 EXPRESSION TAG
SEQADV 5JMN GLU B 1051 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS B 1052 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS B 1053 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS B 1054 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS B 1055 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS B 1056 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS B 1057 UNP P31224 EXPRESSION TAG
SEQADV 5JMN LEU C 1050 UNP P31224 EXPRESSION TAG
SEQADV 5JMN GLU C 1051 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS C 1052 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS C 1053 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS C 1054 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS C 1055 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS C 1056 UNP P31224 EXPRESSION TAG
SEQADV 5JMN HIS C 1057 UNP P31224 EXPRESSION TAG
SEQRES 1 A 1057 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 A 1057 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 A 1057 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 A 1057 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 A 1057 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 A 1057 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 A 1057 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 A 1057 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 A 1057 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 A 1057 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 A 1057 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 A 1057 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 A 1057 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 A 1057 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 A 1057 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 A 1057 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 A 1057 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 A 1057 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 A 1057 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 A 1057 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 A 1057 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 A 1057 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 A 1057 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 A 1057 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 A 1057 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 A 1057 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 A 1057 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 A 1057 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 A 1057 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 A 1057 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 A 1057 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 A 1057 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 A 1057 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 A 1057 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 A 1057 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 A 1057 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 A 1057 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 A 1057 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 A 1057 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 A 1057 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 A 1057 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 A 1057 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 A 1057 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 A 1057 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 A 1057 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 A 1057 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 A 1057 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 A 1057 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 A 1057 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 A 1057 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 A 1057 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 A 1057 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 A 1057 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 A 1057 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 A 1057 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 A 1057 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 A 1057 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 A 1057 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 A 1057 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 A 1057 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 A 1057 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 A 1057 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 A 1057 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 A 1057 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 A 1057 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 A 1057 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 A 1057 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 A 1057 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 A 1057 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 A 1057 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 A 1057 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 A 1057 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 A 1057 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 A 1057 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 A 1057 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 A 1057 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 A 1057 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 A 1057 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 A 1057 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 A 1057 VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES 81 A 1057 GLU HIS SER HIS THR VAL ASP HIS HIS LEU GLU HIS HIS
SEQRES 82 A 1057 HIS HIS HIS HIS
SEQRES 1 B 1057 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 B 1057 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 B 1057 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 B 1057 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 B 1057 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 B 1057 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 B 1057 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 B 1057 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 B 1057 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 B 1057 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 B 1057 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 B 1057 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 B 1057 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 B 1057 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 B 1057 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 B 1057 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 B 1057 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 B 1057 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 B 1057 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 B 1057 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 B 1057 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 B 1057 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 B 1057 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 B 1057 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 B 1057 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 B 1057 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 B 1057 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 B 1057 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 B 1057 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 B 1057 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 B 1057 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 B 1057 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 B 1057 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 B 1057 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 B 1057 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 B 1057 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 B 1057 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 B 1057 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 B 1057 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 B 1057 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 B 1057 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 B 1057 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 B 1057 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 B 1057 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 B 1057 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 B 1057 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 B 1057 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 B 1057 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 B 1057 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 B 1057 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 B 1057 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 B 1057 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 B 1057 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 B 1057 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 B 1057 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 B 1057 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 B 1057 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 B 1057 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 B 1057 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 B 1057 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 B 1057 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 B 1057 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 B 1057 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 B 1057 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 B 1057 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 B 1057 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 B 1057 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 B 1057 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 B 1057 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 B 1057 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 B 1057 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 B 1057 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 B 1057 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 B 1057 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 B 1057 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 B 1057 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 B 1057 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 B 1057 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 B 1057 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 B 1057 VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES 81 B 1057 GLU HIS SER HIS THR VAL ASP HIS HIS LEU GLU HIS HIS
SEQRES 82 B 1057 HIS HIS HIS HIS
SEQRES 1 C 1057 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 C 1057 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 C 1057 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 C 1057 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 C 1057 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 C 1057 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 C 1057 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 C 1057 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 C 1057 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 C 1057 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 C 1057 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 C 1057 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 C 1057 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 C 1057 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 C 1057 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 C 1057 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 C 1057 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 C 1057 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 C 1057 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 C 1057 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 C 1057 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 C 1057 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 C 1057 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 C 1057 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 C 1057 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 C 1057 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 C 1057 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 C 1057 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 C 1057 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 C 1057 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 C 1057 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 C 1057 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 C 1057 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 C 1057 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 C 1057 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 C 1057 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 C 1057 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 C 1057 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 C 1057 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 C 1057 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 C 1057 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 C 1057 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 C 1057 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 C 1057 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 C 1057 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 C 1057 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 C 1057 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 C 1057 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 C 1057 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 C 1057 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 C 1057 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 C 1057 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 C 1057 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 C 1057 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 C 1057 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 C 1057 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 C 1057 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 C 1057 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 C 1057 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 C 1057 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 C 1057 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 C 1057 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 C 1057 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 C 1057 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 C 1057 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 C 1057 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 C 1057 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 C 1057 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 C 1057 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 C 1057 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 C 1057 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 C 1057 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 C 1057 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 C 1057 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 C 1057 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 C 1057 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 C 1057 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 C 1057 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 C 1057 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 C 1057 VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES 81 C 1057 GLU HIS SER HIS THR VAL ASP HIS HIS LEU GLU HIS HIS
SEQRES 82 C 1057 HIS HIS HIS HIS
SEQRES 1 D 169 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 D 169 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY ARG
SEQRES 3 D 169 ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP
SEQRES 4 D 169 VAL ASN ALA ALA ASP VAL VAL GLY TRP THR PRO LEU HIS
SEQRES 5 D 169 LEU ALA ALA TYR TRP GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 D 169 LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA TYR ASP THR
SEQRES 7 D 169 LEU GLY SER THR PRO LEU HIS LEU ALA ALA HIS PHE GLY
SEQRES 8 D 169 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY ALA
SEQRES 9 D 169 ASP VAL ASN ALA LYS ASP ASP ASN GLY ILE THR PRO LEU
SEQRES 10 D 169 HIS LEU ALA ALA ASN ARG GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 D 169 VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP
SEQRES 12 D 169 LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASN ASN
SEQRES 13 D 169 GLY ASN GLU ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN
SEQRES 1 E 169 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 E 169 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY ARG
SEQRES 3 E 169 ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP
SEQRES 4 E 169 VAL ASN ALA ALA ASP VAL VAL GLY TRP THR PRO LEU HIS
SEQRES 5 E 169 LEU ALA ALA TYR TRP GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 E 169 LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA TYR ASP THR
SEQRES 7 E 169 LEU GLY SER THR PRO LEU HIS LEU ALA ALA HIS PHE GLY
SEQRES 8 E 169 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY ALA
SEQRES 9 E 169 ASP VAL ASN ALA LYS ASP ASP ASN GLY ILE THR PRO LEU
SEQRES 10 E 169 HIS LEU ALA ALA ASN ARG GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 E 169 VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP
SEQRES 12 E 169 LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASN ASN
SEQRES 13 E 169 GLY ASN GLU ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN
HET FUA A1101 37
HET LMT A1102 35
HET LMT A1103 35
HET LMT A1104 35
HET SO4 A1105 5
HET GOL A1106 6
HET ETE A1107 14
HET ETE A1108 14
HET HEX A1109 6
HET FUA B1101 37
HET LMT B1102 35
HET LMT B1103 35
HET LMT B1104 35
HET GOL B1105 6
HET GOL B1106 6
HET PTY B1107 50
HET D12 B1108 12
HET OCT B1109 8
HET P3G B1110 17
HET D10 B1111 10
HET D10 B1112 10
HET FUA C1101 37
HET LMT C1102 35
HET LMT C1103 35
HET LMT C1104 35
HET LMT C1105 35
HET SO4 C1106 5
HET GOL C1107 6
HET GOL C1108 6
HET PTY C1109 50
HET PTY C1110 50
HET PTY C1111 50
HET D12 C1112 12
HET D12 C1113 12
HET D12 C1114 12
HET ETE C1115 14
HET OCT C1116 8
HET HEX C1117 6
HET GOL D 201 6
HET GOL E 201 6
HET GOL E 202 6
HETNAM FUA FUSIDIC ACID
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETNAM HEX HEXANE
HETNAM PTY PHOSPHATIDYLETHANOLAMINE
HETNAM D12 DODECANE
HETNAM OCT N-OCTANE
HETNAM P3G 3,6,9,12,15-PENTAOXAHEPTADECANE
HETNAM D10 DECANE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 6 FUA 3(C31 H48 O6)
FORMUL 7 LMT 10(C24 H46 O11)
FORMUL 10 SO4 2(O4 S 2-)
FORMUL 11 GOL 8(C3 H8 O3)
FORMUL 12 ETE 3(C9 H20 O5)
FORMUL 14 HEX 2(C6 H14)
FORMUL 21 PTY 4(C40 H80 N O8 P)
FORMUL 22 D12 4(C12 H26)
FORMUL 23 OCT 2(C8 H18)
FORMUL 24 P3G C12 H26 O5
FORMUL 25 D10 2(C10 H22)
FORMUL 47 HOH *815(H2 O)
HELIX 1 AA1 MET A 1 ARG A 8 1 8
HELIX 2 AA2 ARG A 8 LEU A 30 1 23
HELIX 3 AA3 ASP A 53 VAL A 61 1 9
HELIX 4 AA4 VAL A 61 MET A 69 1 9
HELIX 5 AA5 ASP A 99 MET A 115 1 17
HELIX 6 AA6 PRO A 116 LEU A 118 5 3
HELIX 7 AA7 PRO A 119 GLY A 126 1 8
HELIX 8 AA8 THR A 150 MET A 162 1 13
HELIX 9 AA9 MET A 162 THR A 169 1 8
HELIX 10 AB1 ASN A 189 PHE A 196 1 8
HELIX 11 AB2 THR A 199 ASN A 211 1 13
HELIX 12 AB3 SER A 242 LYS A 248 1 7
HELIX 13 AB4 ASN A 298 LYS A 312 1 15
HELIX 14 AB5 MET A 313 PHE A 317 5 5
HELIX 15 AB6 THR A 329 GLN A 360 1 32
HELIX 16 AB7 ASN A 361 PHE A 386 1 26
HELIX 17 AB8 ASN A 391 GLU A 423 1 33
HELIX 18 AB9 PRO A 426 VAL A 454 1 29
HELIX 19 AC1 PRO A 455 ALA A 457 5 3
HELIX 20 AC2 THR A 463 LEU A 497 1 35
HELIX 21 AC3 GLY A 511 THR A 538 1 28
HELIX 22 AC4 THR A 538 LEU A 559 1 22
HELIX 23 AC5 THR A 583 LYS A 601 1 19
HELIX 24 AC6 ASP A 633 ARG A 637 5 5
HELIX 25 AC7 GLY A 639 ASN A 642 5 4
HELIX 26 AC8 LYS A 643 SER A 656 1 14
HELIX 27 AC9 GLY A 691 LYS A 708 1 18
HELIX 28 AD1 ASP A 732 GLY A 740 1 9
HELIX 29 AD2 SER A 742 GLY A 756 1 15
HELIX 30 AD3 ALA A 777 ARG A 780 5 4
HELIX 31 AD4 LEU A 782 ASP A 788 5 7
HELIX 32 AD5 SER A 836 LYS A 850 1 15
HELIX 33 AD6 GLY A 861 LEU A 868 1 8
HELIX 34 AD7 GLN A 872 GLU A 893 1 22
HELIX 35 AD8 ILE A 897 LEU A 903 1 7
HELIX 36 AD9 VAL A 904 GLY A 920 1 17
HELIX 37 AE1 ASP A 924 LYS A 955 1 32
HELIX 38 AE2 GLY A 959 ARG A 971 1 13
HELIX 39 AE3 LEU A 972 VAL A 986 1 15
HELIX 40 AE4 VAL A 986 SER A 992 1 7
HELIX 41 AE5 GLY A 996 PHE A 1033 1 38
HELIX 42 AE6 PRO B 2 ARG B 8 1 7
HELIX 43 AE7 ARG B 8 LEU B 30 1 23
HELIX 44 AE8 ASP B 53 VAL B 61 1 9
HELIX 45 AE9 VAL B 61 ASN B 68 1 8
HELIX 46 AF1 ASP B 99 MET B 115 1 17
HELIX 47 AF2 PRO B 116 LEU B 118 5 3
HELIX 48 AF3 PRO B 119 GLY B 126 1 8
HELIX 49 AF4 THR B 150 MET B 162 1 13
HELIX 50 AF5 MET B 162 ARG B 168 1 7
HELIX 51 AF6 ASN B 189 PHE B 196 1 8
HELIX 52 AF7 THR B 199 ASN B 211 1 13
HELIX 53 AF8 SER B 242 LYS B 248 1 7
HELIX 54 AF9 ASN B 298 GLU B 314 1 17
HELIX 55 AG1 PRO B 315 PHE B 317 5 3
HELIX 56 AG2 THR B 329 GLN B 360 1 32
HELIX 57 AG3 ASN B 361 PHE B 386 1 26
HELIX 58 AG4 ASN B 391 GLY B 424 1 34
HELIX 59 AG5 PRO B 426 VAL B 454 1 29
HELIX 60 AG6 PRO B 455 PHE B 459 5 5
HELIX 61 AG7 GLY B 460 LEU B 497 1 38
HELIX 62 AG8 LYS B 510 SER B 537 1 28
HELIX 63 AG9 SER B 537 LEU B 559 1 23
HELIX 64 AH1 THR B 583 LYS B 601 1 19
HELIX 65 AH2 ASP B 633 ARG B 637 5 5
HELIX 66 AH3 GLY B 639 ASN B 642 5 4
HELIX 67 AH4 LYS B 643 PHE B 655 1 13
HELIX 68 AH5 SER B 656 ILE B 658 5 3
HELIX 69 AH6 GLY B 691 LYS B 708 1 18
HELIX 70 AH7 ASP B 732 GLY B 740 1 9
HELIX 71 AH8 SER B 742 GLY B 756 1 15
HELIX 72 AH9 ALA B 777 ARG B 780 5 4
HELIX 73 AI1 LEU B 782 ASP B 788 5 7
HELIX 74 AI2 SER B 836 SER B 849 1 14
HELIX 75 AI3 THR B 860 SER B 869 1 10
HELIX 76 AI4 ASN B 871 GLU B 893 1 23
HELIX 77 AI5 ILE B 897 LEU B 903 1 7
HELIX 78 AI6 VAL B 904 GLY B 920 1 17
HELIX 79 AI7 ASP B 924 LYS B 955 1 32
HELIX 80 AI8 GLY B 959 VAL B 986 1 28
HELIX 81 AI9 VAL B 986 SER B 992 1 7
HELIX 82 AJ1 GLY B 996 PHE B 1033 1 38
HELIX 83 AJ2 PRO C 2 ARG C 8 1 7
HELIX 84 AJ3 ARG C 8 LEU C 30 1 23
HELIX 85 AJ4 ASP C 53 VAL C 61 1 9
HELIX 86 AJ5 VAL C 61 GLN C 67 1 7
HELIX 87 AJ6 ASP C 99 MET C 115 1 17
HELIX 88 AJ7 PRO C 116 LEU C 118 5 3
HELIX 89 AJ8 PRO C 119 GLY C 126 1 8
HELIX 90 AJ9 THR C 150 MET C 162 1 13
HELIX 91 AK1 MET C 162 ARG C 168 1 7
HELIX 92 AK2 ASN C 189 PHE C 196 1 8
HELIX 93 AK3 THR C 199 ASN C 211 1 13
HELIX 94 AK4 SER C 242 LYS C 248 1 7
HELIX 95 AK5 ASN C 298 GLU C 314 1 17
HELIX 96 AK6 PRO C 315 PHE C 317 5 3
HELIX 97 AK7 THR C 329 GLN C 360 1 32
HELIX 98 AK8 ASN C 361 ILE C 370 1 10
HELIX 99 AK9 ILE C 370 PHE C 386 1 17
HELIX 100 AL1 ASN C 391 VAL C 406 1 16
HELIX 101 AL2 VAL C 406 GLY C 424 1 19
HELIX 102 AL3 PRO C 426 VAL C 452 1 27
HELIX 103 AL4 PHE C 453 PHE C 458 1 6
HELIX 104 AL5 GLY C 460 MET C 496 1 37
HELIX 105 AL6 GLY C 511 SER C 537 1 27
HELIX 106 AL7 SER C 537 LEU C 559 1 23
HELIX 107 AL8 THR C 583 LYS C 601 1 19
HELIX 108 AL9 ASP C 633 ARG C 637 5 5
HELIX 109 AM1 GLY C 639 ASN C 642 5 4
HELIX 110 AM2 LYS C 643 SER C 656 1 14
HELIX 111 AM3 GLY C 691 LYS C 708 1 18
HELIX 112 AM4 ASP C 732 GLY C 740 1 9
HELIX 113 AM5 SER C 742 GLY C 755 1 14
HELIX 114 AM6 ALA C 777 ARG C 780 5 4
HELIX 115 AM7 LEU C 782 ASP C 788 5 7
HELIX 116 AM8 SER C 836 LYS C 850 1 15
HELIX 117 AM9 THR C 860 GLU C 893 1 34
HELIX 118 AN1 TRP C 895 LEU C 903 1 9
HELIX 119 AN2 VAL C 904 GLY C 920 1 17
HELIX 120 AN3 ASP C 924 GLU C 956 1 33
HELIX 121 AN4 GLY C 959 VAL C 986 1 28
HELIX 122 AN5 VAL C 986 ILE C 991 1 6
HELIX 123 AN6 GLY C 996 LEU C 1017 1 22
HELIX 124 AN7 LEU C 1017 PHE C 1033 1 17
HELIX 125 AN8 SER D 12 GLY D 25 1 14
HELIX 126 AN9 ARG D 26 ASN D 36 1 11
HELIX 127 AO1 THR D 49 GLY D 58 1 10
HELIX 128 AO2 HIS D 59 ASN D 69 1 11
HELIX 129 AO3 THR D 82 PHE D 90 1 9
HELIX 130 AO4 HIS D 92 ASN D 102 1 11
HELIX 131 AO5 THR D 115 ARG D 123 1 9
HELIX 132 AO6 HIS D 125 TYR D 135 1 11
HELIX 133 AO7 THR D 148 GLY D 157 1 10
HELIX 134 AO8 ASN D 158 GLN D 166 1 9
HELIX 135 AO9 LEU E 14 GLY E 25 1 12
HELIX 136 AP1 ARG E 26 ASN E 36 1 11
HELIX 137 AP2 THR E 49 GLY E 58 1 10
HELIX 138 AP3 HIS E 59 ASN E 69 1 11
HELIX 139 AP4 THR E 82 PHE E 90 1 9
HELIX 140 AP5 HIS E 92 ASN E 102 1 11
HELIX 141 AP6 THR E 115 ARG E 123 1 9
HELIX 142 AP7 HIS E 125 TYR E 135 1 11
HELIX 143 AP8 THR E 148 ASN E 156 1 9
HELIX 144 AP9 ASN E 158 GLN E 166 1 9
SHEET 1 AA1 7 SER A 128 LYS A 131 0
SHEET 2 AA1 7 ALA A 42 SER A 48 -1 N THR A 44 O GLU A 130
SHEET 3 AA1 7 THR A 87 PHE A 94 -1 O ILE A 90 N ILE A 45
SHEET 4 AA1 7 LEU A 75 ASP A 83 -1 N MET A 76 O THR A 93
SHEET 5 AA1 7 ARG A 815 TYR A 819 -1 O LEU A 816 N SER A 82
SHEET 6 AA1 7 LEU A 822 ALA A 831 -1 O LEU A 822 N TYR A 819
SHEET 7 AA1 7 LEU A 713 PRO A 718 -1 N THR A 714 O GLN A 830
SHEET 1 AA2 8 SER A 128 LYS A 131 0
SHEET 2 AA2 8 ALA A 42 SER A 48 -1 N THR A 44 O GLU A 130
SHEET 3 AA2 8 THR A 87 PHE A 94 -1 O ILE A 90 N ILE A 45
SHEET 4 AA2 8 LEU A 75 ASP A 83 -1 N MET A 76 O THR A 93
SHEET 5 AA2 8 ARG A 815 TYR A 819 -1 O LEU A 816 N SER A 82
SHEET 6 AA2 8 LEU A 822 ALA A 831 -1 O LEU A 822 N TYR A 819
SHEET 7 AA2 8 GLY A 679 ASP A 686 -1 N ASP A 686 O PRO A 823
SHEET 8 AA2 8 VAL A 855 TRP A 859 -1 O GLY A 856 N ILE A 685
SHEET 1 AA3 4 VAL A 172 LEU A 177 0
SHEET 2 AA3 4 GLN A 284 LEU A 293 -1 O GLY A 290 N GLN A 176
SHEET 3 AA3 4 MET A 138 ASN A 144 -1 N VAL A 140 O LEU A 289
SHEET 4 AA3 4 LEU A 321 ASP A 328 -1 O LYS A 322 N ILE A 143
SHEET 1 AA4 7 VAL A 172 LEU A 177 0
SHEET 2 AA4 7 GLN A 284 LEU A 293 -1 O GLY A 290 N GLN A 176
SHEET 3 AA4 7 ILE A 278 PHE A 281 -1 N PHE A 281 O GLN A 284
SHEET 4 AA4 7 VAL A 606 PHE A 615 -1 O ASN A 613 N ILE A 278
SHEET 5 AA4 7 ARG A 620 LEU A 631 -1 O ILE A 626 N VAL A 612
SHEET 6 AA4 7 VAL A 571 GLN A 577 -1 N VAL A 576 O GLY A 625
SHEET 7 AA4 7 MET A 662 PHE A 666 -1 O MET A 662 N GLN A 577
SHEET 1 AA5 4 ALA A 266 GLY A 272 0
SHEET 2 AA5 4 TYR A 182 MET A 188 -1 N TRP A 187 O LYS A 267
SHEET 3 AA5 4 ARG A 767 SER A 775 1 O MET A 774 N MET A 188
SHEET 4 AA5 4 SER A 757 ASP A 764 -1 N PHE A 762 O LYS A 769
SHEET 1 AA6 4 ALA A 215 LEU A 219 0
SHEET 2 AA6 4 ALA A 232 ILE A 235 -1 O ALA A 232 N LEU A 219
SHEET 3 AA6 4 THR B 724 ILE B 731 1 O ILE B 729 N ILE A 235
SHEET 4 AA6 4 SER B 805 GLY B 812 -1 O SER B 806 N ASP B 730
SHEET 1 AA7 2 LEU A 250 VAL A 253 0
SHEET 2 AA7 2 ARG A 259 LEU A 261 -1 O VAL A 260 N LYS A 252
SHEET 1 AA8 4 SER A 805 GLY A 812 0
SHEET 2 AA8 4 THR A 724 ILE A 731 -1 N ASP A 730 O SER A 806
SHEET 3 AA8 4 ALA C 232 ILE C 235 1 O ILE C 235 N ILE A 729
SHEET 4 AA8 4 ALA C 215 LEU C 219 -1 N LEU C 219 O ALA C 232
SHEET 1 AA9 2 TYR A 790 ARG A 792 0
SHEET 2 AA9 2 MET A 798 PRO A 800 -1 O VAL A 799 N VAL A 791
SHEET 1 AB1 7 SER B 128 LYS B 131 0
SHEET 2 AB1 7 ALA B 42 SER B 48 -1 N SER B 46 O SER B 128
SHEET 3 AB1 7 THR B 87 PHE B 94 -1 O ILE B 90 N ILE B 45
SHEET 4 AB1 7 LEU B 75 ASP B 83 -1 N SER B 79 O THR B 91
SHEET 5 AB1 7 ARG B 815 TYR B 819 -1 O LEU B 816 N SER B 82
SHEET 6 AB1 7 LEU B 822 ALA B 831 -1 O LEU B 822 N TYR B 819
SHEET 7 AB1 7 LEU B 713 PRO B 718 -1 N ARG B 717 O LEU B 828
SHEET 1 AB2 8 SER B 128 LYS B 131 0
SHEET 2 AB2 8 ALA B 42 SER B 48 -1 N SER B 46 O SER B 128
SHEET 3 AB2 8 THR B 87 PHE B 94 -1 O ILE B 90 N ILE B 45
SHEET 4 AB2 8 LEU B 75 ASP B 83 -1 N SER B 79 O THR B 91
SHEET 5 AB2 8 ARG B 815 TYR B 819 -1 O LEU B 816 N SER B 82
SHEET 6 AB2 8 LEU B 822 ALA B 831 -1 O LEU B 822 N TYR B 819
SHEET 7 AB2 8 PHE B 680 ASP B 686 -1 N PHE B 680 O GLY B 829
SHEET 8 AB2 8 VAL B 855 TRP B 859 -1 O ASP B 858 N GLU B 683
SHEET 1 AB3 4 VAL B 172 LEU B 177 0
SHEET 2 AB3 4 GLN B 284 LEU B 293 -1 O LYS B 292 N ASP B 174
SHEET 3 AB3 4 MET B 138 ASN B 144 -1 N VAL B 142 O SER B 287
SHEET 4 AB3 4 LEU B 321 ASP B 328 -1 O VAL B 324 N GLY B 141
SHEET 1 AB4 7 VAL B 172 LEU B 177 0
SHEET 2 AB4 7 GLN B 284 LEU B 293 -1 O LYS B 292 N ASP B 174
SHEET 3 AB4 7 ILE B 278 PHE B 281 -1 N PHE B 281 O GLN B 284
SHEET 4 AB4 7 VAL B 606 ASN B 613 -1 O ASN B 613 N ILE B 278
SHEET 5 AB4 7 THR B 624 LEU B 631 -1 O ILE B 626 N VAL B 612
SHEET 6 AB4 7 VAL B 571 GLN B 577 -1 N PHE B 572 O VAL B 629
SHEET 7 AB4 7 MET B 662 ASN B 667 -1 O MET B 662 N GLN B 577
SHEET 1 AB5 4 ALA B 266 GLY B 271 0
SHEET 2 AB5 4 ALA B 183 MET B 188 -1 N ALA B 183 O GLY B 271
SHEET 3 AB5 4 ARG B 767 SER B 775 1 O MET B 774 N MET B 188
SHEET 4 AB5 4 SER B 757 ASP B 764 -1 N PHE B 762 O LYS B 769
SHEET 1 AB6 4 GLY B 217 LEU B 219 0
SHEET 2 AB6 4 ALA B 232 ILE B 235 -1 O ALA B 232 N LEU B 219
SHEET 3 AB6 4 THR C 724 ILE C 731 1 O PHE C 727 N SER B 233
SHEET 4 AB6 4 SER C 805 GLY C 812 -1 O SER C 806 N ASP C 730
SHEET 1 AB7 2 LEU B 250 VAL B 253 0
SHEET 2 AB7 2 ARG B 259 LEU B 261 -1 O VAL B 260 N LYS B 252
SHEET 1 AB8 2 TYR B 790 ARG B 792 0
SHEET 2 AB8 2 MET B 798 PRO B 800 -1 O VAL B 799 N VAL B 791
SHEET 1 AB9 7 SER C 128 SER C 132 0
SHEET 2 AB9 7 ALA C 42 SER C 48 -1 N THR C 44 O GLU C 130
SHEET 3 AB9 7 THR C 87 PHE C 94 -1 O VAL C 88 N ALA C 47
SHEET 4 AB9 7 LEU C 75 ASP C 83 -1 N SER C 79 O THR C 91
SHEET 5 AB9 7 ARG C 815 TYR C 819 -1 O LEU C 816 N SER C 82
SHEET 6 AB9 7 LEU C 822 ALA C 831 -1 O LEU C 822 N TYR C 819
SHEET 7 AB9 7 LEU C 713 PRO C 718 -1 N ARG C 717 O LEU C 828
SHEET 1 AC1 8 SER C 128 SER C 132 0
SHEET 2 AC1 8 ALA C 42 SER C 48 -1 N THR C 44 O GLU C 130
SHEET 3 AC1 8 THR C 87 PHE C 94 -1 O VAL C 88 N ALA C 47
SHEET 4 AC1 8 LEU C 75 ASP C 83 -1 N SER C 79 O THR C 91
SHEET 5 AC1 8 ARG C 815 TYR C 819 -1 O LEU C 816 N SER C 82
SHEET 6 AC1 8 LEU C 822 ALA C 831 -1 O LEU C 822 N TYR C 819
SHEET 7 AC1 8 PHE C 680 ASP C 686 -1 N PHE C 682 O ILE C 827
SHEET 8 AC1 8 VAL C 855 TRP C 859 -1 O GLY C 856 N ILE C 685
SHEET 1 AC2 4 VAL C 172 LEU C 177 0
SHEET 2 AC2 4 GLN C 284 LEU C 293 -1 O LYS C 292 N GLY C 173
SHEET 3 AC2 4 MET C 138 ASN C 144 -1 N VAL C 142 O SER C 287
SHEET 4 AC2 4 LEU C 321 ASP C 328 -1 O TYR C 327 N VAL C 139
SHEET 1 AC3 7 VAL C 172 LEU C 177 0
SHEET 2 AC3 7 GLN C 284 LEU C 293 -1 O LYS C 292 N GLY C 173
SHEET 3 AC3 7 ILE C 278 PHE C 281 -1 N PHE C 281 O GLN C 284
SHEET 4 AC3 7 VAL C 606 PHE C 615 -1 O ASN C 613 N ILE C 278
SHEET 5 AC3 7 ARG C 620 LEU C 631 -1 O ILE C 626 N VAL C 612
SHEET 6 AC3 7 VAL C 571 GLN C 577 -1 N PHE C 572 O VAL C 629
SHEET 7 AC3 7 MET C 662 PHE C 666 -1 O MET C 662 N GLN C 577
SHEET 1 AC4 4 ALA C 266 GLY C 272 0
SHEET 2 AC4 4 TYR C 182 MET C 188 -1 N ALA C 183 O GLY C 271
SHEET 3 AC4 4 ARG C 767 SER C 775 1 O MET C 774 N MET C 188
SHEET 4 AC4 4 SER C 757 ASP C 764 -1 N PHE C 762 O LYS C 769
SHEET 1 AC5 2 LEU C 250 VAL C 253 0
SHEET 2 AC5 2 ARG C 259 LEU C 261 -1 O VAL C 260 N LYS C 252
SHEET 1 AC6 2 TYR C 790 ARG C 792 0
SHEET 2 AC6 2 MET C 798 PRO C 800 -1 O VAL C 799 N VAL C 791
CISPEP 1 THR A 222 PRO A 223 0 -5.41
CISPEP 2 THR B 222 PRO B 223 0 -7.39
CISPEP 3 THR C 222 PRO C 223 0 -5.24
SITE 1 AC1 6 ILE A 27 LYS A 334 HIS A 338 VAL A 341
SITE 2 AC1 6 LMT A1103 HOH A1201
SITE 1 AC2 7 GLY A 440 GLY A 444 CYS A 887 ALA A 890
SITE 2 AC2 7 LEU A 891 ARG C 8 PHE C 11
SITE 1 AC3 5 ILE A 27 VAL A 32 VAL A 341 ILE A 348
SITE 2 AC3 5 FUA A1101
SITE 1 AC4 7 ARG A 8 PHE A 11 GLN B 439 GLY B 440
SITE 2 AC4 7 VAL B 443 GLY B 444 P3G B1110
SITE 1 AC5 4 ARG A 185 GLU A 273 GLY A 755 TYR A 772
SITE 1 AC6 5 THR A 696 ASN A 700 HOH A1340 ARG E 23
SITE 2 AC6 5 TRP E 57
SITE 1 AC7 2 ALA A 385 HOH A1318
SITE 1 AC8 2 GLY A 957 ARG A1031
SITE 1 AC9 5 LEU B 300 HIS B 338 VAL B 341 LMT B1104
SITE 2 AC9 5 HOH B1308
SITE 1 AD1 7 SER B 530 GLY B 533 ARG B 536 ARG B 540
SITE 2 AD1 7 TYR B 541 PHE B1020 ASP D 72
SITE 1 AD2 1 ARG B 363
SITE 1 AD3 10 ILE B 27 ASN B 298 LEU B 300 ASP B 301
SITE 2 AD3 10 ALA B 304 PHE B 380 FUA B1101 HOH B1202
SITE 3 AD3 10 HOH B1206 HOH B1308
SITE 1 AD4 6 ARG B 239 TYR B 758 ASN B 760 ASP B 761
SITE 2 AD4 6 PRO C 119 GLN C 120
SITE 1 AD5 4 GLN B 108 MET B 115 VAL B 127 GLN C 112
SITE 1 AD6 5 PHE B 899 PHE B1033 HOH B1314 HOH B1323
SITE 2 AD6 5 HOH B1324
SITE 1 AD7 2 MET B 1 MET B 447
SITE 1 AD8 2 LMT A1104 GLN B 439
SITE 1 AD9 2 LYS A 29 VAL B 454
SITE 1 AE1 4 LYS C 334 HIS C 338 VAL C 341 LMT C1104
SITE 1 AE2 6 ALA C 22 LEU C 25 ALA C 26 LYS C 29
SITE 2 AE2 6 HOH C1230 HOH C1381
SITE 1 AE3 5 SER C 530 GLY C 533 ARG C 536 ARG C 540
SITE 2 AE3 5 TYR C 541
SITE 1 AE4 4 LEU C 28 VAL C 32 FUA C1101 HOH C1232
SITE 1 AE5 1 TRP C 515
SITE 1 AE6 3 GLY C 691 HIS C 692 HOH C1272
SITE 1 AE7 6 ARG C 185 GLU C 273 ASN C 274 GLY C 755
SITE 2 AE7 6 GLY C 756 MET C 774
SITE 1 AE8 8 ALA C 160 ASN C 161 ASP C 764 ARG C 765
SITE 2 AE8 8 ARG C 767 LYS C 769 HOH C1222 HOH C1290
SITE 1 AE9 3 VAL C 454 PHE C 458 SER C 875
SITE 1 AF1 7 ARG B 8 PHE B 11 GLN C 439 LEU C 891
SITE 2 AF1 7 GLU C 893 GLU C 947 HEX C1117
SITE 1 AF2 5 SER C 894 TRP C 895 SER C 896 ARG C1030
SITE 2 AF2 5 HOH C1278
SITE 1 AF3 3 MET C 552 PHE C 556 VAL C 557
SITE 1 AF4 2 GLY C 387 PHE C 388
SITE 1 AF5 1 HOH C1307
SITE 1 AF6 2 MET C 1 PTY C1110
SITE 1 AF7 2 ASP D 143 LYS D 147
SITE 1 AF8 3 HOH A1291 ASP E 143 LYS E 147
SITE 1 AF9 4 TYR A 811 GLU E 20 ARG E 23 ASP E 44
CRYST1 145.654 163.248 246.042 90.00 90.00 90.00 P 21 21 21 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 0.006866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004064 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
