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HEADER HYDROLASE 23-MAR-22 7ZB0
TITLE MACROCYCLASE OPHP WITH 15MER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MACROCYCLASE,OPHP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 15MER;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OMPHALOTUS OLEARIUS;
SOURCE 3 ORGANISM_TAXID: 72120;
SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: OMPHALOTUS OLEARIUS;
SOURCE 9 ORGANISM_TAXID: 72120;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MACROCYCLASE FOR OMPHALOTIN A BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SONG,J.H.NAISMITH
REVDAT 1 06-JUL-22 7ZB0 0
JRNL AUTH H.SONG,J.H.NAISMITH
JRNL TITL APO MACROCYCLASE OPHP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 99258
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5223
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) : 2.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7283
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3730
REMARK 3 BIN FREE R VALUE SET COUNT : 395
REMARK 3 BIN FREE R VALUE : 0.4100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 53
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.58000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 1.03000
REMARK 3 B13 (A**2) : -0.26000
REMARK 3 B23 (A**2) : 1.94000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.325
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.391
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.376
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23879 ; 0.007 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 21651 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32378 ; 1.464 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 49975 ; 1.184 ; 1.576
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2857 ; 7.616 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1315 ;31.672 ;21.901
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3789 ;15.755 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 151 ;17.125 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2983 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27066 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5756 ; 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): 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 4 808 B 4 808 23799 0.080 0.050
REMARK 3 2 A 4 809 C 4 809 23647 0.070 0.050
REMARK 3 3 A 4 809 D 4 809 23866 0.080 0.050
REMARK 3 4 B 4 808 C 4 808 23457 0.070 0.050
REMARK 3 5 B 4 808 D 4 808 24125 0.070 0.050
REMARK 3 6 C 4 809 D 4 809 23550 0.080 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 807
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8198 0.3454 -79.5098
REMARK 3 T TENSOR
REMARK 3 T11: 0.2095 T22: 0.8274
REMARK 3 T33: 0.2846 T12: 0.1827
REMARK 3 T13: 0.1453 T23: 0.4025
REMARK 3 L TENSOR
REMARK 3 L11: 1.0721 L22: 0.6131
REMARK 3 L33: 1.7398 L12: -0.1503
REMARK 3 L13: -0.0533 L23: -0.2653
REMARK 3 S TENSOR
REMARK 3 S11: -0.1227 S12: 0.0411 S13: -0.1173
REMARK 3 S21: 0.0493 S22: 0.0196 S23: 0.0119
REMARK 3 S31: 0.0843 S32: 0.1480 S33: 0.1031
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 802
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4273 27.6501 -29.5148
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: 0.4580
REMARK 3 T33: 0.6734 T12: 0.0166
REMARK 3 T13: -0.0549 T23: 0.4020
REMARK 3 L TENSOR
REMARK 3 L11: 1.7359 L22: 1.8771
REMARK 3 L33: 0.9301 L12: -0.7443
REMARK 3 L13: 0.2736 L23: -0.7955
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: 0.3236 S13: 0.1519
REMARK 3 S21: 0.0652 S22: -0.2034 S23: -0.4059
REMARK 3 S31: -0.0774 S32: 0.1418 S33: 0.1959
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 805
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2651 5.1986 18.1090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1852 T22: 0.8409
REMARK 3 T33: 0.4040 T12: 0.2817
REMARK 3 T13: -0.0411 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 3.4154 L22: 0.5032
REMARK 3 L33: 1.2050 L12: 0.2460
REMARK 3 L13: -0.4510 L23: -0.1166
REMARK 3 S TENSOR
REMARK 3 S11: -0.3417 S12: -0.9587 S13: 0.6235
REMARK 3 S21: -0.0185 S22: 0.2033 S23: -0.0107
REMARK 3 S31: 0.0843 S32: 0.1393 S33: 0.1383
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 806
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9410 -26.1647 -33.5017
REMARK 3 T TENSOR
REMARK 3 T11: 0.1630 T22: 0.4673
REMARK 3 T33: 0.2514 T12: 0.1408
REMARK 3 T13: 0.1104 T23: 0.3078
REMARK 3 L TENSOR
REMARK 3 L11: 1.6976 L22: 1.2452
REMARK 3 L33: 0.9404 L12: -0.0130
REMARK 3 L13: 0.3277 L23: -0.7034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0873 S12: 0.0604 S13: -0.0344
REMARK 3 S21: -0.1825 S22: -0.1621 S23: -0.0989
REMARK 3 S31: 0.0369 S32: 0.1403 S33: 0.0748
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7ZB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-22.
REMARK 100 THE DEPOSITION ID IS D_1292121109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104483
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.470
REMARK 200 RESOLUTION RANGE LOW (A) : 64.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 1.37500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5N4C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M BIS-TRIS
REMARK 280 PROPANE (PH 6.0-6.5) AND 28% PEG 3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 225
REMARK 465 ASP A 226
REMARK 465 GLU A 227
REMARK 465 GLY A 228
REMARK 465 LYS A 229
REMARK 465 HIS A 701
REMARK 465 PHE A 702
REMARK 465 ALA A 703
REMARK 465 GLY A 704
REMARK 465 GLN A 732
REMARK 465 GLY A 733
REMARK 465 SER A 734
REMARK 465 VAL A 735
REMARK 465 ASP A 736
REMARK 465 SER A 737
REMARK 465 SER A 738
REMARK 465 ARG A 739
REMARK 465 TRP A 740
REMARK 465 SER A 741
REMARK 465 CYS A 742
REMARK 465 VAL A 743
REMARK 465 THR A 744
REMARK 465 VAL A 745
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 PHE B 3
REMARK 465 ASP B 225
REMARK 465 ASP B 226
REMARK 465 GLU B 227
REMARK 465 GLY B 228
REMARK 465 LYS B 229
REMARK 465 SER B 699
REMARK 465 GLY B 700
REMARK 465 HIS B 701
REMARK 465 PHE B 702
REMARK 465 THR B 731
REMARK 465 GLN B 732
REMARK 465 GLY B 733
REMARK 465 SER B 734
REMARK 465 VAL B 735
REMARK 465 ASP B 736
REMARK 465 SER B 737
REMARK 465 SER B 738
REMARK 465 ARG B 739
REMARK 465 TRP B 740
REMARK 465 SER B 741
REMARK 465 CYS B 742
REMARK 465 VAL B 743
REMARK 465 THR B 744
REMARK 465 VAL B 745
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 PHE C 3
REMARK 465 ASP C 142
REMARK 465 GLY C 143
REMARK 465 ASN C 144
REMARK 465 ALA C 145
REMARK 465 SER C 164
REMARK 465 GLU C 165
REMARK 465 GLN C 186
REMARK 465 GLU C 187
REMARK 465 ARG C 188
REMARK 465 ASP C 226
REMARK 465 GLU C 227
REMARK 465 GLY C 228
REMARK 465 LYS C 229
REMARK 465 GLY C 230
REMARK 465 LEU C 697
REMARK 465 ASN C 698
REMARK 465 SER C 699
REMARK 465 GLY C 700
REMARK 465 HIS C 701
REMARK 465 PHE C 702
REMARK 465 ALA C 703
REMARK 465 GLY C 704
REMARK 465 GLN C 732
REMARK 465 GLY C 733
REMARK 465 SER C 734
REMARK 465 VAL C 735
REMARK 465 ASP C 736
REMARK 465 SER C 737
REMARK 465 SER C 738
REMARK 465 ARG C 739
REMARK 465 TRP C 740
REMARK 465 SER C 741
REMARK 465 CYS C 742
REMARK 465 VAL C 743
REMARK 465 THR C 744
REMARK 465 VAL C 745
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 PHE D 3
REMARK 465 ASP D 225
REMARK 465 ASP D 226
REMARK 465 GLU D 227
REMARK 465 GLY D 228
REMARK 465 LYS D 229
REMARK 465 GLY D 230
REMARK 465 SER D 699
REMARK 465 GLY D 700
REMARK 465 HIS D 701
REMARK 465 PHE D 702
REMARK 465 GLY D 733
REMARK 465 SER D 734
REMARK 465 VAL D 735
REMARK 465 ASP D 736
REMARK 465 SER D 737
REMARK 465 SER D 738
REMARK 465 ARG D 739
REMARK 465 TRP D 740
REMARK 465 SER D 741
REMARK 465 CYS D 742
REMARK 465 VAL D 743
REMARK 465 THR D 744
REMARK 465 VAL D 745
REMARK 465 GLY E 801
REMARK 465 PHE E 802
REMARK 465 PRO E 803
REMARK 465 TRP E 804
REMARK 465 MVA E 810
REMARK 465 IML E 811
REMARK 465 SAR E 812
REMARK 465 VAL E 813
REMARK 465 ILE E 814
REMARK 465 GLY E 815
REMARK 465 GLY F 801
REMARK 465 SAR F 809
REMARK 465 MVA F 810
REMARK 465 IML F 811
REMARK 465 SAR F 812
REMARK 465 VAL F 813
REMARK 465 ILE F 814
REMARK 465 GLY F 815
REMARK 465 GLY G 801
REMARK 465 PHE G 802
REMARK 465 PRO G 803
REMARK 465 TRP G 804
REMARK 465 MVA G 810
REMARK 465 IML G 811
REMARK 465 SAR G 812
REMARK 465 VAL G 813
REMARK 465 ILE G 814
REMARK 465 GLY G 815
REMARK 465 SAR H 812
REMARK 465 VAL H 813
REMARK 465 ILE H 814
REMARK 465 GLY H 815
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 OD2 ASP B 472 OG1 THR B 474 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 HIS A 166 -87.41 -41.57
REMARK 500 SER A 180 62.47 -117.26
REMARK 500 PRO A 192 -92.76 -46.21
REMARK 500 HIS A 201 35.93 72.90
REMARK 500 ASN A 231 -27.50 81.16
REMARK 500 ASN A 236 48.59 74.07
REMARK 500 HIS A 260 70.29 -115.30
REMARK 500 ASP A 283 -165.46 -165.09
REMARK 500 GLU A 297 14.17 -143.29
REMARK 500 ASN A 303 53.57 -109.26
REMARK 500 ALA A 335 85.74 -155.13
REMARK 500 TYR A 338 152.40 76.49
REMARK 500 GLN A 372 -47.88 74.45
REMARK 500 ASP A 373 26.69 -143.30
REMARK 500 TYR A 499 -79.22 -121.71
REMARK 500 TYR A 536 40.21 -109.56
REMARK 500 LEU A 546 -116.42 51.49
REMARK 500 ALA A 580 -109.23 55.47
REMARK 500 ALA A 593 56.75 -153.02
REMARK 500 ILE A 607 -44.19 -135.86
REMARK 500 THR A 616 -110.65 34.12
REMARK 500 SER A 641 102.78 -45.64
REMARK 500 ASP A 651 30.37 -148.17
REMARK 500 HIS B 166 53.33 36.91
REMARK 500 SER B 180 57.64 -117.29
REMARK 500 HIS B 201 35.62 72.58
REMARK 500 ASN B 231 16.61 -153.65
REMARK 500 ASN B 236 47.19 75.54
REMARK 500 HIS B 260 69.31 -117.55
REMARK 500 ASP B 283 -164.52 -161.58
REMARK 500 GLU B 297 13.42 -141.15
REMARK 500 ASN B 303 41.54 -101.78
REMARK 500 ALA B 335 86.53 -157.97
REMARK 500 TYR B 338 151.71 77.80
REMARK 500 GLN B 372 -50.31 76.82
REMARK 500 ASP B 373 26.04 -143.67
REMARK 500 TYR B 499 -78.44 -120.59
REMARK 500 TYR B 536 40.34 -109.87
REMARK 500 LEU B 546 -116.96 51.03
REMARK 500 ALA B 580 -109.78 55.97
REMARK 500 ALA B 593 57.83 -153.51
REMARK 500 ILE B 607 -44.26 -136.19
REMARK 500 THR B 616 -113.79 39.85
REMARK 500 SER B 641 103.44 -46.44
REMARK 500 ASP B 651 42.88 -149.42
REMARK 500 THR B 652 -90.09 -115.73
REMARK 500 VAL B 653 99.57 81.45
REMARK 500 SER C 140 -142.51 -95.87
REMARK 500 SER C 180 61.60 -117.22
REMARK 500 LYS C 190 -157.64 -169.05
REMARK 500
REMARK 500 THIS ENTRY HAS 97 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 GLN A 730 THR A 731 149.81
REMARK 500 MVA G 808 SAR G 809 146.31
REMARK 500 SAR H 809 MVA H 810 113.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 803 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 288 O
REMARK 620 2 ASP C 311 O 101.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 804 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 499 O
REMARK 620 2 GLY C 500 O 76.6
REMARK 620 3 ASN C 581 O 93.1 126.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 805 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU C 546 O
REMARK 620 2 TYR C 625 O 111.2
REMARK 620 3 TYR C 640 OH 139.7 108.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 806 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 481 OG1
REMARK 620 2 TYR D 525 O 105.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 805 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL D 600 O
REMARK 620 2 THR D 602 OG1 121.4
REMARK 620 3 LEU D 658 O 70.3 105.0
REMARK 620 N 1 2
DBREF 7ZB0 A 1 745 PDB 7ZB0 7ZB0 1 745
DBREF 7ZB0 B 1 745 PDB 7ZB0 7ZB0 1 745
DBREF 7ZB0 C 1 745 PDB 7ZB0 7ZB0 1 745
DBREF 7ZB0 D 1 745 PDB 7ZB0 7ZB0 1 745
DBREF 7ZB0 E 801 815 PDB 7ZB0 7ZB0 801 815
DBREF 7ZB0 F 801 815 PDB 7ZB0 7ZB0 801 815
DBREF 7ZB0 G 801 815 PDB 7ZB0 7ZB0 801 815
DBREF 7ZB0 H 801 815 PDB 7ZB0 7ZB0 801 815
SEQRES 1 A 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 A 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 A 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 A 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 A 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 A 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 A 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 A 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 A 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 A 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 A 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 A 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 A 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 A 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 A 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 A 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 A 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 A 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 A 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 A 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 A 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 A 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 A 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 A 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 A 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 A 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 A 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 A 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 A 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 A 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 A 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 A 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 A 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 A 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 A 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 A 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 A 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 A 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 A 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 A 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 A 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 A 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 A 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 A 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 A 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 A 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 A 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 A 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 A 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 A 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 A 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 A 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 A 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 A 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 A 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 A 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 A 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 A 745 CYS VAL THR VAL
SEQRES 1 B 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 B 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 B 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 B 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 B 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 B 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 B 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 B 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 B 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 B 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 B 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 B 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 B 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 B 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 B 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 B 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 B 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 B 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 B 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 B 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 B 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 B 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 B 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 B 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 B 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 B 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 B 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 B 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 B 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 B 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 B 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 B 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 B 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 B 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 B 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 B 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 B 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 B 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 B 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 B 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 B 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 B 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 B 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 B 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 B 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 B 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 B 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 B 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 B 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 B 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 B 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 B 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 B 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 B 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 B 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 B 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 B 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 B 745 CYS VAL THR VAL
SEQRES 1 C 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 C 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 C 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 C 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 C 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 C 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 C 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 C 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 C 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 C 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 C 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 C 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 C 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 C 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 C 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 C 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 C 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 C 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 C 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 C 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 C 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 C 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 C 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 C 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 C 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 C 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 C 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 C 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 C 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 C 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 C 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 C 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 C 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 C 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 C 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 C 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 C 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 C 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 C 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 C 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 C 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 C 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 C 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 C 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 C 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 C 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 C 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 C 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 C 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 C 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 C 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 C 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 C 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 C 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 C 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 C 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 C 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 C 745 CYS VAL THR VAL
SEQRES 1 D 745 MET SER PHE PRO GLY TRP GLY PRO TYR PRO PRO VAL GLU
SEQRES 2 D 745 ARG ASP GLU THR SER ALA ILE THR TYR SER SER LYS LEU
SEQRES 3 D 745 HIS GLY SER VAL THR VAL ARG ASP PRO TYR SER GLN LEU
SEQRES 4 D 745 GLU VAL PRO PHE GLU ASP SER GLU GLU THR LYS ALA PHE
SEQRES 5 D 745 VAL HIS SER GLN ARG LYS PHE ALA ARG THR TYR LEU ASP
SEQRES 6 D 745 GLU ASN PRO ASP ARG GLU ALA TRP LEU GLU THR LEU LYS
SEQRES 7 D 745 LYS SER TRP ASN TYR ARG ARG PHE SER ALA LEU LYS PRO
SEQRES 8 D 745 GLU SER ASP GLY HIS TYR TYR PHE GLU TYR ASN ASP GLY
SEQRES 9 D 745 LEU GLN SER GLN LEU SER LEU TYR ARG VAL ARG MET GLY
SEQRES 10 D 745 GLU GLU ASP THR VAL LEU THR GLU SER GLY PRO GLY GLY
SEQRES 11 D 745 GLU LEU PHE PHE ASN PRO ASN LEU LEU SER LEU ASP GLY
SEQRES 12 D 745 ASN ALA ALA LEU THR GLY PHE VAL MET SER PRO CYS GLY
SEQRES 13 D 745 ASN TYR TRP ALA TYR GLY VAL SER GLU HIS GLY SER ASP
SEQRES 14 D 745 TRP MET SER ILE TYR VAL ARG LYS THR SER SER PRO HIS
SEQRES 15 D 745 LEU PRO SER GLN GLU ARG GLY LYS ASP PRO GLY ARG MET
SEQRES 16 D 745 ASN ASP LYS ILE ARG HIS VAL ARG PHE PHE ILE VAL SER
SEQRES 17 D 745 TRP THR SER ASP SER LYS GLY PHE PHE TYR SER ARG TYR
SEQRES 18 D 745 PRO PRO GLU ASP ASP GLU GLY LYS GLY ASN ALA PRO ALA
SEQRES 19 D 745 MET ASN CYS MET VAL TYR TYR HIS ARG ILE GLY GLU ASP
SEQRES 20 D 745 GLN GLU SER ASP VAL LEU VAL HIS GLU ASP PRO GLU HIS
SEQRES 21 D 745 PRO PHE TRP ILE SER SER VAL GLN LEU THR PRO SER GLY
SEQRES 22 D 745 ARG TYR ILE LEU PHE ALA ALA SER ARG ASP ALA SER HIS
SEQRES 23 D 745 THR GLN LEU VAL LYS ILE ALA ASP LEU HIS GLU ASN ASP
SEQRES 24 D 745 ILE GLY THR ASN MET LYS TRP LYS ASN LEU HIS ASP PRO
SEQRES 25 D 745 TRP GLU ALA ARG PHE THR ILE VAL GLY ASP GLU GLY SER
SEQRES 26 D 745 LYS ILE TYR PHE MET THR ASN LEU LYS ALA LYS ASN TYR
SEQRES 27 D 745 LYS VAL ALA THR PHE ASP ALA ASN HIS PRO ASP GLU GLY
SEQRES 28 D 745 LEU THR THR LEU ILE ALA GLU ASP PRO ASN ALA PHE LEU
SEQRES 29 D 745 VAL SER ALA SER ILE HIS ALA GLN ASP LYS LEU LEU LEU
SEQRES 30 D 745 VAL TYR LEU ARG ASN ALA SER HIS GLU ILE HIS ILE ARG
SEQRES 31 D 745 ASP LEU THR THR GLY LYS PRO LEU GLY ARG ILE PHE GLU
SEQRES 32 D 745 ASP LEU LEU GLY GLN PHE MET VAL SER GLY ARG ARG GLN
SEQRES 33 D 745 ASP ASN ASP ILE PHE VAL LEU PHE SER SER PHE LEU SER
SEQRES 34 D 745 PRO GLY THR VAL TYR ARG TYR THR PHE GLY GLU GLU LYS
SEQRES 35 D 745 GLY TYR ARG SER LEU PHE ARG ALA ILE SER ILE PRO GLY
SEQRES 36 D 745 LEU ASN LEU ASP ASP PHE MET THR GLU SER VAL PHE TYR
SEQRES 37 D 745 PRO SER LYS ASP GLY THR SER VAL HIS MET PHE ILE THR
SEQRES 38 D 745 ARG PRO LYS ASP VAL LEU LEU ASP GLY THR SER PRO VAL
SEQRES 39 D 745 LEU GLN TYR GLY TYR GLY GLY PHE SER LEU ALA MET LEU
SEQRES 40 D 745 PRO THR PHE SER LEU SER THR LEU LEU PHE CYS LYS ILE
SEQRES 41 D 745 TYR ARG ALA ILE TYR ALA ILE PRO ASN ILE ARG GLY GLY
SEQRES 42 D 745 SER GLU TYR GLY GLU SER TRP HIS ARG GLU GLY MET LEU
SEQRES 43 D 745 ASP LYS LYS GLN ASN VAL PHE ASP ASP PHE ASN ALA ALA
SEQRES 44 D 745 THR GLU TRP LEU ILE ALA ASN LYS TYR ALA SER LYS ASP
SEQRES 45 D 745 ARG ILE ALA ILE ARG GLY GLY ALA ASN GLY GLY VAL LEU
SEQRES 46 D 745 THR THR ALA CYS ALA ASN GLN ALA PRO GLY LEU TYR ARG
SEQRES 47 D 745 CYS VAL ILE THR ILE GLU GLY ILE ILE ASP MET LEU ARG
SEQRES 48 D 745 PHE PRO LYS PHE THR PHE GLY ALA SER TRP ARG SER GLU
SEQRES 49 D 745 TYR GLY ASP PRO GLU ASP PRO GLU ASP PHE ASP PHE ILE
SEQRES 50 D 745 PHE LYS TYR SER PRO TYR HIS ASN ILE PRO PRO PRO GLY
SEQRES 51 D 745 ASP THR VAL MET PRO ALA MET LEU PHE PHE THR ALA ALA
SEQRES 52 D 745 TYR ASP ASP ARG VAL SER PRO LEU HIS THR PHE LYS HIS
SEQRES 53 D 745 VAL ALA ALA LEU GLN HIS ASN PHE PRO LYS GLY PRO ASN
SEQRES 54 D 745 PRO CYS LEU MET ARG ILE ASP LEU ASN SER GLY HIS PHE
SEQRES 55 D 745 ALA GLY LYS SER THR GLN GLU MET LEU GLU GLU THR ALA
SEQRES 56 D 745 ASP GLU TYR SER PHE ILE GLY LYS SER MET GLY LEU THR
SEQRES 57 D 745 MET GLN THR GLN GLY SER VAL ASP SER SER ARG TRP SER
SEQRES 58 D 745 CYS VAL THR VAL
SEQRES 1 E 15 GLY PHE PRO TRP MVA ILE MVA MVA SAR MVA IML SAR VAL
SEQRES 2 E 15 ILE GLY
SEQRES 1 F 15 GLY PHE PRO TRP MVA ILE MVA MVA SAR MVA IML SAR VAL
SEQRES 2 F 15 ILE GLY
SEQRES 1 G 15 GLY PHE PRO TRP MVA ILE MVA MVA SAR MVA IML SAR VAL
SEQRES 2 G 15 ILE GLY
SEQRES 1 H 15 GLY PHE PRO TRP MVA ILE MVA MVA SAR MVA IML SAR VAL
SEQRES 2 H 15 ILE GLY
HET MVA E 805 8
HET MVA E 807 8
HET MVA E 808 8
HET SAR E 809 5
HET MVA F 805 8
HET MVA F 807 8
HET MVA F 808 8
HET MVA G 805 8
HET MVA G 807 8
HET MVA G 808 8
HET SAR G 809 5
HET MVA H 805 8
HET MVA H 807 8
HET MVA H 808 8
HET SAR H 809 5
HET MVA H 810 8
HET IML H 811 9
HET EDO B 801 4
HET BCT B 802 4
HET EDO C 806 4
HET EDO C 801 4
HET PEG C 802 7
HET NA C 803 1
HET NA C 804 1
HET NA C 805 1
HET PEG D 807 7
HET EDO D 801 4
HET EDO D 802 4
HET EDO D 803 4
HET NA D 804 1
HET NA D 805 1
HET NA D 806 1
HETNAM MVA N-METHYLVALINE
HETNAM SAR SARCOSINE
HETNAM IML N-METHYL-ISOLEUCINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM BCT BICARBONATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 MVA 13(C6 H13 N O2)
FORMUL 5 SAR 3(C3 H7 N O2)
FORMUL 8 IML C7 H15 N O2
FORMUL 9 EDO 6(C2 H6 O2)
FORMUL 10 BCT C H O3 1-
FORMUL 13 PEG 2(C4 H10 O3)
FORMUL 14 NA 6(NA 1+)
FORMUL 24 HOH *53(H2 O)
HELIX 1 AA1 TYR A 36 VAL A 41 5 6
HELIX 2 AA2 PRO A 42 ASP A 45 5 4
HELIX 3 AA3 SER A 46 GLU A 66 1 21
HELIX 4 AA4 ASN A 67 ASN A 82 1 16
HELIX 5 AA5 GLU A 118 VAL A 122 5 5
HELIX 6 AA6 ASN A 135 LEU A 139 5 5
HELIX 7 AA7 ASP A 247 ASP A 251 5 5
HELIX 8 AA8 HIS A 296 ASN A 298 5 3
HELIX 9 AA9 HIS A 347 GLU A 350 5 4
HELIX 10 AB1 ASN A 457 ASP A 459 5 3
HELIX 11 AB2 SER A 511 TYR A 521 1 11
HELIX 12 AB3 GLU A 538 GLU A 543 1 6
HELIX 13 AB4 GLY A 544 ASP A 547 5 4
HELIX 14 AB5 LYS A 548 ASN A 566 1 19
HELIX 15 AB6 ASN A 581 ALA A 593 1 13
HELIX 16 AB7 PRO A 594 TYR A 597 5 4
HELIX 17 AB8 ARG A 611 PHE A 615 5 5
HELIX 18 AB9 PHE A 617 SER A 620 5 4
HELIX 19 AC1 TRP A 621 GLY A 626 1 6
HELIX 20 AC2 ASP A 630 SER A 641 1 12
HELIX 21 AC3 PRO A 642 ASN A 645 5 4
HELIX 22 AC4 PRO A 670 PHE A 684 1 15
HELIX 23 AC5 SER A 706 GLY A 726 1 21
HELIX 24 AC6 TYR B 36 VAL B 41 5 6
HELIX 25 AC7 PRO B 42 ASP B 45 5 4
HELIX 26 AC8 SER B 46 GLU B 66 1 21
HELIX 27 AC9 ASN B 67 ASN B 82 1 16
HELIX 28 AD1 GLU B 118 VAL B 122 5 5
HELIX 29 AD2 ASN B 135 LEU B 139 5 5
HELIX 30 AD3 ASP B 247 ASP B 251 5 5
HELIX 31 AD4 HIS B 347 GLU B 350 5 4
HELIX 32 AD5 ASN B 457 ASP B 459 5 3
HELIX 33 AD6 SER B 511 TYR B 521 1 11
HELIX 34 AD7 GLU B 538 GLU B 543 1 6
HELIX 35 AD8 GLY B 544 LYS B 548 5 5
HELIX 36 AD9 LYS B 549 ASN B 566 1 18
HELIX 37 AE1 ASN B 581 ALA B 593 1 13
HELIX 38 AE2 PRO B 594 TYR B 597 5 4
HELIX 39 AE3 ARG B 611 PHE B 615 5 5
HELIX 40 AE4 PHE B 617 SER B 620 5 4
HELIX 41 AE5 TRP B 621 GLY B 626 1 6
HELIX 42 AE6 ASP B 630 SER B 641 1 12
HELIX 43 AE7 PRO B 642 ASN B 645 5 4
HELIX 44 AE8 PRO B 648 THR B 652 5 5
HELIX 45 AE9 PRO B 670 PHE B 684 1 15
HELIX 46 AF1 SER B 706 GLY B 726 1 21
HELIX 47 AF2 TYR C 36 VAL C 41 5 6
HELIX 48 AF3 PRO C 42 ASP C 45 5 4
HELIX 49 AF4 SER C 46 GLU C 66 1 21
HELIX 50 AF5 ASN C 67 ASN C 82 1 16
HELIX 51 AF6 GLU C 118 VAL C 122 5 5
HELIX 52 AF7 ASN C 135 LEU C 139 5 5
HELIX 53 AF8 ASP C 247 ASP C 251 5 5
HELIX 54 AF9 HIS C 296 ASN C 298 5 3
HELIX 55 AG1 HIS C 347 GLU C 350 5 4
HELIX 56 AG2 ASN C 457 ASP C 459 5 3
HELIX 57 AG3 SER C 511 TYR C 521 1 11
HELIX 58 AG4 GLU C 538 GLU C 543 1 6
HELIX 59 AG5 GLY C 544 ASP C 547 5 4
HELIX 60 AG6 LYS C 548 ASN C 566 1 19
HELIX 61 AG7 ASN C 581 ALA C 593 1 13
HELIX 62 AG8 PRO C 594 TYR C 597 5 4
HELIX 63 AG9 ARG C 611 PHE C 615 5 5
HELIX 64 AH1 PHE C 617 SER C 620 5 4
HELIX 65 AH2 TRP C 621 GLY C 626 1 6
HELIX 66 AH3 ASP C 630 SER C 641 1 12
HELIX 67 AH4 PRO C 642 ASN C 645 5 4
HELIX 68 AH5 PRO C 648 THR C 652 5 5
HELIX 69 AH6 PRO C 670 PHE C 684 1 15
HELIX 70 AH7 SER C 706 GLY C 726 1 21
HELIX 71 AH8 TYR D 36 VAL D 41 5 6
HELIX 72 AH9 PRO D 42 ASP D 45 5 4
HELIX 73 AI1 SER D 46 GLU D 66 1 21
HELIX 74 AI2 ASN D 67 ASN D 82 1 16
HELIX 75 AI3 GLU D 118 VAL D 122 5 5
HELIX 76 AI4 ASN D 135 LEU D 139 5 5
HELIX 77 AI5 ASP D 247 ASP D 251 5 5
HELIX 78 AI6 HIS D 347 GLU D 350 5 4
HELIX 79 AI7 ASN D 457 ASP D 459 5 3
HELIX 80 AI8 SER D 511 TYR D 521 1 11
HELIX 81 AI9 GLY D 537 GLU D 543 1 7
HELIX 82 AJ1 GLY D 544 LYS D 548 5 5
HELIX 83 AJ2 LYS D 549 ASN D 566 1 18
HELIX 84 AJ3 ASN D 581 ALA D 593 1 13
HELIX 85 AJ4 PRO D 594 TYR D 597 5 4
HELIX 86 AJ5 ARG D 611 PHE D 615 5 5
HELIX 87 AJ6 PHE D 617 SER D 620 5 4
HELIX 88 AJ7 TRP D 621 GLY D 626 1 6
HELIX 89 AJ8 ASP D 630 SER D 641 1 12
HELIX 90 AJ9 PRO D 642 ASN D 645 5 4
HELIX 91 AK1 PRO D 648 THR D 652 5 5
HELIX 92 AK2 PRO D 670 PHE D 684 1 15
HELIX 93 AK3 SER D 706 GLY D 726 1 21
SHEET 1 AA1 2 ALA A 19 SER A 24 0
SHEET 2 AA1 2 GLY A 28 ARG A 33 -1 O VAL A 32 N ILE A 20
SHEET 1 AA2 3 ARG A 85 PHE A 86 0
SHEET 2 AA2 3 HIS A 96 ASN A 102 -1 O ASN A 102 N ARG A 85
SHEET 3 AA2 3 LYS A 90 PRO A 91 -1 N LYS A 90 O TYR A 98
SHEET 1 AA3 4 ARG A 85 PHE A 86 0
SHEET 2 AA3 4 HIS A 96 ASN A 102 -1 O ASN A 102 N ARG A 85
SHEET 3 AA3 4 SER A 110 ARG A 115 -1 O TYR A 112 N PHE A 99
SHEET 4 AA3 4 GLU A 131 PHE A 134 -1 O PHE A 134 N LEU A 111
SHEET 1 AA4 4 ALA A 146 MET A 152 0
SHEET 2 AA4 4 TYR A 158 SER A 164 -1 O ALA A 160 N VAL A 151
SHEET 3 AA4 4 MET A 171 LYS A 177 -1 O TYR A 174 N TYR A 161
SHEET 4 AA4 4 LYS A 198 VAL A 202 -1 O VAL A 202 N MET A 171
SHEET 1 AA5 4 SER A 208 TRP A 209 0
SHEET 2 AA5 4 GLY A 215 ARG A 220 -1 O PHE A 217 N SER A 208
SHEET 3 AA5 4 MET A 238 ARG A 243 -1 O MET A 238 N ARG A 220
SHEET 4 AA5 4 VAL A 252 HIS A 255 -1 O VAL A 254 N VAL A 239
SHEET 1 AA6 4 ILE A 264 LEU A 269 0
SHEET 2 AA6 4 TYR A 275 SER A 281 -1 O LEU A 277 N GLN A 268
SHEET 3 AA6 4 LEU A 289 ASP A 294 -1 O LEU A 289 N ALA A 280
SHEET 4 AA6 4 LYS A 307 ASN A 308 -1 O LYS A 307 N ILE A 292
SHEET 1 AA7 4 PHE A 317 GLU A 323 0
SHEET 2 AA7 4 LYS A 326 THR A 331 -1 O TYR A 328 N VAL A 320
SHEET 3 AA7 4 LYS A 339 ASP A 344 -1 O ALA A 341 N PHE A 329
SHEET 4 AA7 4 LEU A 352 ILE A 356 -1 O THR A 353 N THR A 342
SHEET 1 AA8 4 PHE A 363 HIS A 370 0
SHEET 2 AA8 4 LYS A 374 ARG A 381 -1 O LEU A 376 N SER A 368
SHEET 3 AA8 4 SER A 384 ASP A 391 -1 O HIS A 388 N LEU A 377
SHEET 4 AA8 4 PRO A 397 ILE A 401 -1 O GLY A 399 N ILE A 389
SHEET 1 AA9 4 GLN A 408 SER A 412 0
SHEET 2 AA9 4 ASP A 419 SER A 425 -1 O PHE A 421 N SER A 412
SHEET 3 AA9 4 THR A 432 THR A 437 -1 O TYR A 434 N VAL A 422
SHEET 4 AA9 4 TYR A 444 ALA A 450 -1 O ARG A 449 N VAL A 433
SHEET 1 AB1 8 PHE A 461 PRO A 469 0
SHEET 2 AB1 8 SER A 475 PRO A 483 -1 O VAL A 476 N TYR A 468
SHEET 3 AB1 8 ILE A 524 PRO A 528 -1 O TYR A 525 N THR A 481
SHEET 4 AB1 8 VAL A 494 TYR A 497 1 N LEU A 495 O ILE A 524
SHEET 5 AB1 8 ILE A 574 GLY A 579 1 O ALA A 575 N VAL A 494
SHEET 6 AB1 8 CYS A 599 ILE A 603 1 O CYS A 599 N ILE A 576
SHEET 7 AB1 8 ALA A 656 ALA A 662 1 O PHE A 660 N THR A 602
SHEET 8 AB1 8 CYS A 691 ASP A 696 1 O ARG A 694 N PHE A 659
SHEET 1 AB2 2 ALA B 19 SER B 24 0
SHEET 2 AB2 2 GLY B 28 ARG B 33 -1 O VAL B 32 N ILE B 20
SHEET 1 AB3 3 ARG B 85 PHE B 86 0
SHEET 2 AB3 3 HIS B 96 ASN B 102 -1 O ASN B 102 N ARG B 85
SHEET 3 AB3 3 LYS B 90 PRO B 91 -1 N LYS B 90 O TYR B 98
SHEET 1 AB4 4 ARG B 85 PHE B 86 0
SHEET 2 AB4 4 HIS B 96 ASN B 102 -1 O ASN B 102 N ARG B 85
SHEET 3 AB4 4 SER B 110 ARG B 115 -1 O TYR B 112 N PHE B 99
SHEET 4 AB4 4 GLU B 131 PHE B 134 -1 O PHE B 134 N LEU B 111
SHEET 1 AB5 4 ALA B 146 MET B 152 0
SHEET 2 AB5 4 TYR B 158 SER B 164 -1 O ALA B 160 N VAL B 151
SHEET 3 AB5 4 MET B 171 LYS B 177 -1 O TYR B 174 N TYR B 161
SHEET 4 AB5 4 LYS B 198 VAL B 202 -1 O ILE B 199 N ILE B 173
SHEET 1 AB6 4 SER B 208 TRP B 209 0
SHEET 2 AB6 4 GLY B 215 ARG B 220 -1 O PHE B 217 N SER B 208
SHEET 3 AB6 4 MET B 238 ARG B 243 -1 O MET B 238 N ARG B 220
SHEET 4 AB6 4 VAL B 252 HIS B 255 -1 O VAL B 254 N VAL B 239
SHEET 1 AB7 4 ILE B 264 LEU B 269 0
SHEET 2 AB7 4 TYR B 275 SER B 281 -1 O LEU B 277 N GLN B 268
SHEET 3 AB7 4 LEU B 289 ASP B 294 -1 O LEU B 289 N ALA B 280
SHEET 4 AB7 4 LYS B 307 ASN B 308 -1 O LYS B 307 N ILE B 292
SHEET 1 AB8 4 PHE B 317 GLU B 323 0
SHEET 2 AB8 4 LYS B 326 THR B 331 -1 O TYR B 328 N VAL B 320
SHEET 3 AB8 4 LYS B 339 ASP B 344 -1 O ALA B 341 N PHE B 329
SHEET 4 AB8 4 LEU B 352 ILE B 356 -1 O THR B 353 N THR B 342
SHEET 1 AB9 4 PHE B 363 HIS B 370 0
SHEET 2 AB9 4 LYS B 374 ARG B 381 -1 O LEU B 376 N SER B 368
SHEET 3 AB9 4 SER B 384 ASP B 391 -1 O ARG B 390 N LEU B 375
SHEET 4 AB9 4 PRO B 397 ILE B 401 -1 O GLY B 399 N ILE B 389
SHEET 1 AC1 4 GLN B 408 SER B 412 0
SHEET 2 AC1 4 ASP B 419 SER B 425 -1 O PHE B 421 N SER B 412
SHEET 3 AC1 4 THR B 432 THR B 437 -1 O TYR B 434 N VAL B 422
SHEET 4 AC1 4 TYR B 444 ALA B 450 -1 O ARG B 449 N VAL B 433
SHEET 1 AC2 8 PHE B 461 PRO B 469 0
SHEET 2 AC2 8 SER B 475 PRO B 483 -1 O VAL B 476 N TYR B 468
SHEET 3 AC2 8 ILE B 524 PRO B 528 -1 O TYR B 525 N THR B 481
SHEET 4 AC2 8 VAL B 494 TYR B 497 1 N LEU B 495 O ILE B 524
SHEET 5 AC2 8 ILE B 574 GLY B 579 1 O ALA B 575 N VAL B 494
SHEET 6 AC2 8 CYS B 599 ILE B 603 1 O CYS B 599 N ILE B 576
SHEET 7 AC2 8 ALA B 656 ALA B 662 1 O PHE B 660 N THR B 602
SHEET 8 AC2 8 CYS B 691 ASP B 696 1 O ARG B 694 N PHE B 659
SHEET 1 AC3 2 ALA C 19 SER C 24 0
SHEET 2 AC3 2 GLY C 28 ARG C 33 -1 O VAL C 30 N TYR C 22
SHEET 1 AC4 3 ARG C 85 PHE C 86 0
SHEET 2 AC4 3 HIS C 96 ASN C 102 -1 O ASN C 102 N ARG C 85
SHEET 3 AC4 3 LYS C 90 PRO C 91 -1 N LYS C 90 O TYR C 98
SHEET 1 AC5 4 ARG C 85 PHE C 86 0
SHEET 2 AC5 4 HIS C 96 ASN C 102 -1 O ASN C 102 N ARG C 85
SHEET 3 AC5 4 SER C 110 ARG C 115 -1 O TYR C 112 N PHE C 99
SHEET 4 AC5 4 GLU C 131 PHE C 134 -1 O PHE C 134 N LEU C 111
SHEET 1 AC6 4 GLY C 149 MET C 152 0
SHEET 2 AC6 4 TYR C 158 GLY C 162 -1 O ALA C 160 N VAL C 151
SHEET 3 AC6 4 MET C 171 LYS C 177 -1 O TYR C 174 N TYR C 161
SHEET 4 AC6 4 LYS C 198 VAL C 202 -1 O VAL C 202 N MET C 171
SHEET 1 AC7 4 SER C 208 TRP C 209 0
SHEET 2 AC7 4 GLY C 215 ARG C 220 -1 O PHE C 217 N SER C 208
SHEET 3 AC7 4 MET C 238 ARG C 243 -1 O MET C 238 N ARG C 220
SHEET 4 AC7 4 VAL C 252 HIS C 255 -1 O VAL C 254 N VAL C 239
SHEET 1 AC8 4 ILE C 264 LEU C 269 0
SHEET 2 AC8 4 TYR C 275 SER C 281 -1 O LEU C 277 N GLN C 268
SHEET 3 AC8 4 LEU C 289 ASP C 294 -1 O LEU C 289 N ALA C 280
SHEET 4 AC8 4 LYS C 307 HIS C 310 -1 O LYS C 307 N ILE C 292
SHEET 1 AC9 4 PHE C 317 GLU C 323 0
SHEET 2 AC9 4 LYS C 326 THR C 331 -1 O TYR C 328 N VAL C 320
SHEET 3 AC9 4 LYS C 339 ASP C 344 -1 O ALA C 341 N PHE C 329
SHEET 4 AC9 4 LEU C 352 ILE C 356 -1 O THR C 353 N THR C 342
SHEET 1 AD1 4 PHE C 363 HIS C 370 0
SHEET 2 AD1 4 LYS C 374 ARG C 381 -1 O LEU C 376 N SER C 368
SHEET 3 AD1 4 SER C 384 ASP C 391 -1 O HIS C 388 N LEU C 377
SHEET 4 AD1 4 PRO C 397 ILE C 401 -1 O GLY C 399 N ILE C 389
SHEET 1 AD2 4 GLN C 408 SER C 412 0
SHEET 2 AD2 4 ASP C 419 SER C 425 -1 O SER C 425 N GLN C 408
SHEET 3 AD2 4 THR C 432 THR C 437 -1 O TYR C 434 N VAL C 422
SHEET 4 AD2 4 TYR C 444 ALA C 450 -1 O ARG C 449 N VAL C 433
SHEET 1 AD3 8 PHE C 461 PRO C 469 0
SHEET 2 AD3 8 SER C 475 PRO C 483 -1 O VAL C 476 N TYR C 468
SHEET 3 AD3 8 ILE C 524 PRO C 528 -1 O TYR C 525 N THR C 481
SHEET 4 AD3 8 VAL C 494 TYR C 497 1 N LEU C 495 O ILE C 524
SHEET 5 AD3 8 ILE C 574 GLY C 579 1 O ALA C 575 N VAL C 494
SHEET 6 AD3 8 CYS C 599 ILE C 603 1 O CYS C 599 N ILE C 576
SHEET 7 AD3 8 ALA C 656 ALA C 662 1 O PHE C 660 N THR C 602
SHEET 8 AD3 8 CYS C 691 ASP C 696 1 O ARG C 694 N PHE C 659
SHEET 1 AD4 2 ALA D 19 SER D 24 0
SHEET 2 AD4 2 GLY D 28 ARG D 33 -1 O VAL D 30 N TYR D 22
SHEET 1 AD5 3 ARG D 85 PHE D 86 0
SHEET 2 AD5 3 HIS D 96 ASN D 102 -1 O ASN D 102 N ARG D 85
SHEET 3 AD5 3 LYS D 90 PRO D 91 -1 N LYS D 90 O TYR D 98
SHEET 1 AD6 4 ARG D 85 PHE D 86 0
SHEET 2 AD6 4 HIS D 96 ASN D 102 -1 O ASN D 102 N ARG D 85
SHEET 3 AD6 4 SER D 110 ARG D 115 -1 O TYR D 112 N PHE D 99
SHEET 4 AD6 4 GLU D 131 PHE D 134 -1 O PHE D 134 N LEU D 111
SHEET 1 AD7 4 ALA D 146 MET D 152 0
SHEET 2 AD7 4 TYR D 158 SER D 164 -1 O ALA D 160 N VAL D 151
SHEET 3 AD7 4 MET D 171 LYS D 177 -1 O TYR D 174 N TYR D 161
SHEET 4 AD7 4 LYS D 198 VAL D 202 -1 O ILE D 199 N ILE D 173
SHEET 1 AD8 4 SER D 208 TRP D 209 0
SHEET 2 AD8 4 GLY D 215 ARG D 220 -1 O PHE D 217 N SER D 208
SHEET 3 AD8 4 MET D 238 ARG D 243 -1 O MET D 238 N ARG D 220
SHEET 4 AD8 4 VAL D 252 HIS D 255 -1 O VAL D 254 N VAL D 239
SHEET 1 AD9 4 ILE D 264 LEU D 269 0
SHEET 2 AD9 4 TYR D 275 SER D 281 -1 O LEU D 277 N GLN D 268
SHEET 3 AD9 4 LEU D 289 ASP D 294 -1 O LEU D 289 N ALA D 280
SHEET 4 AD9 4 LYS D 307 ASN D 308 -1 O LYS D 307 N ILE D 292
SHEET 1 AE1 4 PHE D 317 GLU D 323 0
SHEET 2 AE1 4 LYS D 326 THR D 331 -1 O TYR D 328 N VAL D 320
SHEET 3 AE1 4 LYS D 339 ASP D 344 -1 O ALA D 341 N PHE D 329
SHEET 4 AE1 4 LEU D 352 ILE D 356 -1 O THR D 353 N THR D 342
SHEET 1 AE2 4 PHE D 363 HIS D 370 0
SHEET 2 AE2 4 LYS D 374 ARG D 381 -1 O LEU D 376 N SER D 368
SHEET 3 AE2 4 SER D 384 ASP D 391 -1 O HIS D 388 N LEU D 377
SHEET 4 AE2 4 PRO D 397 ILE D 401 -1 O GLY D 399 N ILE D 389
SHEET 1 AE3 4 GLN D 408 SER D 412 0
SHEET 2 AE3 4 ASP D 419 SER D 425 -1 O PHE D 421 N SER D 412
SHEET 3 AE3 4 THR D 432 THR D 437 -1 O TYR D 434 N VAL D 422
SHEET 4 AE3 4 TYR D 444 ALA D 450 -1 O ARG D 449 N VAL D 433
SHEET 1 AE4 8 PHE D 461 PRO D 469 0
SHEET 2 AE4 8 SER D 475 PRO D 483 -1 O VAL D 476 N TYR D 468
SHEET 3 AE4 8 ILE D 524 PRO D 528 -1 O TYR D 525 N THR D 481
SHEET 4 AE4 8 VAL D 494 TYR D 497 1 N LEU D 495 O ILE D 524
SHEET 5 AE4 8 ILE D 574 GLY D 579 1 O ALA D 575 N VAL D 494
SHEET 6 AE4 8 CYS D 599 ILE D 603 1 O CYS D 599 N ILE D 576
SHEET 7 AE4 8 ALA D 656 ALA D 662 1 O PHE D 660 N THR D 602
SHEET 8 AE4 8 CYS D 691 ASP D 696 1 O ARG D 694 N PHE D 659
LINK C MVA E 805 N ILE E 806 1555 1555 1.34
LINK C ILE E 806 N MVA E 807 1555 1555 1.40
LINK C MVA E 807 N MVA E 808 1555 1555 1.37
LINK C MVA E 808 N SAR E 809 1555 1555 1.35
LINK C TRP F 804 N MVA F 805 1555 1555 1.34
LINK C MVA F 805 N ILE F 806 1555 1555 1.34
LINK C ILE F 806 N MVA F 807 1555 1555 1.37
LINK C MVA F 807 N MVA F 808 1555 1555 1.36
LINK C MVA G 805 N ILE G 806 1555 1555 1.34
LINK C ILE G 806 N MVA G 807 1555 1555 1.38
LINK C MVA G 807 N MVA G 808 1555 1555 1.37
LINK C MVA G 808 N SAR G 809 1555 1555 1.35
LINK C TRP H 804 N MVA H 805 1555 1555 1.34
LINK C MVA H 805 N ILE H 806 1555 1555 1.34
LINK C ILE H 806 N MVA H 807 1555 1555 1.38
LINK C MVA H 807 N MVA H 808 1555 1555 1.35
LINK C MVA H 808 N SAR H 809 1555 1555 1.36
LINK C SAR H 809 N MVA H 810 1555 1555 1.33
LINK C MVA H 810 N IML H 811 1555 1555 1.41
LINK O GLN C 288 NA NA C 803 1555 1555 3.09
LINK O ASP C 311 NA NA C 803 1555 1555 2.63
LINK O TYR C 499 NA NA C 804 1555 1555 2.53
LINK O GLY C 500 NA NA C 804 1555 1555 2.95
LINK O LEU C 546 NA NA C 805 1555 1555 2.47
LINK O ASN C 581 NA NA C 804 1555 1555 2.92
LINK O TYR C 625 NA NA C 805 1555 1555 2.56
LINK OH TYR C 640 NA NA C 805 1555 1555 2.51
LINK OG1 THR D 481 NA NA D 806 1555 1555 2.87
LINK O TYR D 525 NA NA D 806 1555 1555 2.87
LINK O VAL D 600 NA NA D 805 1555 1555 2.92
LINK OG1 THR D 602 NA NA D 805 1555 1555 3.03
LINK O LEU D 658 NA NA D 805 1555 1555 3.02
CISPEP 1 GLY A 7 PRO A 8 0 -8.07
CISPEP 2 GLY A 687 PRO A 688 0 5.62
CISPEP 3 GLY B 7 PRO B 8 0 -5.87
CISPEP 4 GLY B 687 PRO B 688 0 3.79
CISPEP 5 GLY C 7 PRO C 8 0 -8.70
CISPEP 6 GLY C 687 PRO C 688 0 5.51
CISPEP 7 GLY D 7 PRO D 8 0 -6.30
CISPEP 8 GLY D 687 PRO D 688 0 4.91
CISPEP 9 TRP F 804 MVA F 805 0 -24.54
CISPEP 10 TRP H 804 MVA H 805 0 -24.05
CRYST1 70.220 106.180 114.790 113.04 101.67 93.24 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014241 0.000806 0.003593 0.00000
SCALE2 0.000000 0.009433 0.004265 0.00000
SCALE3 0.000000 0.000000 0.009762 0.00000
TER 5770 THR A 731
TER 11521 GLN B 730
TER 17189 THR C 731
TER 22952 GLN D 732
TER 22990 SAR E 809
TER 23055 MVA F 808
TER 23093 SAR G 809
TER 23184 IML H 811
MASTER 635 0 32 93 164 0 0 623277 8 198 240
END |