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HEADER HYDROLASE 04-MAY-21 7MP4
TITLE CRYSTAL STRUCTURE OF EPIPHYAS POSTVITTANA ANTENNAL CARBOXYLESTERASE 24
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE-24;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EPIPHYAS POSTVITTANA;
SOURCE 3 ORGANISM_TAXID: 65032;
SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 1 BOLD-2017;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 2449148;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS ESTERASE ODORANT DEGRADING ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HAMIAUX,C.CARRAHER
REVDAT 1 11-MAY-22 7MP4 0
JRNL AUTH C.HAMIAUX,C.CARRAGHER,C.LOFSTEDT,J.A.CORCORAN
JRNL TITL CRYSTAL STRUCTURE OF EPIPHYAS POSTVITTANA ANTENNAL
JRNL TITL 2 CARBOXYLESTERASE 24
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.43 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) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 179626
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9515
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) : 2.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13187
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 683
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 33176
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 488
REMARK 3 SOLVENT ATOMS : 1198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : -0.42000
REMARK 3 B12 (A**2) : -0.31000
REMARK 3 B13 (A**2) : -0.60000
REMARK 3 B23 (A**2) : 0.32000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.418
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.201
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.344
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 34680 ; 0.004 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 31472 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 47296 ; 1.350 ; 1.650
REMARK 3 BOND ANGLES OTHERS (DEGREES): 72672 ; 1.154 ; 1.572
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4264 ; 7.174 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1704 ;31.907 ;22.300
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5208 ;14.891 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 176 ;14.822 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4472 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 39488 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 8168 ; 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 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 539 4
REMARK 3 1 B 1 B 539 4
REMARK 3 1 C 1 C 539 4
REMARK 3 1 D 1 D 539 4
REMARK 3 1 E 1 E 539 4
REMARK 3 1 F 1 F 539 4
REMARK 3 1 G 1 G 539 4
REMARK 3 1 H 1 H 539 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 8143 ; 0.430 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 8143 ; 0.390 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 8143 ; 0.400 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 8143 ; 0.410 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 E (A): 8143 ; 0.440 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 F (A): 8143 ; 0.390 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 G (A): 8143 ; 0.410 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 H (A): 8143 ; 0.410 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 8143 ; 4.220 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 8143 ; 6.690 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 8143 ; 1.990 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 8143 ; 1.920 ; 2.000
REMARK 3 MEDIUM THERMAL 1 E (A**2): 8143 ; 3.810 ; 2.000
REMARK 3 MEDIUM THERMAL 1 F (A**2): 8143 ; 2.470 ; 2.000
REMARK 3 MEDIUM THERMAL 1 G (A**2): 8143 ; 1.900 ; 2.000
REMARK 3 MEDIUM THERMAL 1 H (A**2): 8143 ; 2.520 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
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 1 A 534
REMARK 3 ORIGIN FOR THE GROUP (A): -0.368 0.925 0.674
REMARK 3 T TENSOR
REMARK 3 T11: 0.1445 T22: 0.2498
REMARK 3 T33: 0.1838 T12: -0.0805
REMARK 3 T13: 0.1326 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.6917 L22: 0.5810
REMARK 3 L33: 0.5501 L12: 0.0513
REMARK 3 L13: -0.1429 L23: 0.0529
REMARK 3 S TENSOR
REMARK 3 S11: 0.0418 S12: -0.0588 S13: -0.0589
REMARK 3 S21: 0.0004 S22: 0.0033 S23: 0.0408
REMARK 3 S31: 0.0125 S32: 0.0105 S33: -0.0451
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 1 B 534
REMARK 3 ORIGIN FOR THE GROUP (A): 31.340 35.276 -0.489
REMARK 3 T TENSOR
REMARK 3 T11: 0.1175 T22: 0.1839
REMARK 3 T33: 0.3982 T12: -0.0888
REMARK 3 T13: 0.1141 T23: -0.0874
REMARK 3 L TENSOR
REMARK 3 L11: 0.9131 L22: 1.1369
REMARK 3 L33: 0.5547 L12: -0.1707
REMARK 3 L13: -0.0882 L23: 0.3831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0958 S12: 0.0700 S13: 0.2599
REMARK 3 S21: 0.0033 S22: 0.2322 S23: -0.3567
REMARK 3 S31: -0.0121 S32: 0.0434 S33: -0.1364
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 1 C 534
REMARK 3 ORIGIN FOR THE GROUP (A): 21.400 12.436 -57.950
REMARK 3 T TENSOR
REMARK 3 T11: 0.1736 T22: 0.2161
REMARK 3 T33: 0.2796 T12: -0.0839
REMARK 3 T13: 0.1715 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 1.4512 L22: 0.7915
REMARK 3 L33: 0.9050 L12: -0.4707
REMARK 3 L13: 0.2505 L23: -0.5789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: 0.2082 S13: 0.3030
REMARK 3 S21: -0.0213 S22: -0.1520 S23: -0.2200
REMARK 3 S31: 0.1000 S32: 0.0895 S33: 0.1561
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 1 D 534
REMARK 3 ORIGIN FOR THE GROUP (A): -23.765 1.857 -59.191
REMARK 3 T TENSOR
REMARK 3 T11: 0.1696 T22: 0.2271
REMARK 3 T33: 0.1941 T12: -0.0798
REMARK 3 T13: 0.1231 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.0221 L22: 0.8418
REMARK 3 L33: 0.4495 L12: -0.0653
REMARK 3 L13: 0.3677 L23: -0.1557
REMARK 3 S TENSOR
REMARK 3 S11: 0.1431 S12: -0.1847 S13: -0.0797
REMARK 3 S21: -0.0924 S22: -0.0359 S23: 0.1344
REMARK 3 S31: 0.0330 S32: -0.0104 S33: -0.1072
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 534
REMARK 3 ORIGIN FOR THE GROUP (A): -51.178 -17.088 -15.007
REMARK 3 T TENSOR
REMARK 3 T11: 0.1604 T22: 0.2382
REMARK 3 T33: 0.2013 T12: -0.0825
REMARK 3 T13: 0.1506 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.3346 L22: 0.6428
REMARK 3 L33: 0.4474 L12: 0.2850
REMARK 3 L13: 0.4003 L23: -0.0517
REMARK 3 S TENSOR
REMARK 3 S11: -0.0952 S12: 0.1033 S13: 0.1371
REMARK 3 S21: -0.0320 S22: -0.0218 S23: -0.0665
REMARK 3 S31: 0.0211 S32: 0.0126 S33: 0.1170
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 534
REMARK 3 ORIGIN FOR THE GROUP (A): -73.614 -46.266 13.835
REMARK 3 T TENSOR
REMARK 3 T11: 0.1739 T22: 0.4022
REMARK 3 T33: 0.2065 T12: -0.0369
REMARK 3 T13: 0.1620 T23: 0.0845
REMARK 3 L TENSOR
REMARK 3 L11: 1.0711 L22: 0.9019
REMARK 3 L33: 1.0521 L12: -0.4299
REMARK 3 L13: 0.3165 L23: -0.7645
REMARK 3 S TENSOR
REMARK 3 S11: -0.1892 S12: -0.2729 S13: -0.1831
REMARK 3 S21: 0.0097 S22: 0.3851 S23: 0.1079
REMARK 3 S31: -0.0240 S32: -0.3847 S33: -0.1958
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 534
REMARK 3 ORIGIN FOR THE GROUP (A): -99.166 -46.659 -45.124
REMARK 3 T TENSOR
REMARK 3 T11: 0.1582 T22: 0.2445
REMARK 3 T33: 0.1778 T12: -0.0683
REMARK 3 T13: 0.1466 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.6452 L22: 0.6651
REMARK 3 L33: 0.7608 L12: 0.1130
REMARK 3 L13: -0.1148 L23: 0.2490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0142 S12: -0.0354 S13: -0.0642
REMARK 3 S21: -0.0127 S22: -0.0636 S23: 0.0774
REMARK 3 S31: -0.0552 S32: -0.1352 S33: 0.0494
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 534
REMARK 3 ORIGIN FOR THE GROUP (A): -61.671 -39.822 -72.238
REMARK 3 T TENSOR
REMARK 3 T11: 0.2394 T22: 0.2262
REMARK 3 T33: 0.1892 T12: -0.0471
REMARK 3 T13: 0.1892 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.3832 L22: 1.0599
REMARK 3 L33: 0.5671 L12: 0.2119
REMARK 3 L13: -0.1982 L23: -0.1127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0732 S12: -0.0529 S13: -0.0320
REMARK 3 S21: -0.1504 S22: -0.1169 S23: -0.0921
REMARK 3 S31: -0.0326 S32: 0.0572 S33: 0.0437
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7MP4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1000256592.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953646
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 189143
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430
REMARK 200 RESOLUTION RANGE LOW (A) : 48.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: 5THM
REMARK 200
REMARK 200 REMARK: LONG ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 7.5 25% SOKALAN CP5,
REMARK 280 VAPOR DIFFUSION, HANGING 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, 5, 6, 7, 8
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, M
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, N
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, O
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, P
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 ILE A 535
REMARK 465 ARG A 536
REMARK 465 ASP A 537
REMARK 465 GLU A 538
REMARK 465 LEU A 539
REMARK 465 GLU A 540
REMARK 465 ASN A 541
REMARK 465 LEU A 542
REMARK 465 TYR A 543
REMARK 465 PHE A 544
REMARK 465 GLN A 545
REMARK 465 GLY A 546
REMARK 465 HIS A 547
REMARK 465 HIS A 548
REMARK 465 HIS A 549
REMARK 465 HIS A 550
REMARK 465 HIS A 551
REMARK 465 HIS A 552
REMARK 465 HIS A 553
REMARK 465 HIS A 554
REMARK 465 HIS A 555
REMARK 465 HIS A 556
REMARK 465 ILE B 535
REMARK 465 ARG B 536
REMARK 465 ASP B 537
REMARK 465 GLU B 538
REMARK 465 LEU B 539
REMARK 465 GLU B 540
REMARK 465 ASN B 541
REMARK 465 LEU B 542
REMARK 465 TYR B 543
REMARK 465 PHE B 544
REMARK 465 GLN B 545
REMARK 465 GLY B 546
REMARK 465 HIS B 547
REMARK 465 HIS B 548
REMARK 465 HIS B 549
REMARK 465 HIS B 550
REMARK 465 HIS B 551
REMARK 465 HIS B 552
REMARK 465 HIS B 553
REMARK 465 HIS B 554
REMARK 465 HIS B 555
REMARK 465 HIS B 556
REMARK 465 ILE C 535
REMARK 465 ARG C 536
REMARK 465 ASP C 537
REMARK 465 GLU C 538
REMARK 465 LEU C 539
REMARK 465 GLU C 540
REMARK 465 ASN C 541
REMARK 465 LEU C 542
REMARK 465 TYR C 543
REMARK 465 PHE C 544
REMARK 465 GLN C 545
REMARK 465 GLY C 546
REMARK 465 HIS C 547
REMARK 465 HIS C 548
REMARK 465 HIS C 549
REMARK 465 HIS C 550
REMARK 465 HIS C 551
REMARK 465 HIS C 552
REMARK 465 HIS C 553
REMARK 465 HIS C 554
REMARK 465 HIS C 555
REMARK 465 HIS C 556
REMARK 465 ILE D 535
REMARK 465 ARG D 536
REMARK 465 ASP D 537
REMARK 465 GLU D 538
REMARK 465 LEU D 539
REMARK 465 GLU D 540
REMARK 465 ASN D 541
REMARK 465 LEU D 542
REMARK 465 TYR D 543
REMARK 465 PHE D 544
REMARK 465 GLN D 545
REMARK 465 GLY D 546
REMARK 465 HIS D 547
REMARK 465 HIS D 548
REMARK 465 HIS D 549
REMARK 465 HIS D 550
REMARK 465 HIS D 551
REMARK 465 HIS D 552
REMARK 465 HIS D 553
REMARK 465 HIS D 554
REMARK 465 HIS D 555
REMARK 465 HIS D 556
REMARK 465 ILE E 535
REMARK 465 ARG E 536
REMARK 465 ASP E 537
REMARK 465 GLU E 538
REMARK 465 LEU E 539
REMARK 465 GLU E 540
REMARK 465 ASN E 541
REMARK 465 LEU E 542
REMARK 465 TYR E 543
REMARK 465 PHE E 544
REMARK 465 GLN E 545
REMARK 465 GLY E 546
REMARK 465 HIS E 547
REMARK 465 HIS E 548
REMARK 465 HIS E 549
REMARK 465 HIS E 550
REMARK 465 HIS E 551
REMARK 465 HIS E 552
REMARK 465 HIS E 553
REMARK 465 HIS E 554
REMARK 465 HIS E 555
REMARK 465 HIS E 556
REMARK 465 ILE F 535
REMARK 465 ARG F 536
REMARK 465 ASP F 537
REMARK 465 GLU F 538
REMARK 465 LEU F 539
REMARK 465 GLU F 540
REMARK 465 ASN F 541
REMARK 465 LEU F 542
REMARK 465 TYR F 543
REMARK 465 PHE F 544
REMARK 465 GLN F 545
REMARK 465 GLY F 546
REMARK 465 HIS F 547
REMARK 465 HIS F 548
REMARK 465 HIS F 549
REMARK 465 HIS F 550
REMARK 465 HIS F 551
REMARK 465 HIS F 552
REMARK 465 HIS F 553
REMARK 465 HIS F 554
REMARK 465 HIS F 555
REMARK 465 HIS F 556
REMARK 465 ILE G 535
REMARK 465 ARG G 536
REMARK 465 ASP G 537
REMARK 465 GLU G 538
REMARK 465 LEU G 539
REMARK 465 GLU G 540
REMARK 465 ASN G 541
REMARK 465 LEU G 542
REMARK 465 TYR G 543
REMARK 465 PHE G 544
REMARK 465 GLN G 545
REMARK 465 GLY G 546
REMARK 465 HIS G 547
REMARK 465 HIS G 548
REMARK 465 HIS G 549
REMARK 465 HIS G 550
REMARK 465 HIS G 551
REMARK 465 HIS G 552
REMARK 465 HIS G 553
REMARK 465 HIS G 554
REMARK 465 HIS G 555
REMARK 465 HIS G 556
REMARK 465 ILE H 535
REMARK 465 ARG H 536
REMARK 465 ASP H 537
REMARK 465 GLU H 538
REMARK 465 LEU H 539
REMARK 465 GLU H 540
REMARK 465 ASN H 541
REMARK 465 LEU H 542
REMARK 465 TYR H 543
REMARK 465 PHE H 544
REMARK 465 GLN H 545
REMARK 465 GLY H 546
REMARK 465 HIS H 547
REMARK 465 HIS H 548
REMARK 465 HIS H 549
REMARK 465 HIS H 550
REMARK 465 HIS H 551
REMARK 465 HIS H 552
REMARK 465 HIS H 553
REMARK 465 HIS H 554
REMARK 465 HIS H 555
REMARK 465 HIS H 556
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 O HOH G 746 O HOH G 755 2.16
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 PHE A 43 -14.58 82.56
REMARK 500 CYS A 81 -3.38 -145.57
REMARK 500 ALA A 112 147.70 -170.47
REMARK 500 PHE A 140 21.03 -141.54
REMARK 500 ALA A 148 84.75 -158.61
REMARK 500 SER A 184 -115.62 60.63
REMARK 500 PRO A 267 131.34 -39.49
REMARK 500 PRO A 277 150.71 -43.48
REMARK 500 SER A 310 149.84 -171.39
REMARK 500 PHE A 390 -63.67 -126.33
REMARK 500 HIS A 437 123.80 -35.73
REMARK 500 ALA A 438 2.79 83.60
REMARK 500 THR A 473 -78.01 -119.25
REMARK 500 ASN A 529 -112.44 48.10
REMARK 500 PHE B 43 -16.94 79.32
REMARK 500 CYS B 81 -6.05 -146.36
REMARK 500 PHE B 140 11.76 -142.11
REMARK 500 ALA B 148 88.12 -167.66
REMARK 500 SER B 184 -118.74 56.31
REMARK 500 PRO B 267 133.36 -38.47
REMARK 500 PHE B 390 -60.37 -128.71
REMARK 500 HIS B 437 122.97 -27.22
REMARK 500 ALA B 438 -2.28 82.80
REMARK 500 ASN B 529 -105.83 60.69
REMARK 500 PHE C 43 -16.95 74.53
REMARK 500 CYS C 81 -1.88 -150.57
REMARK 500 ALA C 112 144.13 -173.65
REMARK 500 ALA C 148 89.16 -169.60
REMARK 500 SER C 184 -118.67 59.74
REMARK 500 PRO C 267 126.44 -36.68
REMARK 500 PRO C 277 150.83 -46.91
REMARK 500 PHE C 390 -56.95 -127.74
REMARK 500 HIS C 437 121.93 -22.16
REMARK 500 ALA C 438 -0.77 79.50
REMARK 500 THR C 473 -81.30 -116.23
REMARK 500 ASP C 514 54.88 -148.04
REMARK 500 ASN C 529 -110.40 51.58
REMARK 500 PHE D 43 -0.47 76.37
REMARK 500 ALA D 148 82.81 -163.91
REMARK 500 SER D 184 -119.82 62.07
REMARK 500 GLU D 314 50.17 -118.79
REMARK 500 ASN D 370 -4.71 72.72
REMARK 500 PHE D 390 -53.70 -126.28
REMARK 500 HIS D 437 124.61 -27.25
REMARK 500 ALA D 438 -1.08 83.28
REMARK 500 THR D 473 -67.13 -123.15
REMARK 500 ASP D 514 64.27 -159.96
REMARK 500 ASN D 529 -123.06 49.19
REMARK 500 PHE E 43 -13.98 74.13
REMARK 500 CYS E 81 -1.07 -145.56
REMARK 500
REMARK 500 THIS ENTRY HAS 94 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 SER B 436 HIS B 437 145.43
REMARK 500 SER H 436 HIS H 437 145.84
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7MP4 A 1 556 PDB 7MP4 7MP4 1 556
DBREF 7MP4 B 1 556 PDB 7MP4 7MP4 1 556
DBREF 7MP4 C 1 556 PDB 7MP4 7MP4 1 556
DBREF 7MP4 D 1 556 PDB 7MP4 7MP4 1 556
DBREF 7MP4 E 1 556 PDB 7MP4 7MP4 1 556
DBREF 7MP4 F 1 556 PDB 7MP4 7MP4 1 556
DBREF 7MP4 G 1 556 PDB 7MP4 7MP4 1 556
DBREF 7MP4 H 1 556 PDB 7MP4 7MP4 1 556
SEQRES 1 A 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 A 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 A 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 A 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 A 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 A 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 A 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 A 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 A 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 A 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 A 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 A 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 A 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 A 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 A 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 A 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 A 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 A 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 A 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 A 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 A 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 A 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 A 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 A 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 A 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 A 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 A 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 A 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 A 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 A 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 A 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 A 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 A 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 A 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 A 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 A 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 A 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 A 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 A 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 A 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 A 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 A 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 A 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 B 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 B 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 B 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 B 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 B 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 B 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 B 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 B 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 B 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 B 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 B 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 B 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 B 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 B 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 B 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 B 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 B 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 B 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 B 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 B 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 B 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 B 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 B 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 B 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 B 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 B 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 B 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 B 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 B 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 B 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 B 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 B 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 B 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 B 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 B 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 B 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 B 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 B 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 B 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 B 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 B 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 B 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 C 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 C 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 C 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 C 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 C 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 C 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 C 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 C 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 C 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 C 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 C 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 C 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 C 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 C 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 C 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 C 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 C 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 C 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 C 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 C 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 C 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 C 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 C 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 C 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 C 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 C 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 C 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 C 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 C 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 C 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 C 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 C 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 C 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 C 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 C 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 C 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 C 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 C 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 C 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 C 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 C 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 C 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 D 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 D 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 D 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 D 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 D 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 D 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 D 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 D 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 D 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 D 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 D 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 D 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 D 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 D 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 D 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 D 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 D 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 D 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 D 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 D 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 D 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 D 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 D 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 D 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 D 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 D 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 D 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 D 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 D 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 D 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 D 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 D 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 D 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 D 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 D 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 D 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 D 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 D 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 D 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 D 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 D 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 D 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 E 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 E 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 E 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 E 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 E 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 E 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 E 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 E 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 E 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 E 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 E 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 E 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 E 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 E 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 E 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 E 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 E 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 E 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 E 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 E 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 E 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 E 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 E 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 E 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 E 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 E 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 E 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 E 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 E 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 E 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 E 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 E 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 E 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 E 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 E 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 E 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 E 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 E 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 E 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 E 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 E 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 E 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 E 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 F 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 F 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 F 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 F 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 F 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 F 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 F 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 F 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 F 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 F 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 F 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 F 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 F 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 F 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 F 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 F 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 F 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 F 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 F 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 F 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 F 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 F 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 F 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 F 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 F 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 F 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 F 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 F 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 F 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 F 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 F 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 F 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 F 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 F 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 F 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 F 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 F 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 F 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 F 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 F 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 F 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 F 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 F 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 G 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 G 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 G 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 G 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 G 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 G 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 G 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 G 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 G 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 G 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 G 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 G 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 G 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 G 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 G 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 G 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 G 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 G 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 G 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 G 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 G 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 G 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 G 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 G 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 G 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 G 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 G 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 G 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 G 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 G 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 G 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 G 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 G 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 G 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 G 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 G 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 G 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 G 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 G 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 G 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 G 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 G 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 G 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 H 556 SER LYS PRO VAL VAL ARG VAL THR GLN GLY VAL LEU GLN
SEQRES 2 H 556 GLY SER TRP LYS VAL SER THR HIS GLY ARG THR TYR ALA
SEQRES 3 H 556 SER PHE GLU GLY VAL PRO TYR ALA ARG PRO PRO VAL GLY
SEQRES 4 H 556 LYS TYR ARG PHE ARG GLU PRO GLN HIS LEU LYS PRO TRP
SEQRES 5 H 556 ALA GLY VAL TRP ASP ALA SER LYS THR LEU PRO GLN CYS
SEQRES 6 H 556 LEU GLN TRP ASP PRO PHE GLN GLN GLU VAL SER GLY SER
SEQRES 7 H 556 GLU ASN CYS LEU TYR ILE ASN VAL HIS THR PRO LYS LEU
SEQRES 8 H 556 SER ALA GLY ALA SER LEU PRO VAL VAL VAL PHE ILE HIS
SEQRES 9 H 556 GLY GLY ALA PHE MET TYR GLY ALA GLY SER LEU TYR ASP
SEQRES 10 H 556 VAL SER HIS LEU MET ASP ARG ASP VAL VAL ALA VAL THR
SEQRES 11 H 556 PHE ASN TYR ARG LEU GLY PRO LEU GLY PHE LEU SER THR
SEQRES 12 H 556 GLY ASP GLU SER ALA PRO GLY ASN ALA GLY LEU LYS ASP
SEQRES 13 H 556 GLN ALA PHE ALA LEU GLN TRP VAL LYS ASN ASN VAL MET
SEQRES 14 H 556 MET PHE GLY GLY ASN PRO ASP SER VAL THR LEU THR GLY
SEQRES 15 H 556 CYS SER ALA GLY GLY ALA SER VAL HIS TYR HIS TYR LEU
SEQRES 16 H 556 SER PRO LEU SER LYS GLY ASN PHE ALA ARG GLY ILE ALA
SEQRES 17 H 556 PHE SER GLY ALA ALA PHE ALA SER TRP THR HIS ALA VAL
SEQRES 18 H 556 LYS PRO LEU GLN ASN ALA ARG SER LEU ALA ALA ILE VAL
SEQRES 19 H 556 GLY CYS PRO THR GLY THR ASN ARG GLU LEU VAL ASP CYS
SEQRES 20 H 556 LEU LYS TYR ARG PRO ALA GLU VAL VAL VAL GLY ALA GLN
SEQRES 21 H 556 ILE GLU MET LEU GLU PHE PRO TYR GLN GLN MET PHE THR
SEQRES 22 H 556 PRO PHE THR PRO THR VAL GLU PRO GLN GLY THR ARG ASP
SEQRES 23 H 556 ALA PHE LEU THR GLN TYR PRO PHE LEU VAL ALA GLN ALA
SEQRES 24 H 556 GLY GLY MET HIS LYS VAL PRO LEU ILE THR SER VAL THR
SEQRES 25 H 556 SER GLU GLU GLY LEU TYR PRO ALA ALA VAL TYR GLN LYS
SEQRES 26 H 556 SER PRO ASP THR LEU ALA TYR LEU GLU ALA ASN TRP ASP
SEQRES 27 H 556 GLN LEU ALA SER ASN ILE PHE GLU TYR ASN ASP THR LEU
SEQRES 28 H 556 PRO VAL ASN GLN ARG ALA GLY VAL ALA ALA LYS ILE LYS
SEQRES 29 H 556 GLN ARG TYR LEU GLY ASN LYS PRO VAL SER GLN GLU THR
SEQRES 30 H 556 TYR PRO GLN LEU VAL GLN ALA LEU GLY ASP ARG LEU PHE
SEQRES 31 H 556 ALA VAL ASP VAL GLY LYS LEU ALA GLN ILE HIS ALA ARG
SEQRES 32 H 556 HIS SER GLY GLN PRO THR TYR LEU TYR ARG TYR SER PHE
SEQRES 33 H 556 ARG GLY GLU LYS SER LEU SER ASN MET MET ALA SER ASN
SEQRES 34 H 556 ASP LYS ASN TYR GLY VAL SER HIS ALA ASP ASP ILE PHE
SEQRES 35 H 556 HIS ILE PHE LYS PHE PRO SER LEU SER SER THR SER SER
SEQRES 36 H 556 GLU ASP VAL ARG MET THR GLU ALA LEU ILE ASP MET ILE
SEQRES 37 H 556 TYR SER PHE SER THR THR GLY ASN PRO LYS LEU THR ASN
SEQRES 38 H 556 GLU ALA PRO VAL TRP THR PRO VAL THR PRO GLY SER ALA
SEQRES 39 H 556 GLU LEU SER TYR LEU GLU ILE ALA SER PRO SER ARG MET
SEQRES 40 H 556 GLU MET LYS SER SER SER ASP PHE GLY HIS ARG SER PHE
SEQRES 41 H 556 TRP ASP SER LEU GLY PHE VAL GLU ASN GLU ASN TYR ARG
SEQRES 42 H 556 HIS ILE ARG ASP GLU LEU GLU ASN LEU TYR PHE GLN GLY
SEQRES 43 H 556 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET MAN I 4 11
HET MAN I 5 11
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET MAN J 4 11
HET MAN J 5 11
HET NAG K 1 14
HET NAG K 2 14
HET BMA K 3 11
HET MAN K 4 11
HET MAN K 5 11
HET NAG L 1 14
HET NAG L 2 14
HET BMA L 3 11
HET MAN L 4 11
HET MAN L 5 11
HET NAG M 1 14
HET NAG M 2 14
HET BMA M 3 11
HET MAN M 4 11
HET MAN M 5 11
HET NAG N 1 14
HET NAG N 2 14
HET BMA N 3 11
HET MAN N 4 11
HET MAN N 5 11
HET NAG O 1 14
HET NAG O 2 14
HET BMA O 3 11
HET MAN O 4 11
HET MAN O 5 11
HET NAG P 1 14
HET NAG P 2 14
HET BMA P 3 11
HET MAN P 4 11
HET MAN P 5 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 9 NAG 16(C8 H15 N O6)
FORMUL 9 BMA 8(C6 H12 O6)
FORMUL 9 MAN 16(C6 H12 O6)
FORMUL 17 HOH *1198(H2 O)
HELIX 1 AA1 VAL A 38 ARG A 42 5 5
HELIX 2 AA2 ALA A 112 TYR A 116 5 5
HELIX 3 AA3 HIS A 120 ARG A 124 5 5
HELIX 4 AA4 LEU A 135 LEU A 141 1 7
HELIX 5 AA5 ASN A 151 VAL A 168 1 18
HELIX 6 AA6 MET A 169 PHE A 171 5 3
HELIX 7 AA7 SER A 184 SER A 196 1 13
HELIX 8 AA8 PRO A 197 LYS A 200 5 4
HELIX 9 AA9 ALA A 215 HIS A 219 5 5
HELIX 10 AB1 LYS A 222 VAL A 234 1 13
HELIX 11 AB2 THR A 240 ARG A 251 1 12
HELIX 12 AB3 PRO A 252 GLN A 260 1 9
HELIX 13 AB4 ILE A 261 MET A 263 5 3
HELIX 14 AB5 PRO A 267 MET A 271 5 5
HELIX 15 AB6 TYR A 292 ALA A 299 1 8
HELIX 16 AB7 GLY A 316 ALA A 321 1 6
HELIX 17 AB8 VAL A 322 LYS A 325 5 4
HELIX 18 AB9 ASP A 328 ASN A 336 1 9
HELIX 19 AC1 ASN A 336 PHE A 345 1 10
HELIX 20 AC2 PRO A 352 ASN A 354 5 3
HELIX 21 AC3 GLN A 355 GLY A 369 1 15
HELIX 22 AC4 THR A 377 PHE A 390 1 14
HELIX 23 AC5 PHE A 390 SER A 405 1 16
HELIX 24 AC6 SER A 421 SER A 428 1 8
HELIX 25 AC7 ASP A 440 PHE A 445 1 6
HELIX 26 AC8 SER A 454 THR A 474 1 21
HELIX 27 AC9 ASP A 514 GLY A 516 5 3
HELIX 28 AD1 HIS A 517 ASP A 522 1 6
HELIX 29 AD2 GLU A 528 TYR A 532 5 5
HELIX 30 AD3 VAL B 38 ARG B 42 5 5
HELIX 31 AD4 ALA B 112 TYR B 116 5 5
HELIX 32 AD5 HIS B 120 ARG B 124 5 5
HELIX 33 AD6 LEU B 135 LEU B 141 1 7
HELIX 34 AD7 ASN B 151 VAL B 168 1 18
HELIX 35 AD8 MET B 169 PHE B 171 5 3
HELIX 36 AD9 SER B 184 SER B 196 1 13
HELIX 37 AE1 PRO B 197 LYS B 200 5 4
HELIX 38 AE2 ALA B 215 HIS B 219 5 5
HELIX 39 AE3 LYS B 222 VAL B 234 1 13
HELIX 40 AE4 THR B 240 ARG B 251 1 12
HELIX 41 AE5 PRO B 252 GLN B 260 1 9
HELIX 42 AE6 ILE B 261 MET B 263 5 3
HELIX 43 AE7 PRO B 267 MET B 271 5 5
HELIX 44 AE8 TYR B 292 ALA B 299 1 8
HELIX 45 AE9 GLY B 316 ALA B 321 1 6
HELIX 46 AF1 VAL B 322 GLN B 324 5 3
HELIX 47 AF2 ASP B 328 ASN B 336 1 9
HELIX 48 AF3 ASN B 336 PHE B 345 1 10
HELIX 49 AF4 PRO B 352 ASN B 354 5 3
HELIX 50 AF5 GLN B 355 GLY B 369 1 15
HELIX 51 AF6 THR B 377 PHE B 390 1 14
HELIX 52 AF7 PHE B 390 SER B 405 1 16
HELIX 53 AF8 SER B 421 SER B 428 1 8
HELIX 54 AF9 ASP B 440 PHE B 445 1 6
HELIX 55 AG1 SER B 454 THR B 474 1 21
HELIX 56 AG2 HIS B 517 ASP B 522 1 6
HELIX 57 AG3 SER B 523 GLY B 525 5 3
HELIX 58 AG4 GLU B 528 TYR B 532 5 5
HELIX 59 AG5 VAL C 38 ARG C 42 5 5
HELIX 60 AG6 ALA C 112 TYR C 116 5 5
HELIX 61 AG7 HIS C 120 ARG C 124 5 5
HELIX 62 AG8 LEU C 135 LEU C 141 1 7
HELIX 63 AG9 ASN C 151 VAL C 168 1 18
HELIX 64 AH1 MET C 169 PHE C 171 5 3
HELIX 65 AH2 SER C 184 SER C 196 1 13
HELIX 66 AH3 PRO C 197 LYS C 200 5 4
HELIX 67 AH4 ALA C 215 HIS C 219 5 5
HELIX 68 AH5 LYS C 222 VAL C 234 1 13
HELIX 69 AH6 THR C 240 ARG C 251 1 12
HELIX 70 AH7 PRO C 252 ALA C 259 1 8
HELIX 71 AH8 GLN C 260 MET C 263 5 4
HELIX 72 AH9 PRO C 267 MET C 271 5 5
HELIX 73 AI1 TYR C 292 ALA C 299 1 8
HELIX 74 AI2 GLY C 316 ALA C 321 1 6
HELIX 75 AI3 VAL C 322 LYS C 325 5 4
HELIX 76 AI4 ASP C 328 ASN C 336 1 9
HELIX 77 AI5 ASN C 336 PHE C 345 1 10
HELIX 78 AI6 PRO C 352 ASN C 354 5 3
HELIX 79 AI7 GLN C 355 GLY C 369 1 15
HELIX 80 AI8 THR C 377 PHE C 390 1 14
HELIX 81 AI9 PHE C 390 GLY C 406 1 17
HELIX 82 AJ1 SER C 421 SER C 428 1 8
HELIX 83 AJ2 ASP C 440 PHE C 445 1 6
HELIX 84 AJ3 SER C 454 THR C 474 1 21
HELIX 85 AJ4 HIS C 517 ASP C 522 1 6
HELIX 86 AJ5 GLU C 528 TYR C 532 5 5
HELIX 87 AJ6 VAL D 38 ARG D 42 5 5
HELIX 88 AJ7 ALA D 112 TYR D 116 5 5
HELIX 89 AJ8 HIS D 120 ARG D 124 5 5
HELIX 90 AJ9 LEU D 135 LEU D 141 1 7
HELIX 91 AK1 ASN D 151 VAL D 168 1 18
HELIX 92 AK2 MET D 169 PHE D 171 5 3
HELIX 93 AK3 SER D 184 SER D 196 1 13
HELIX 94 AK4 PRO D 197 LYS D 200 5 4
HELIX 95 AK5 ALA D 215 HIS D 219 5 5
HELIX 96 AK6 LYS D 222 VAL D 234 1 13
HELIX 97 AK7 THR D 240 ARG D 251 1 12
HELIX 98 AK8 PRO D 252 GLN D 260 1 9
HELIX 99 AK9 ILE D 261 MET D 263 5 3
HELIX 100 AL1 PRO D 267 MET D 271 5 5
HELIX 101 AL2 TYR D 292 ALA D 299 1 8
HELIX 102 AL3 GLY D 316 ALA D 321 1 6
HELIX 103 AL4 VAL D 322 LYS D 325 5 4
HELIX 104 AL5 ASP D 328 ASN D 336 1 9
HELIX 105 AL6 ASN D 336 PHE D 345 1 10
HELIX 106 AL7 PRO D 352 ASN D 354 5 3
HELIX 107 AL8 GLN D 355 GLY D 369 1 15
HELIX 108 AL9 THR D 377 PHE D 390 1 14
HELIX 109 AM1 PHE D 390 SER D 405 1 16
HELIX 110 AM2 SER D 421 SER D 428 1 8
HELIX 111 AM3 ASP D 440 PHE D 445 1 6
HELIX 112 AM4 SER D 454 THR D 474 1 21
HELIX 113 AM5 HIS D 517 ASP D 522 1 6
HELIX 114 AM6 GLU D 528 TYR D 532 5 5
HELIX 115 AM7 VAL E 38 ARG E 42 5 5
HELIX 116 AM8 ALA E 112 TYR E 116 5 5
HELIX 117 AM9 HIS E 120 ARG E 124 5 5
HELIX 118 AN1 LEU E 135 LEU E 141 1 7
HELIX 119 AN2 ASN E 151 VAL E 168 1 18
HELIX 120 AN3 MET E 169 PHE E 171 5 3
HELIX 121 AN4 SER E 184 SER E 196 1 13
HELIX 122 AN5 PRO E 197 LYS E 200 5 4
HELIX 123 AN6 ALA E 215 HIS E 219 5 5
HELIX 124 AN7 LYS E 222 VAL E 234 1 13
HELIX 125 AN8 THR E 240 ARG E 251 1 12
HELIX 126 AN9 PRO E 252 GLN E 260 1 9
HELIX 127 AO1 ILE E 261 MET E 263 5 3
HELIX 128 AO2 PRO E 267 MET E 271 5 5
HELIX 129 AO3 TYR E 292 ALA E 299 1 8
HELIX 130 AO4 GLY E 316 ALA E 321 1 6
HELIX 131 AO5 VAL E 322 LYS E 325 5 4
HELIX 132 AO6 ASP E 328 ASN E 336 1 9
HELIX 133 AO7 ASN E 336 PHE E 345 1 10
HELIX 134 AO8 PRO E 352 ASN E 354 5 3
HELIX 135 AO9 GLN E 355 GLY E 369 1 15
HELIX 136 AP1 THR E 377 PHE E 390 1 14
HELIX 137 AP2 PHE E 390 SER E 405 1 16
HELIX 138 AP3 LEU E 422 SER E 428 1 7
HELIX 139 AP4 ASP E 440 PHE E 445 1 6
HELIX 140 AP5 SER E 454 THR E 474 1 21
HELIX 141 AP6 HIS E 517 ASP E 522 1 6
HELIX 142 AP7 GLU E 528 TYR E 532 5 5
HELIX 143 AP8 VAL F 38 ARG F 42 5 5
HELIX 144 AP9 ALA F 112 TYR F 116 5 5
HELIX 145 AQ1 HIS F 120 ARG F 124 5 5
HELIX 146 AQ2 LEU F 135 LEU F 141 1 7
HELIX 147 AQ3 ASN F 151 VAL F 168 1 18
HELIX 148 AQ4 MET F 169 PHE F 171 5 3
HELIX 149 AQ5 SER F 184 LEU F 195 1 12
HELIX 150 AQ6 SER F 196 LYS F 200 5 5
HELIX 151 AQ7 ALA F 215 HIS F 219 5 5
HELIX 152 AQ8 LYS F 222 VAL F 234 1 13
HELIX 153 AQ9 THR F 240 ARG F 251 1 12
HELIX 154 AR1 PRO F 252 GLN F 260 1 9
HELIX 155 AR2 ILE F 261 MET F 263 5 3
HELIX 156 AR3 TYR F 292 ALA F 299 1 8
HELIX 157 AR4 GLY F 316 ALA F 321 1 6
HELIX 158 AR5 VAL F 322 LYS F 325 5 4
HELIX 159 AR6 ASP F 328 ASN F 336 1 9
HELIX 160 AR7 ASN F 336 PHE F 345 1 10
HELIX 161 AR8 PRO F 352 ASN F 354 5 3
HELIX 162 AR9 GLN F 355 GLY F 369 1 15
HELIX 163 AS1 THR F 377 PHE F 390 1 14
HELIX 164 AS2 PHE F 390 GLY F 406 1 17
HELIX 165 AS3 SER F 421 SER F 428 1 8
HELIX 166 AS4 ASP F 440 PHE F 445 1 6
HELIX 167 AS5 SER F 454 THR F 474 1 21
HELIX 168 AS6 HIS F 517 ASP F 522 1 6
HELIX 169 AS7 GLU F 528 TYR F 532 5 5
HELIX 170 AS8 VAL G 38 ARG G 42 5 5
HELIX 171 AS9 ALA G 112 TYR G 116 5 5
HELIX 172 AT1 HIS G 120 ARG G 124 5 5
HELIX 173 AT2 LEU G 135 LEU G 141 1 7
HELIX 174 AT3 ASN G 151 VAL G 168 1 18
HELIX 175 AT4 MET G 169 PHE G 171 5 3
HELIX 176 AT5 SER G 184 SER G 196 1 13
HELIX 177 AT6 PRO G 197 LYS G 200 5 4
HELIX 178 AT7 ALA G 215 HIS G 219 5 5
HELIX 179 AT8 LYS G 222 VAL G 234 1 13
HELIX 180 AT9 THR G 240 ARG G 251 1 12
HELIX 181 AU1 PRO G 252 GLN G 260 1 9
HELIX 182 AU2 ILE G 261 MET G 263 5 3
HELIX 183 AU3 PRO G 267 MET G 271 5 5
HELIX 184 AU4 TYR G 292 ALA G 299 1 8
HELIX 185 AU5 GLY G 316 ALA G 321 1 6
HELIX 186 AU6 VAL G 322 LYS G 325 5 4
HELIX 187 AU7 ASP G 328 ASN G 336 1 9
HELIX 188 AU8 ASN G 336 PHE G 345 1 10
HELIX 189 AU9 PRO G 352 ASN G 354 5 3
HELIX 190 AV1 GLN G 355 GLY G 369 1 15
HELIX 191 AV2 THR G 377 PHE G 390 1 14
HELIX 192 AV3 PHE G 390 SER G 405 1 16
HELIX 193 AV4 SER G 421 SER G 428 1 8
HELIX 194 AV5 ASP G 440 PHE G 445 1 6
HELIX 195 AV6 SER G 454 THR G 474 1 21
HELIX 196 AV7 HIS G 517 ASP G 522 1 6
HELIX 197 AV8 GLU G 528 TYR G 532 5 5
HELIX 198 AV9 VAL H 38 ARG H 42 5 5
HELIX 199 AW1 ALA H 112 TYR H 116 5 5
HELIX 200 AW2 HIS H 120 ARG H 124 5 5
HELIX 201 AW3 LEU H 135 LEU H 141 1 7
HELIX 202 AW4 ASN H 151 VAL H 168 1 18
HELIX 203 AW5 MET H 169 PHE H 171 5 3
HELIX 204 AW6 SER H 184 SER H 196 1 13
HELIX 205 AW7 PRO H 197 LYS H 200 5 4
HELIX 206 AW8 ALA H 215 HIS H 219 5 5
HELIX 207 AW9 LYS H 222 VAL H 234 1 13
HELIX 208 AX1 THR H 240 ARG H 251 1 12
HELIX 209 AX2 PRO H 252 GLN H 260 1 9
HELIX 210 AX3 ILE H 261 MET H 263 5 3
HELIX 211 AX4 TYR H 292 ALA H 299 1 8
HELIX 212 AX5 GLY H 316 ALA H 321 1 6
HELIX 213 AX6 VAL H 322 LYS H 325 5 4
HELIX 214 AX7 ASP H 328 ASN H 336 1 9
HELIX 215 AX8 ASN H 336 PHE H 345 1 10
HELIX 216 AX9 PRO H 352 ASN H 354 5 3
HELIX 217 AY1 GLN H 355 GLY H 369 1 15
HELIX 218 AY2 THR H 377 PHE H 390 1 14
HELIX 219 AY3 PHE H 390 SER H 405 1 16
HELIX 220 AY4 SER H 421 SER H 428 1 8
HELIX 221 AY5 ASP H 440 PHE H 445 1 6
HELIX 222 AY6 SER H 454 THR H 474 1 21
HELIX 223 AY7 ASP H 514 GLY H 516 5 3
HELIX 224 AY8 HIS H 517 ASP H 522 1 6
HELIX 225 AY9 GLU H 528 TYR H 532 5 5
SHEET 1 AA1 3 VAL A 4 VAL A 7 0
SHEET 2 AA1 3 GLY A 10 GLN A 13 -1 O LEU A 12 N VAL A 5
SHEET 3 AA1 3 VAL A 55 ASP A 57 1 O TRP A 56 N VAL A 11
SHEET 1 AA211 SER A 15 VAL A 18 0
SHEET 2 AA211 THR A 24 PRO A 32 -1 O TYR A 25 N LYS A 17
SHEET 3 AA211 TYR A 83 THR A 88 -1 O THR A 88 N ALA A 26
SHEET 4 AA211 VAL A 127 PHE A 131 -1 O THR A 130 N ASN A 85
SHEET 5 AA211 LEU A 97 ILE A 103 1 N VAL A 100 O VAL A 127
SHEET 6 AA211 GLY A 173 CYS A 183 1 O ASN A 174 N LEU A 97
SHEET 7 AA211 ARG A 205 PHE A 209 1 O PHE A 209 N GLY A 182
SHEET 8 AA211 LEU A 307 THR A 312 1 O ILE A 308 N ALA A 208
SHEET 9 AA211 THR A 409 TYR A 414 1 O TYR A 410 N LEU A 307
SHEET 10 AA211 LEU A 496 ILE A 501 1 O ILE A 501 N ARG A 413
SHEET 11 AA211 MET A 507 SER A 512 -1 O LYS A 510 N TYR A 498
SHEET 1 AA3 2 GLN A 67 ASP A 69 0
SHEET 2 AA3 2 GLU A 74 SER A 76 -1 O GLU A 74 N ASP A 69
SHEET 1 AA4 3 VAL B 4 VAL B 7 0
SHEET 2 AA4 3 GLY B 10 GLN B 13 -1 O LEU B 12 N VAL B 5
SHEET 3 AA4 3 VAL B 55 ASP B 57 1 O TRP B 56 N VAL B 11
SHEET 1 AA511 SER B 15 VAL B 18 0
SHEET 2 AA511 THR B 24 PRO B 32 -1 O SER B 27 N SER B 15
SHEET 3 AA511 TYR B 83 THR B 88 -1 O THR B 88 N ALA B 26
SHEET 4 AA511 VAL B 127 PHE B 131 -1 O THR B 130 N ASN B 85
SHEET 5 AA511 LEU B 97 ILE B 103 1 N VAL B 100 O VAL B 127
SHEET 6 AA511 GLY B 173 CYS B 183 1 O THR B 179 N VAL B 99
SHEET 7 AA511 ARG B 205 PHE B 209 1 O ARG B 205 N LEU B 180
SHEET 8 AA511 LEU B 307 THR B 312 1 O ILE B 308 N ALA B 208
SHEET 9 AA511 THR B 409 TYR B 414 1 O TYR B 410 N LEU B 307
SHEET 10 AA511 TYR B 498 ILE B 501 1 O ILE B 501 N ARG B 413
SHEET 11 AA511 MET B 507 LYS B 510 -1 O LYS B 510 N TYR B 498
SHEET 1 AA6 2 GLN B 67 ASP B 69 0
SHEET 2 AA6 2 GLU B 74 SER B 76 -1 O GLU B 74 N ASP B 69
SHEET 1 AA7 3 VAL C 4 VAL C 7 0
SHEET 2 AA7 3 GLY C 10 GLN C 13 -1 O LEU C 12 N VAL C 5
SHEET 3 AA7 3 VAL C 55 ASP C 57 1 O TRP C 56 N VAL C 11
SHEET 1 AA811 SER C 15 VAL C 18 0
SHEET 2 AA811 THR C 24 PRO C 32 -1 O TYR C 25 N LYS C 17
SHEET 3 AA811 TYR C 83 THR C 88 -1 O THR C 88 N ALA C 26
SHEET 4 AA811 VAL C 127 PHE C 131 -1 O THR C 130 N ASN C 85
SHEET 5 AA811 LEU C 97 ILE C 103 1 N VAL C 100 O VAL C 127
SHEET 6 AA811 GLY C 173 CYS C 183 1 O THR C 179 N VAL C 99
SHEET 7 AA811 ARG C 205 PHE C 209 1 O ARG C 205 N LEU C 180
SHEET 8 AA811 LEU C 307 THR C 312 1 O ILE C 308 N ALA C 208
SHEET 9 AA811 THR C 409 TYR C 414 1 O TYR C 410 N LEU C 307
SHEET 10 AA811 LEU C 496 SER C 503 1 O ILE C 501 N ARG C 413
SHEET 11 AA811 ARG C 506 SER C 512 -1 O SER C 512 N LEU C 496
SHEET 1 AA9 2 GLN C 67 ASP C 69 0
SHEET 2 AA9 2 GLU C 74 SER C 76 -1 O GLU C 74 N ASP C 69
SHEET 1 AB1 3 VAL D 4 VAL D 7 0
SHEET 2 AB1 3 GLY D 10 GLN D 13 -1 O LEU D 12 N VAL D 5
SHEET 3 AB1 3 VAL D 55 ASP D 57 1 O TRP D 56 N VAL D 11
SHEET 1 AB211 SER D 15 VAL D 18 0
SHEET 2 AB211 THR D 24 PRO D 32 -1 O SER D 27 N SER D 15
SHEET 3 AB211 TYR D 83 THR D 88 -1 O ILE D 84 N VAL D 31
SHEET 4 AB211 VAL D 127 PHE D 131 -1 O THR D 130 N ASN D 85
SHEET 5 AB211 LEU D 97 ILE D 103 1 N VAL D 100 O VAL D 127
SHEET 6 AB211 GLY D 173 CYS D 183 1 O THR D 179 N VAL D 99
SHEET 7 AB211 ARG D 205 PHE D 209 1 O ARG D 205 N LEU D 180
SHEET 8 AB211 LEU D 307 THR D 312 1 O ILE D 308 N ALA D 208
SHEET 9 AB211 THR D 409 TYR D 414 1 O TYR D 414 N VAL D 311
SHEET 10 AB211 LEU D 496 ILE D 501 1 O ILE D 501 N ARG D 413
SHEET 11 AB211 MET D 507 SER D 512 -1 O GLU D 508 N GLU D 500
SHEET 1 AB3 2 GLN D 67 ASP D 69 0
SHEET 2 AB3 2 GLU D 74 SER D 76 -1 O GLU D 74 N ASP D 69
SHEET 1 AB4 3 VAL E 4 VAL E 7 0
SHEET 2 AB4 3 GLY E 10 GLN E 13 -1 O LEU E 12 N VAL E 5
SHEET 3 AB4 3 VAL E 55 ASP E 57 1 O TRP E 56 N VAL E 11
SHEET 1 AB511 SER E 15 VAL E 18 0
SHEET 2 AB511 THR E 24 PRO E 32 -1 O TYR E 25 N LYS E 17
SHEET 3 AB511 TYR E 83 THR E 88 -1 O ILE E 84 N VAL E 31
SHEET 4 AB511 VAL E 127 PHE E 131 -1 O THR E 130 N ASN E 85
SHEET 5 AB511 LEU E 97 ILE E 103 1 N VAL E 100 O VAL E 127
SHEET 6 AB511 GLY E 173 CYS E 183 1 O THR E 179 N VAL E 99
SHEET 7 AB511 ARG E 205 PHE E 209 1 O PHE E 209 N GLY E 182
SHEET 8 AB511 LEU E 307 THR E 312 1 O ILE E 308 N ALA E 208
SHEET 9 AB511 THR E 409 TYR E 414 1 O TYR E 414 N VAL E 311
SHEET 10 AB511 LEU E 496 ILE E 501 1 O ILE E 501 N ARG E 413
SHEET 11 AB511 MET E 507 SER E 512 -1 O GLU E 508 N GLU E 500
SHEET 1 AB6 2 GLN E 67 ASP E 69 0
SHEET 2 AB6 2 GLU E 74 SER E 76 -1 O GLU E 74 N ASP E 69
SHEET 1 AB7 3 VAL F 4 VAL F 7 0
SHEET 2 AB7 3 GLY F 10 GLN F 13 -1 O LEU F 12 N VAL F 5
SHEET 3 AB7 3 VAL F 55 ASP F 57 1 O TRP F 56 N VAL F 11
SHEET 1 AB811 SER F 15 VAL F 18 0
SHEET 2 AB811 THR F 24 PRO F 32 -1 O SER F 27 N SER F 15
SHEET 3 AB811 TYR F 83 THR F 88 -1 O ILE F 84 N VAL F 31
SHEET 4 AB811 VAL F 127 PHE F 131 -1 O THR F 130 N ASN F 85
SHEET 5 AB811 LEU F 97 ILE F 103 1 N VAL F 100 O VAL F 129
SHEET 6 AB811 GLY F 173 CYS F 183 1 O THR F 179 N VAL F 99
SHEET 7 AB811 ARG F 205 PHE F 209 1 O ILE F 207 N LEU F 180
SHEET 8 AB811 LEU F 307 THR F 312 1 O ILE F 308 N ALA F 208
SHEET 9 AB811 THR F 409 TYR F 414 1 O TYR F 410 N LEU F 307
SHEET 10 AB811 LEU F 496 SER F 503 1 O ILE F 501 N ARG F 413
SHEET 11 AB811 ARG F 506 SER F 512 -1 O LYS F 510 N TYR F 498
SHEET 1 AB9 2 GLN F 67 ASP F 69 0
SHEET 2 AB9 2 GLU F 74 SER F 76 -1 O GLU F 74 N ASP F 69
SHEET 1 AC1 3 VAL G 4 VAL G 7 0
SHEET 2 AC1 3 GLY G 10 GLN G 13 -1 O LEU G 12 N VAL G 5
SHEET 3 AC1 3 VAL G 55 ASP G 57 1 O TRP G 56 N VAL G 11
SHEET 1 AC211 SER G 15 VAL G 18 0
SHEET 2 AC211 THR G 24 PRO G 32 -1 O SER G 27 N SER G 15
SHEET 3 AC211 TYR G 83 THR G 88 -1 O ILE G 84 N VAL G 31
SHEET 4 AC211 VAL G 127 PHE G 131 -1 O THR G 130 N ASN G 85
SHEET 5 AC211 LEU G 97 ILE G 103 1 N VAL G 100 O VAL G 127
SHEET 6 AC211 GLY G 173 CYS G 183 1 O THR G 179 N VAL G 99
SHEET 7 AC211 ARG G 205 PHE G 209 1 O ARG G 205 N LEU G 180
SHEET 8 AC211 LEU G 307 THR G 312 1 O ILE G 308 N ALA G 208
SHEET 9 AC211 THR G 409 TYR G 414 1 O TYR G 410 N LEU G 307
SHEET 10 AC211 TYR G 498 SER G 503 1 O ILE G 501 N ARG G 413
SHEET 11 AC211 ARG G 506 LYS G 510 -1 O GLU G 508 N GLU G 500
SHEET 1 AC3 2 GLN G 67 ASP G 69 0
SHEET 2 AC3 2 GLU G 74 SER G 76 -1 O GLU G 74 N ASP G 69
SHEET 1 AC4 3 VAL H 4 VAL H 7 0
SHEET 2 AC4 3 GLY H 10 GLN H 13 -1 O LEU H 12 N VAL H 5
SHEET 3 AC4 3 VAL H 55 ASP H 57 1 O TRP H 56 N VAL H 11
SHEET 1 AC511 SER H 15 VAL H 18 0
SHEET 2 AC511 THR H 24 PRO H 32 -1 O SER H 27 N SER H 15
SHEET 3 AC511 TYR H 83 THR H 88 -1 O THR H 88 N ALA H 26
SHEET 4 AC511 VAL H 127 PHE H 131 -1 O THR H 130 N ASN H 85
SHEET 5 AC511 LEU H 97 ILE H 103 1 N VAL H 100 O VAL H 127
SHEET 6 AC511 GLY H 173 CYS H 183 1 O THR H 179 N VAL H 99
SHEET 7 AC511 ARG H 205 PHE H 209 1 O ARG H 205 N LEU H 180
SHEET 8 AC511 LEU H 307 THR H 312 1 O ILE H 308 N ALA H 208
SHEET 9 AC511 THR H 409 TYR H 414 1 O TYR H 410 N LEU H 307
SHEET 10 AC511 LEU H 496 SER H 503 1 O ILE H 501 N ARG H 413
SHEET 11 AC511 ARG H 506 SER H 512 -1 O LYS H 510 N TYR H 498
SHEET 1 AC6 2 GLN H 67 ASP H 69 0
SHEET 2 AC6 2 GLU H 74 SER H 76 -1 O GLU H 74 N ASP H 69
SSBOND 1 CYS A 65 CYS A 81 1555 1555 2.06
SSBOND 2 CYS A 236 CYS A 247 1555 1555 2.06
SSBOND 3 CYS B 65 CYS B 81 1555 1555 2.05
SSBOND 4 CYS B 236 CYS B 247 1555 1555 2.06
SSBOND 5 CYS C 65 CYS C 81 1555 1555 2.06
SSBOND 6 CYS C 236 CYS C 247 1555 1555 2.07
SSBOND 7 CYS D 65 CYS D 81 1555 1555 2.05
SSBOND 8 CYS D 236 CYS D 247 1555 1555 2.06
SSBOND 9 CYS E 65 CYS E 81 1555 1555 2.04
SSBOND 10 CYS E 236 CYS E 247 1555 1555 2.06
SSBOND 11 CYS F 65 CYS F 81 1555 1555 2.02
SSBOND 12 CYS F 236 CYS F 247 1555 1555 2.06
SSBOND 13 CYS G 65 CYS G 81 1555 1555 2.05
SSBOND 14 CYS G 236 CYS G 247 1555 1555 2.05
SSBOND 15 CYS H 65 CYS H 81 1555 1555 2.05
SSBOND 16 CYS H 236 CYS H 247 1555 1555 2.05
LINK ND2 ASN A 348 C1 NAG I 1 1555 1555 1.43
LINK ND2 ASN B 348 C1 NAG J 1 1555 1555 1.45
LINK ND2 ASN C 348 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN D 348 C1 NAG L 1 1555 1555 1.43
LINK ND2 ASN E 348 C1 NAG M 1 1555 1555 1.42
LINK ND2 ASN F 348 C1 NAG N 1 1555 1555 1.44
LINK ND2 ASN G 348 C1 NAG O 1 1555 1555 1.44
LINK ND2 ASN H 348 C1 NAG P 1 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.42
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.42
LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45
LINK O2 MAN I 4 C1 MAN I 5 1555 1555 1.43
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.42
LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.43
LINK O2 MAN J 4 C1 MAN J 5 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.43
LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.42
LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.46
LINK O2 MAN K 4 C1 MAN K 5 1555 1555 1.43
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.43
LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.42
LINK O3 BMA L 3 C1 MAN L 4 1555 1555 1.45
LINK O2 MAN L 4 C1 MAN L 5 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.42
LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.43
LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.44
LINK O2 MAN M 4 C1 MAN M 5 1555 1555 1.43
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44
LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44
LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.44
LINK O2 MAN N 4 C1 MAN N 5 1555 1555 1.44
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.42
LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.43
LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.46
LINK O2 MAN O 4 C1 MAN O 5 1555 1555 1.43
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44
LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44
LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.44
LINK O2 MAN P 4 C1 MAN P 5 1555 1555 1.45
CISPEP 1 TYR A 318 PRO A 319 0 8.60
CISPEP 2 TYR B 318 PRO B 319 0 5.24
CISPEP 3 TYR C 318 PRO C 319 0 4.16
CISPEP 4 TYR D 318 PRO D 319 0 5.72
CISPEP 5 TYR E 318 PRO E 319 0 5.80
CISPEP 6 TYR F 318 PRO F 319 0 6.98
CISPEP 7 TYR G 318 PRO G 319 0 7.39
CISPEP 8 TYR H 318 PRO H 319 0 7.26
CRYST1 107.475 113.967 125.772 78.31 70.18 65.88 P 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009304 -0.004166 -0.003051 0.00000
SCALE2 0.000000 0.009614 -0.000720 0.00000
SCALE3 0.000000 0.000000 0.008475 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.400898 -0.514933 0.757710 30.73705 1
MTRIX2 2 -0.525248 -0.548452 -0.650627 36.41433 1
MTRIX3 2 0.750597 -0.658820 -0.050595 0.36573 1
MTRIX1 3 -0.495522 -0.868584 -0.004358 20.78144 1
MTRIX2 3 -0.867815 0.495284 -0.039880 11.02165 1
MTRIX3 3 0.036797 -0.015980 -0.999195 -57.82088 1
MTRIX1 4 0.689706 0.111529 -0.715449 -26.52861 1
MTRIX2 4 0.691427 0.191973 0.696474 58.21593 1
MTRIX3 4 0.215024 -0.975042 0.055291 10.85777 1
MTRIX1 5 -0.830648 0.103814 0.547034 -32.90692 1
MTRIX2 5 0.116999 -0.927987 0.353768 -3.64967 1
MTRIX3 5 0.544366 0.357859 0.758685 46.04147 1
MTRIX1 6 0.694734 0.699589 0.167090 80.84615 1
MTRIX2 6 -0.001135 0.233372 -0.972387 25.09010 1
MTRIX3 6 -0.719266 0.675361 0.162926 -23.28895 1
MTRIX1 7 0.313305 0.789044 -0.528441 43.68258 1
MTRIX2 7 0.782895 -0.529564 -0.326553 39.11231 1
MTRIX3 7 -0.537508 -0.311402 -0.783654 -102.53239 1
MTRIX1 8 -0.933161 -0.286645 -0.216898 -85.00703 1
MTRIX2 8 -0.250702 0.086572 0.964185 58.56431 1
MTRIX3 8 -0.257602 0.954117 -0.152648 11.75947 1
TER 4148 HIS A 534
TER 8296 HIS B 534
TER 12444 HIS C 534
TER 16592 HIS D 534
TER 20740 HIS E 534
TER 24888 HIS F 534
TER 29036 HIS G 534
TER 33184 HIS H 534
MASTER 720 0 40 225 128 0 0 3034862 8 528 344
END |