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HEADER HYDROLASE 03-FEB-16 5FV4
TITLE PIG LIVER ESTERASE 5 (PLE5)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: PLE5;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: SHUFFLE T7 EXPRESS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET-15B
KEYWDS HYDROLASE, ESTERASE, ESTERASE-LIPASE SUPERFAMILY, CARBOXYLESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WERTEN,G.J.PALM,L.BERNDT,W.HINRICHS
REVDAT 1 15-FEB-17 5FV4 0
JRNL AUTH S.WERTEN,G.J.PALM,L.BERNDT,W.HINRICHS
JRNL TITL PIG LIVER ESTERASE 5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.74
REMARK 3 NUMBER OF REFLECTIONS : 137701
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) : 0.18043
REMARK 3 R VALUE (WORKING SET) : 0.17912
REMARK 3 FREE R VALUE : 0.20510
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 7248
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) : 2.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.462
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10152
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.300
REMARK 3 BIN FREE R VALUE SET COUNT : 534
REMARK 3 BIN FREE R VALUE : 0.319
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 517
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.262
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.180
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.97
REMARK 3 B22 (A**2) : -1.01
REMARK 3 B33 (A**2) : 0.12
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.33
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.359
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.179
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.945
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25254 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 23880 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34368 ; 1.562 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 55176 ; 1.282 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3174 ; 6.036 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1062 ;36.055 ;24.294
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4038 ;15.055 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;18.059 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3762 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 28560 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5628 ; 0.007 ; 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): 12714 ; 2.003 ; 3.808
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 12713 ; 2.002 ; 3.807
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15882 ; 3.201 ; 5.706
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12540 ; 2.379 ; 4.050
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 6
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 15
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 5 534 B 5 534 65956 0.04 0.05
REMARK 3 2 A 5 534 C 5 534 66270 0.03 0.05
REMARK 3 3 A 5 534 D 5 534 65952 0.04 0.05
REMARK 3 4 A 5 534 E 5 534 66352 0.03 0.05
REMARK 3 5 A 5 534 F 5 534 66070 0.04 0.05
REMARK 3 6 B 5 534 C 5 534 66236 0.04 0.05
REMARK 3 7 B 5 534 D 5 534 65930 0.04 0.05
REMARK 3 8 B 5 534 E 5 534 66124 0.03 0.05
REMARK 3 9 B 5 534 F 5 534 66236 0.04 0.05
REMARK 3 10 C 5 534 D 5 534 66184 0.04 0.05
REMARK 3 11 C 5 534 E 5 534 66416 0.03 0.05
REMARK 3 12 C 5 534 F 5 534 66314 0.04 0.05
REMARK 3 13 D 5 534 E 5 534 66212 0.03 0.05
REMARK 3 14 D 5 534 F 5 534 66080 0.04 0.05
REMARK 3 15 E 5 534 F 5 534 66338 0.03 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 5 A 534
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3369 146.5089 110.4509
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.2745
REMARK 3 T33: 0.0074 T12: 0.0389
REMARK 3 T13: 0.0076 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.9714 L22: 1.0485
REMARK 3 L33: 1.1799 L12: -0.2950
REMARK 3 L13: -0.4756 L23: 0.4712
REMARK 3 S TENSOR
REMARK 3 S11: 0.0239 S12: 0.1959 S13: 0.0227
REMARK 3 S21: -0.1300 S22: -0.0318 S23: -0.0361
REMARK 3 S31: 0.0206 S32: -0.0032 S33: 0.0079
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 5 B 534
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7178 154.3572 56.2409
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: 0.3959
REMARK 3 T33: 0.1845 T12: -0.0291
REMARK 3 T13: -0.0054 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 1.3205 L22: 0.8905
REMARK 3 L33: 1.2975 L12: 0.2764
REMARK 3 L13: -0.2420 L23: -0.1655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0429 S12: -0.4293 S13: -0.0522
REMARK 3 S21: 0.1499 S22: -0.1249 S23: -0.0471
REMARK 3 S31: 0.0518 S32: 0.0424 S33: 0.0820
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 5 C 534
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2740 96.7865 69.7522
REMARK 3 T TENSOR
REMARK 3 T11: 0.0492 T22: 0.1365
REMARK 3 T33: 0.2327 T12: 0.0221
REMARK 3 T13: -0.0027 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 0.8455 L22: 1.7606
REMARK 3 L33: 1.1773 L12: -0.3445
REMARK 3 L13: -0.0100 L23: -0.0193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0199 S12: 0.0460 S13: 0.3000
REMARK 3 S21: -0.0770 S22: -0.0838 S23: -0.1897
REMARK 3 S31: -0.2305 S32: -0.0605 S33: 0.0639
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 5 D 534
REMARK 3 ORIGIN FOR THE GROUP (A): -37.0960 130.3568 112.2242
REMARK 3 T TENSOR
REMARK 3 T11: 0.1627 T22: 0.3425
REMARK 3 T33: 0.3671 T12: -0.0105
REMARK 3 T13: -0.1352 T23: -0.1993
REMARK 3 L TENSOR
REMARK 3 L11: 1.9309 L22: 1.1792
REMARK 3 L33: 2.4881 L12: 0.0454
REMARK 3 L13: 1.1763 L23: 0.0819
REMARK 3 S TENSOR
REMARK 3 S11: 0.3264 S12: 0.4432 S13: -0.5249
REMARK 3 S21: -0.1121 S22: 0.0943 S23: 0.1280
REMARK 3 S31: 0.5905 S32: 0.0460 S33: -0.4208
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 5 E 534
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1109 93.8800 99.4280
REMARK 3 T TENSOR
REMARK 3 T11: 0.2557 T22: 0.2868
REMARK 3 T33: 0.5836 T12: -0.1157
REMARK 3 T13: -0.0891 T23: -0.1660
REMARK 3 L TENSOR
REMARK 3 L11: 0.9888 L22: 2.1139
REMARK 3 L33: 2.0673 L12: 0.2367
REMARK 3 L13: 0.1507 L23: -0.2170
REMARK 3 S TENSOR
REMARK 3 S11: -0.0570 S12: -0.2457 S13: 0.4233
REMARK 3 S21: 0.3215 S22: -0.0632 S23: -0.0158
REMARK 3 S31: -0.6580 S32: 0.2641 S33: 0.1201
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 5 F 534
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8107 136.9797 58.7750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0855 T22: 0.3078
REMARK 3 T33: 0.0804 T12: 0.0626
REMARK 3 T13: -0.0037 T23: 0.1072
REMARK 3 L TENSOR
REMARK 3 L11: 1.2649 L22: 0.9915
REMARK 3 L33: 2.2907 L12: -0.3363
REMARK 3 L13: 0.5522 L23: -0.3044
REMARK 3 S TENSOR
REMARK 3 S11: 0.0952 S12: -0.1613 S13: -0.2429
REMARK 3 S21: -0.0094 S22: 0.0198 S23: 0.1559
REMARK 3 S31: 0.4210 S32: 0.1237 S33: -0.1149
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
REMARK 3 RIDING POSITIONS.
REMARK 3 U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 5FV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-16.
REMARK 100 THE PDBE ID CODE IS EBI-66170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-15
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 : PETRA III
REMARK 200 BEAMLINE : P13 (MX1)
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 : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 144950
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 71.14
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.3
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.1
REMARK 200 R MERGE FOR SHELL (I) : 0.77
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.02
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: PDB ENTRY 1MX9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 18% PEG
REMARK 280 4000 AT 295 K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 94.01000
REMARK 290 SMTRY3 2 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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY A 1
REMARK 465 GLN A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 GLU A 535
REMARK 465 ALA A 536
REMARK 465 ALA A 537
REMARK 465 LYS A 538
REMARK 465 LYS A 539
REMARK 465 PRO A 540
REMARK 465 PRO A 541
REMARK 465 LYS A 542
REMARK 465 ILE A 543
REMARK 465 LYS A 544
REMARK 465 GLY B 1
REMARK 465 GLN B 2
REMARK 465 PRO B 3
REMARK 465 ALA B 4
REMARK 465 GLU B 535
REMARK 465 ALA B 536
REMARK 465 ALA B 537
REMARK 465 LYS B 538
REMARK 465 LYS B 539
REMARK 465 PRO B 540
REMARK 465 PRO B 541
REMARK 465 LYS B 542
REMARK 465 ILE B 543
REMARK 465 LYS B 544
REMARK 465 GLY C 1
REMARK 465 GLN C 2
REMARK 465 PRO C 3
REMARK 465 ALA C 4
REMARK 465 GLU C 535
REMARK 465 ALA C 536
REMARK 465 ALA C 537
REMARK 465 LYS C 538
REMARK 465 LYS C 539
REMARK 465 PRO C 540
REMARK 465 PRO C 541
REMARK 465 LYS C 542
REMARK 465 ILE C 543
REMARK 465 LYS C 544
REMARK 465 GLY D 1
REMARK 465 GLN D 2
REMARK 465 PRO D 3
REMARK 465 ALA D 4
REMARK 465 GLU D 535
REMARK 465 ALA D 536
REMARK 465 ALA D 537
REMARK 465 LYS D 538
REMARK 465 LYS D 539
REMARK 465 PRO D 540
REMARK 465 PRO D 541
REMARK 465 LYS D 542
REMARK 465 ILE D 543
REMARK 465 LYS D 544
REMARK 465 GLY E 1
REMARK 465 GLN E 2
REMARK 465 PRO E 3
REMARK 465 ALA E 4
REMARK 465 GLU E 535
REMARK 465 ALA E 536
REMARK 465 ALA E 537
REMARK 465 LYS E 538
REMARK 465 LYS E 539
REMARK 465 PRO E 540
REMARK 465 PRO E 541
REMARK 465 LYS E 542
REMARK 465 ILE E 543
REMARK 465 LYS E 544
REMARK 465 GLY F 1
REMARK 465 GLN F 2
REMARK 465 PRO F 3
REMARK 465 ALA F 4
REMARK 465 GLU F 535
REMARK 465 ALA F 536
REMARK 465 ALA F 537
REMARK 465 LYS F 538
REMARK 465 LYS F 539
REMARK 465 PRO F 540
REMARK 465 PRO F 541
REMARK 465 LYS F 542
REMARK 465 ILE F 543
REMARK 465 LYS F 544
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLY D 492 OE1 GLU E 493 1455 1.85
REMARK 500 O LEU D 495 OE2 GLU E 493 1455 1.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 47 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 295 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 295 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 LEU D 26 CB - CG - CD1 ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG D 113 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG E 113 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG F 47 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP F 465 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP F 465 CB - CG - OD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 59 -167.52 62.48
REMARK 500 CYS A 99 11.38 -140.98
REMARK 500 ARG A 115 53.75 -140.88
REMARK 500 SER A 168 82.24 -157.65
REMARK 500 SER A 204 -122.98 63.07
REMARK 500 MET A 243 25.04 -141.40
REMARK 500 VAL A 308 -71.58 -131.42
REMARK 500 TRP A 339 -57.25 -153.70
REMARK 500 ASP A 502 -150.85 -110.72
REMARK 500 ARG A 519 56.56 70.47
REMARK 500 GLN B 28 109.46 -49.90
REMARK 500 PHE B 59 -166.37 63.34
REMARK 500 THR B 63 61.56 -119.40
REMARK 500 SER B 168 84.61 -160.90
REMARK 500 SER B 204 -121.51 62.66
REMARK 500 VAL B 308 -72.07 -131.29
REMARK 500 TRP B 339 -58.22 -153.81
REMARK 500 ASP B 502 -152.78 -111.58
REMARK 500 ARG B 519 57.05 70.18
REMARK 500 PHE C 59 -167.62 63.55
REMARK 500 THR C 63 61.05 -119.89
REMARK 500 ARG C 113 79.79 -110.92
REMARK 500 SER C 168 84.04 -162.29
REMARK 500 SER C 204 -121.34 63.98
REMARK 500 MET C 243 28.10 -142.93
REMARK 500 VAL C 308 -71.01 -131.12
REMARK 500 TRP C 339 -56.24 -153.84
REMARK 500 ASP C 502 -152.00 -110.59
REMARK 500 ARG C 519 56.83 70.65
REMARK 500 GLN D 28 109.22 -49.36
REMARK 500 PHE D 59 -165.06 63.21
REMARK 500 SER D 168 82.35 -160.40
REMARK 500 SER D 204 -124.23 61.75
REMARK 500 VAL D 308 -73.15 -131.43
REMARK 500 TRP D 339 -57.22 -153.47
REMARK 500 GLU D 351 -30.17 -39.97
REMARK 500 ASP D 502 -152.66 -112.14
REMARK 500 ARG D 519 56.85 70.40
REMARK 500 PHE E 59 -167.36 62.34
REMARK 500 THR E 63 63.08 -117.13
REMARK 500 SER E 168 83.05 -160.44
REMARK 500 SER E 204 -122.59 60.45
REMARK 500 VAL E 308 -70.52 -130.89
REMARK 500 TRP E 339 -57.16 -153.42
REMARK 500 ASP E 502 -151.66 -111.88
REMARK 500 ARG E 519 57.29 70.00
REMARK 500 PHE F 59 -163.70 61.91
REMARK 500 THR F 63 61.45 -118.38
REMARK 500 SER F 168 84.37 -159.60
REMARK 500 SER F 197 80.76 -150.90
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE DIFFERENCES BETWEEN UNIPROT AND THE SAMPLE ARE
REMARK 999 DUE TO A LOCAL CLONE BEING USED.
DBREF 5FV4 A 1 544 UNP A9GYW6 A9GYW6_PIG 1 544
DBREF 5FV4 B 1 544 UNP A9GYW6 A9GYW6_PIG 1 544
DBREF 5FV4 C 1 544 UNP A9GYW6 A9GYW6_PIG 1 544
DBREF 5FV4 D 1 544 UNP A9GYW6 A9GYW6_PIG 1 544
DBREF 5FV4 E 1 544 UNP A9GYW6 A9GYW6_PIG 1 544
DBREF 5FV4 F 1 544 UNP A9GYW6 A9GYW6_PIG 1 544
SEQADV 5FV4 ASP A 73 UNP A9GYW6 GLU 73 CONFLICT
SEQADV 5FV4 VAL A 75 UNP A9GYW6 ILE 75 CONFLICT
SEQADV 5FV4 ALA A 76 UNP A9GYW6 GLY 76 CONFLICT
SEQADV 5FV4 THR A 80 UNP A9GYW6 LEU 80 CONFLICT
SEQADV 5FV4 ALA A 459 UNP A9GYW6 PHE 459 CONFLICT
SEQADV 5FV4 PHE A 461 UNP A9GYW6 LEU 461 CONFLICT
SEQADV 5FV4 ARG A 463 UNP A9GYW6 LYS 463 CONFLICT
SEQADV 5FV4 ASP B 73 UNP A9GYW6 GLU 73 CONFLICT
SEQADV 5FV4 VAL B 75 UNP A9GYW6 ILE 75 CONFLICT
SEQADV 5FV4 ALA B 76 UNP A9GYW6 GLY 76 CONFLICT
SEQADV 5FV4 THR B 80 UNP A9GYW6 LEU 80 CONFLICT
SEQADV 5FV4 ALA B 459 UNP A9GYW6 PHE 459 CONFLICT
SEQADV 5FV4 PHE B 461 UNP A9GYW6 LEU 461 CONFLICT
SEQADV 5FV4 ARG B 463 UNP A9GYW6 LYS 463 CONFLICT
SEQADV 5FV4 ASP C 73 UNP A9GYW6 GLU 73 CONFLICT
SEQADV 5FV4 VAL C 75 UNP A9GYW6 ILE 75 CONFLICT
SEQADV 5FV4 ALA C 76 UNP A9GYW6 GLY 76 CONFLICT
SEQADV 5FV4 THR C 80 UNP A9GYW6 LEU 80 CONFLICT
SEQADV 5FV4 ALA C 459 UNP A9GYW6 PHE 459 CONFLICT
SEQADV 5FV4 PHE C 461 UNP A9GYW6 LEU 461 CONFLICT
SEQADV 5FV4 ARG C 463 UNP A9GYW6 LYS 463 CONFLICT
SEQADV 5FV4 ASP D 73 UNP A9GYW6 GLU 73 CONFLICT
SEQADV 5FV4 VAL D 75 UNP A9GYW6 ILE 75 CONFLICT
SEQADV 5FV4 ALA D 76 UNP A9GYW6 GLY 76 CONFLICT
SEQADV 5FV4 THR D 80 UNP A9GYW6 LEU 80 CONFLICT
SEQADV 5FV4 ALA D 459 UNP A9GYW6 PHE 459 CONFLICT
SEQADV 5FV4 PHE D 461 UNP A9GYW6 LEU 461 CONFLICT
SEQADV 5FV4 ARG D 463 UNP A9GYW6 LYS 463 CONFLICT
SEQADV 5FV4 ASP E 73 UNP A9GYW6 GLU 73 CONFLICT
SEQADV 5FV4 VAL E 75 UNP A9GYW6 ILE 75 CONFLICT
SEQADV 5FV4 ALA E 76 UNP A9GYW6 GLY 76 CONFLICT
SEQADV 5FV4 THR E 80 UNP A9GYW6 LEU 80 CONFLICT
SEQADV 5FV4 ALA E 459 UNP A9GYW6 PHE 459 CONFLICT
SEQADV 5FV4 PHE E 461 UNP A9GYW6 LEU 461 CONFLICT
SEQADV 5FV4 ARG E 463 UNP A9GYW6 LYS 463 CONFLICT
SEQADV 5FV4 ASP F 73 UNP A9GYW6 GLU 73 CONFLICT
SEQADV 5FV4 VAL F 75 UNP A9GYW6 ILE 75 CONFLICT
SEQADV 5FV4 ALA F 76 UNP A9GYW6 GLY 76 CONFLICT
SEQADV 5FV4 THR F 80 UNP A9GYW6 LEU 80 CONFLICT
SEQADV 5FV4 ALA F 459 UNP A9GYW6 PHE 459 CONFLICT
SEQADV 5FV4 PHE F 461 UNP A9GYW6 LEU 461 CONFLICT
SEQADV 5FV4 ARG F 463 UNP A9GYW6 LYS 463 CONFLICT
SEQRES 1 A 544 GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN
SEQRES 2 A 544 GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU
SEQRES 3 A 544 ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA
SEQRES 4 A 544 LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN
SEQRES 5 A 544 PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER
SEQRES 6 A 544 TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN
SEQRES 7 A 544 MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU
SEQRES 8 A 544 ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 9 A 544 TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO
SEQRES 10 A 544 VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY
SEQRES 11 A 544 GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS
SEQRES 12 A 544 GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY
SEQRES 13 A 544 ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG
SEQRES 14 A 544 GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS
SEQRES 15 A 544 TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO
SEQRES 16 A 544 GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU
SEQRES 17 A 544 SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN
SEQRES 18 A 544 LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE
SEQRES 19 A 544 THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA
SEQRES 20 A 544 LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR
SEQRES 21 A 544 SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU
SEQRES 22 A 544 ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE
SEQRES 23 A 544 ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO
SEQRES 24 A 544 PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS
SEQRES 25 A 544 MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR
SEQRES 26 A 544 VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 A 544 TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU
SEQRES 28 A 544 GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP
SEQRES 29 A 544 LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR
SEQRES 30 A 544 PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 A 544 PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY
SEQRES 32 A 544 ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG
SEQRES 33 A 544 GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 A 544 PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO
SEQRES 35 A 544 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER
SEQRES 36 A 544 VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU
SEQRES 37 A 544 GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP
SEQRES 38 A 544 ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 A 544 LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR
SEQRES 40 A 544 LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU
SEQRES 41 A 544 LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER
SEQRES 42 A 544 LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS
SEQRES 1 B 544 GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN
SEQRES 2 B 544 GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU
SEQRES 3 B 544 ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA
SEQRES 4 B 544 LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN
SEQRES 5 B 544 PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER
SEQRES 6 B 544 TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN
SEQRES 7 B 544 MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU
SEQRES 8 B 544 ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 9 B 544 TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO
SEQRES 10 B 544 VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY
SEQRES 11 B 544 GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS
SEQRES 12 B 544 GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY
SEQRES 13 B 544 ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG
SEQRES 14 B 544 GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS
SEQRES 15 B 544 TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO
SEQRES 16 B 544 GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU
SEQRES 17 B 544 SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN
SEQRES 18 B 544 LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE
SEQRES 19 B 544 THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA
SEQRES 20 B 544 LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR
SEQRES 21 B 544 SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU
SEQRES 22 B 544 ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE
SEQRES 23 B 544 ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO
SEQRES 24 B 544 PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS
SEQRES 25 B 544 MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR
SEQRES 26 B 544 VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 B 544 TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU
SEQRES 28 B 544 GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP
SEQRES 29 B 544 LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR
SEQRES 30 B 544 PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 B 544 PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY
SEQRES 32 B 544 ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG
SEQRES 33 B 544 GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 B 544 PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO
SEQRES 35 B 544 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER
SEQRES 36 B 544 VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU
SEQRES 37 B 544 GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP
SEQRES 38 B 544 ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 B 544 LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR
SEQRES 40 B 544 LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU
SEQRES 41 B 544 LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER
SEQRES 42 B 544 LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS
SEQRES 1 C 544 GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN
SEQRES 2 C 544 GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU
SEQRES 3 C 544 ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA
SEQRES 4 C 544 LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN
SEQRES 5 C 544 PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER
SEQRES 6 C 544 TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN
SEQRES 7 C 544 MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU
SEQRES 8 C 544 ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 9 C 544 TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO
SEQRES 10 C 544 VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY
SEQRES 11 C 544 GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS
SEQRES 12 C 544 GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY
SEQRES 13 C 544 ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG
SEQRES 14 C 544 GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS
SEQRES 15 C 544 TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO
SEQRES 16 C 544 GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU
SEQRES 17 C 544 SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN
SEQRES 18 C 544 LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE
SEQRES 19 C 544 THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA
SEQRES 20 C 544 LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR
SEQRES 21 C 544 SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU
SEQRES 22 C 544 ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE
SEQRES 23 C 544 ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO
SEQRES 24 C 544 PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS
SEQRES 25 C 544 MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR
SEQRES 26 C 544 VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 C 544 TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU
SEQRES 28 C 544 GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP
SEQRES 29 C 544 LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR
SEQRES 30 C 544 PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 C 544 PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY
SEQRES 32 C 544 ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG
SEQRES 33 C 544 GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 C 544 PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO
SEQRES 35 C 544 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER
SEQRES 36 C 544 VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU
SEQRES 37 C 544 GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP
SEQRES 38 C 544 ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 C 544 LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR
SEQRES 40 C 544 LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU
SEQRES 41 C 544 LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER
SEQRES 42 C 544 LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS
SEQRES 1 D 544 GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN
SEQRES 2 D 544 GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU
SEQRES 3 D 544 ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA
SEQRES 4 D 544 LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN
SEQRES 5 D 544 PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER
SEQRES 6 D 544 TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN
SEQRES 7 D 544 MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU
SEQRES 8 D 544 ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 9 D 544 TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO
SEQRES 10 D 544 VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY
SEQRES 11 D 544 GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS
SEQRES 12 D 544 GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY
SEQRES 13 D 544 ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG
SEQRES 14 D 544 GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS
SEQRES 15 D 544 TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO
SEQRES 16 D 544 GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU
SEQRES 17 D 544 SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN
SEQRES 18 D 544 LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE
SEQRES 19 D 544 THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA
SEQRES 20 D 544 LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR
SEQRES 21 D 544 SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU
SEQRES 22 D 544 ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE
SEQRES 23 D 544 ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO
SEQRES 24 D 544 PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS
SEQRES 25 D 544 MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR
SEQRES 26 D 544 VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 D 544 TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU
SEQRES 28 D 544 GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP
SEQRES 29 D 544 LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR
SEQRES 30 D 544 PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 D 544 PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY
SEQRES 32 D 544 ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG
SEQRES 33 D 544 GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 D 544 PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO
SEQRES 35 D 544 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER
SEQRES 36 D 544 VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU
SEQRES 37 D 544 GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP
SEQRES 38 D 544 ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 D 544 LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR
SEQRES 40 D 544 LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU
SEQRES 41 D 544 LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER
SEQRES 42 D 544 LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS
SEQRES 1 E 544 GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN
SEQRES 2 E 544 GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU
SEQRES 3 E 544 ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA
SEQRES 4 E 544 LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN
SEQRES 5 E 544 PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER
SEQRES 6 E 544 TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN
SEQRES 7 E 544 MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU
SEQRES 8 E 544 ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 9 E 544 TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO
SEQRES 10 E 544 VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY
SEQRES 11 E 544 GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS
SEQRES 12 E 544 GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY
SEQRES 13 E 544 ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG
SEQRES 14 E 544 GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS
SEQRES 15 E 544 TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO
SEQRES 16 E 544 GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU
SEQRES 17 E 544 SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN
SEQRES 18 E 544 LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE
SEQRES 19 E 544 THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA
SEQRES 20 E 544 LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR
SEQRES 21 E 544 SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU
SEQRES 22 E 544 ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE
SEQRES 23 E 544 ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO
SEQRES 24 E 544 PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS
SEQRES 25 E 544 MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR
SEQRES 26 E 544 VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 E 544 TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU
SEQRES 28 E 544 GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP
SEQRES 29 E 544 LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR
SEQRES 30 E 544 PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 E 544 PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY
SEQRES 32 E 544 ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG
SEQRES 33 E 544 GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 E 544 PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO
SEQRES 35 E 544 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER
SEQRES 36 E 544 VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU
SEQRES 37 E 544 GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP
SEQRES 38 E 544 ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 E 544 LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR
SEQRES 40 E 544 LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU
SEQRES 41 E 544 LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER
SEQRES 42 E 544 LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS
SEQRES 1 F 544 GLY GLN PRO ALA SER PRO PRO VAL VAL ASP THR ALA GLN
SEQRES 2 F 544 GLY ARG VAL LEU GLY LYS TYR VAL SER LEU GLU GLY LEU
SEQRES 3 F 544 ALA GLN PRO VAL ALA VAL PHE LEU GLY VAL PRO PHE ALA
SEQRES 4 F 544 LYS PRO PRO LEU GLY SER LEU ARG PHE ALA PRO PRO GLN
SEQRES 5 F 544 PRO ALA GLU PRO TRP SER PHE VAL LYS ASN THR THR SER
SEQRES 6 F 544 TYR PRO PRO MET CYS CYS GLN ASP PRO VAL ALA GLY GLN
SEQRES 7 F 544 MET THR SER ASP LEU PHE THR ASN ARG LYS GLU ARG LEU
SEQRES 8 F 544 ILE PRO GLU PHE SER GLU ASP CYS LEU TYR LEU ASN ILE
SEQRES 9 F 544 TYR THR PRO ALA ASP LEU THR LYS ARG GLY ARG LEU PRO
SEQRES 10 F 544 VAL MET VAL TRP ILE HIS GLY GLY GLY LEU VAL VAL GLY
SEQRES 11 F 544 GLY ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS
SEQRES 12 F 544 GLU ASN VAL VAL VAL VAL ALA ILE GLN TYR ARG LEU GLY
SEQRES 13 F 544 ILE TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG
SEQRES 14 F 544 GLY ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU HIS
SEQRES 15 F 544 TRP VAL GLN GLU ASN ILE ALA ASN PHE GLY GLY ASP PRO
SEQRES 16 F 544 GLY SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU
SEQRES 17 F 544 SER VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN
SEQRES 18 F 544 LEU PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA PHE
SEQRES 19 F 544 THR ALA GLY LEU VAL ARG LYS ASP MET LYS ALA ALA ALA
SEQRES 20 F 544 LYS GLN ILE ALA VAL LEU ALA GLY CYS LYS THR THR THR
SEQRES 21 F 544 SER ALA VAL PHE VAL HIS CYS LEU ARG GLN LYS SER GLU
SEQRES 22 F 544 ASP GLU LEU LEU ASP LEU THR LEU LYS MET LYS PHE PHE
SEQRES 23 F 544 ALA LEU ASP LEU HIS GLY ASP PRO ARG GLU SER HIS PRO
SEQRES 24 F 544 PHE LEU THR THR VAL VAL ASP GLY VAL LEU LEU PRO LYS
SEQRES 25 F 544 MET PRO GLU GLU ILE LEU ALA GLU LYS ASP PHE ASN THR
SEQRES 26 F 544 VAL PRO TYR ILE VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES 27 F 544 TRP LEU LEU PRO THR MET MET GLY PHE PRO LEU SER GLU
SEQRES 28 F 544 GLY LYS LEU ASP GLN LYS THR ALA THR SER LEU LEU TRP
SEQRES 29 F 544 LYS SER TYR PRO ILE ALA ASN ILE PRO GLU GLU LEU THR
SEQRES 30 F 544 PRO VAL ALA THR ASP LYS TYR LEU GLY GLY THR ASP ASP
SEQRES 31 F 544 PRO VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU MET GLY
SEQRES 32 F 544 ASP VAL VAL PHE GLY VAL PRO SER VAL THR VAL ALA ARG
SEQRES 33 F 544 GLN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES 34 F 544 PHE GLN TYR ARG PRO SER PHE SER SER ASP LYS LYS PRO
SEQRES 35 F 544 LYS THR VAL ILE GLY ASP HIS GLY ASP GLU ILE PHE SER
SEQRES 36 F 544 VAL PHE GLY ALA PRO PHE LEU ARG GLY ASP ALA PRO GLU
SEQRES 37 F 544 GLU GLU VAL SER LEU SER LYS THR VAL MET LYS PHE TRP
SEQRES 38 F 544 ALA ASN PHE ALA ARG SER GLY ASN PRO ASN GLY GLU GLY
SEQRES 39 F 544 LEU PRO HIS TRP PRO MET TYR ASP GLN GLU GLU GLY TYR
SEQRES 40 F 544 LEU GLN ILE GLY VAL ASN THR GLN ALA ALA LYS ARG LEU
SEQRES 41 F 544 LYS GLY GLU GLU VAL ALA PHE TRP ASN ASP LEU LEU SER
SEQRES 42 F 544 LYS GLU ALA ALA LYS LYS PRO PRO LYS ILE LYS
FORMUL 7 HOH *517(H2 O)
HELIX 1 1 LEU A 43 ARG A 47 5 5
HELIX 2 2 ASP A 73 THR A 85 1 13
HELIX 3 3 GLY A 131 TYR A 135 5 5
HELIX 4 4 GLY A 137 ASN A 145 1 9
HELIX 5 5 LEU A 155 PHE A 161 1 7
HELIX 6 6 ASN A 171 ILE A 188 1 18
HELIX 7 7 ALA A 189 PHE A 191 5 3
HELIX 8 8 SER A 204 SER A 216 1 13
HELIX 9 9 PRO A 217 LYS A 220 5 4
HELIX 10 10 PHE A 234 GLY A 237 5 4
HELIX 11 11 MET A 243 GLY A 255 1 13
HELIX 12 12 THR A 260 LYS A 271 1 12
HELIX 13 13 SER A 272 LYS A 284 1 13
HELIX 14 14 ASP A 293 SER A 297 5 5
HELIX 15 15 MET A 313 LYS A 321 1 9
HELIX 16 16 TRP A 339 MET A 345 1 7
HELIX 17 17 ASP A 355 SER A 366 1 12
HELIX 18 18 SER A 366 ASN A 371 1 6
HELIX 19 19 PRO A 373 GLU A 375 5 3
HELIX 20 20 LEU A 376 GLY A 386 1 11
HELIX 21 21 ASP A 390 PHE A 407 1 18
HELIX 22 22 PHE A 407 ALA A 421 1 15
HELIX 23 23 GLY A 450 PHE A 457 1 8
HELIX 24 24 GLY A 458 LEU A 462 5 5
HELIX 25 25 PRO A 467 GLY A 488 1 22
HELIX 26 26 LYS A 521 LEU A 532 1 12
HELIX 27 27 LEU B 43 ARG B 47 5 5
HELIX 28 28 ASP B 73 THR B 85 1 13
HELIX 29 29 GLY B 131 TYR B 135 5 5
HELIX 30 30 GLY B 137 ASN B 145 1 9
HELIX 31 31 LEU B 155 PHE B 161 1 7
HELIX 32 32 ASN B 171 ILE B 188 1 18
HELIX 33 33 ALA B 189 PHE B 191 5 3
HELIX 34 34 SER B 204 SER B 216 1 13
HELIX 35 35 PRO B 217 LYS B 220 5 4
HELIX 36 36 PHE B 234 GLY B 237 5 4
HELIX 37 37 MET B 243 GLY B 255 1 13
HELIX 38 38 THR B 260 LYS B 271 1 12
HELIX 39 39 SER B 272 LYS B 284 1 13
HELIX 40 40 ASP B 293 SER B 297 5 5
HELIX 41 41 MET B 313 LYS B 321 1 9
HELIX 42 42 TRP B 339 GLY B 346 1 8
HELIX 43 43 ASP B 355 SER B 366 1 12
HELIX 44 44 SER B 366 ASN B 371 1 6
HELIX 45 45 PRO B 373 GLU B 375 5 3
HELIX 46 46 LEU B 376 GLY B 386 1 11
HELIX 47 47 ASP B 390 PHE B 407 1 18
HELIX 48 48 PHE B 407 ALA B 421 1 15
HELIX 49 49 GLY B 450 PHE B 457 1 8
HELIX 50 50 GLY B 458 LEU B 462 5 5
HELIX 51 51 PRO B 467 GLY B 488 1 22
HELIX 52 52 LYS B 521 LEU B 532 1 12
HELIX 53 53 LEU C 43 ARG C 47 5 5
HELIX 54 54 ASP C 73 THR C 85 1 13
HELIX 55 55 GLY C 131 TYR C 135 5 5
HELIX 56 56 GLY C 137 ASN C 145 1 9
HELIX 57 57 LEU C 155 PHE C 161 1 7
HELIX 58 58 ASN C 171 ILE C 188 1 18
HELIX 59 59 ALA C 189 PHE C 191 5 3
HELIX 60 60 SER C 204 SER C 216 1 13
HELIX 61 61 PRO C 217 LYS C 220 5 4
HELIX 62 62 PHE C 234 GLY C 237 5 4
HELIX 63 63 MET C 243 GLY C 255 1 13
HELIX 64 64 THR C 260 LYS C 271 1 12
HELIX 65 65 SER C 272 LYS C 284 1 13
HELIX 66 66 ASP C 293 SER C 297 5 5
HELIX 67 67 MET C 313 LYS C 321 1 9
HELIX 68 68 TRP C 339 MET C 345 1 7
HELIX 69 69 ASP C 355 SER C 366 1 12
HELIX 70 70 SER C 366 ASN C 371 1 6
HELIX 71 71 PRO C 373 GLU C 375 5 3
HELIX 72 72 LEU C 376 GLY C 386 1 11
HELIX 73 73 ASP C 390 PHE C 407 1 18
HELIX 74 74 PHE C 407 ALA C 421 1 15
HELIX 75 75 GLY C 450 PHE C 457 1 8
HELIX 76 76 GLY C 458 LEU C 462 5 5
HELIX 77 77 PRO C 467 GLY C 488 1 22
HELIX 78 78 LYS C 521 LEU C 532 1 12
HELIX 79 79 LEU D 43 ARG D 47 5 5
HELIX 80 80 ASP D 73 THR D 85 1 13
HELIX 81 81 GLY D 131 TYR D 135 5 5
HELIX 82 82 GLY D 137 ASN D 145 1 9
HELIX 83 83 LEU D 155 PHE D 161 1 7
HELIX 84 84 ASN D 171 ILE D 188 1 18
HELIX 85 85 ALA D 189 PHE D 191 5 3
HELIX 86 86 SER D 204 SER D 216 1 13
HELIX 87 87 PRO D 217 LYS D 220 5 4
HELIX 88 88 PHE D 234 GLY D 237 5 4
HELIX 89 89 MET D 243 GLY D 255 1 13
HELIX 90 90 THR D 260 LYS D 271 1 12
HELIX 91 91 SER D 272 LYS D 284 1 13
HELIX 92 92 ASP D 293 SER D 297 5 5
HELIX 93 93 MET D 313 LYS D 321 1 9
HELIX 94 94 TRP D 339 MET D 345 1 7
HELIX 95 95 ASP D 355 SER D 366 1 12
HELIX 96 96 SER D 366 ASN D 371 1 6
HELIX 97 97 PRO D 373 GLU D 375 5 3
HELIX 98 98 LEU D 376 GLY D 386 1 11
HELIX 99 99 ASP D 390 PHE D 407 1 18
HELIX 100 100 PHE D 407 ALA D 421 1 15
HELIX 101 101 GLY D 450 PHE D 457 1 8
HELIX 102 102 GLY D 458 LEU D 462 5 5
HELIX 103 103 PRO D 467 GLY D 488 1 22
HELIX 104 104 LYS D 521 LEU D 532 1 12
HELIX 105 105 LEU E 43 ARG E 47 5 5
HELIX 106 106 ASP E 73 THR E 85 1 13
HELIX 107 107 GLY E 131 TYR E 135 5 5
HELIX 108 108 GLY E 137 ASN E 145 1 9
HELIX 109 109 LEU E 155 PHE E 161 1 7
HELIX 110 110 ASN E 171 ILE E 188 1 18
HELIX 111 111 ALA E 189 PHE E 191 5 3
HELIX 112 112 SER E 204 SER E 216 1 13
HELIX 113 113 PRO E 217 LYS E 220 5 4
HELIX 114 114 PHE E 234 GLY E 237 5 4
HELIX 115 115 MET E 243 GLY E 255 1 13
HELIX 116 116 THR E 260 LYS E 271 1 12
HELIX 117 117 SER E 272 LYS E 284 1 13
HELIX 118 118 ASP E 293 SER E 297 5 5
HELIX 119 119 MET E 313 LYS E 321 1 9
HELIX 120 120 TRP E 339 MET E 345 1 7
HELIX 121 121 ASP E 355 SER E 366 1 12
HELIX 122 122 SER E 366 ASN E 371 1 6
HELIX 123 123 PRO E 373 GLU E 375 5 3
HELIX 124 124 LEU E 376 GLY E 386 1 11
HELIX 125 125 ASP E 390 PHE E 407 1 18
HELIX 126 126 PHE E 407 ALA E 421 1 15
HELIX 127 127 GLY E 450 PHE E 457 1 8
HELIX 128 128 GLY E 458 LEU E 462 5 5
HELIX 129 129 PRO E 467 GLY E 488 1 22
HELIX 130 130 LYS E 521 LEU E 532 1 12
HELIX 131 131 LEU F 43 ARG F 47 5 5
HELIX 132 132 ASP F 73 THR F 85 1 13
HELIX 133 133 GLY F 131 TYR F 135 5 5
HELIX 134 134 GLY F 137 ASN F 145 1 9
HELIX 135 135 LEU F 155 PHE F 161 1 7
HELIX 136 136 ASN F 171 ILE F 188 1 18
HELIX 137 137 ALA F 189 PHE F 191 5 3
HELIX 138 138 SER F 204 SER F 216 1 13
HELIX 139 139 PRO F 217 LYS F 220 5 4
HELIX 140 140 PHE F 234 GLY F 237 5 4
HELIX 141 141 MET F 243 GLY F 255 1 13
HELIX 142 142 THR F 260 LYS F 271 1 12
HELIX 143 143 SER F 272 LYS F 284 1 13
HELIX 144 144 ASP F 293 SER F 297 5 5
HELIX 145 145 MET F 313 LYS F 321 1 9
HELIX 146 146 TRP F 339 MET F 345 1 7
HELIX 147 147 ASP F 355 SER F 366 1 12
HELIX 148 148 SER F 366 ASN F 371 1 6
HELIX 149 149 PRO F 373 GLU F 375 5 3
HELIX 150 150 LEU F 376 GLY F 386 1 11
HELIX 151 151 ASP F 390 PHE F 407 1 18
HELIX 152 152 PHE F 407 ALA F 421 1 15
HELIX 153 153 GLY F 450 PHE F 457 1 8
HELIX 154 154 GLY F 458 ARG F 463 1 6
HELIX 155 155 PRO F 467 GLY F 488 1 22
HELIX 156 156 LYS F 521 LEU F 532 1 12
SHEET 1 AA 3 VAL A 8 VAL A 9 0
SHEET 2 AA 3 ARG A 15 LEU A 17 -1 O VAL A 16 N VAL A 9
SHEET 3 AA 3 VAL A 60 ASN A 62 1 O LYS A 61 N LEU A 17
SHEET 1 AB11 LYS A 19 SER A 22 0
SHEET 2 AB11 PRO A 29 PRO A 37 -1 O VAL A 30 N VAL A 21
SHEET 3 AB11 TYR A 101 THR A 106 -1 O LEU A 102 N VAL A 36
SHEET 4 AB11 VAL A 147 ILE A 151 -1 O VAL A 148 N TYR A 105
SHEET 5 AB11 LEU A 116 ILE A 122 1 O PRO A 117 N VAL A 147
SHEET 6 AB11 GLY A 193 GLU A 203 1 N ASP A 194 O LEU A 116
SHEET 7 AB11 ARG A 225 GLU A 229 1 O ARG A 225 N ILE A 200
SHEET 8 AB11 TYR A 328 ASN A 333 1 O ILE A 329 N SER A 228
SHEET 9 AB11 THR A 425 GLN A 431 1 O TYR A 426 N VAL A 330
SHEET 10 AB11 GLY A 506 GLY A 511 1 O LEU A 508 N GLU A 429
SHEET 11 AB11 GLN A 515 LYS A 518 -1 O GLN A 515 N GLN A 509
SHEET 1 AC 2 MET A 69 CYS A 70 0
SHEET 2 AC 2 PHE A 95 SER A 96 1 N SER A 96 O MET A 69
SHEET 1 AD 2 VAL A 239 ARG A 240 0
SHEET 2 AD 2 THR A 303 VAL A 304 1 O THR A 303 N ARG A 240
SHEET 1 BA 3 VAL B 8 VAL B 9 0
SHEET 2 BA 3 ARG B 15 LEU B 17 -1 O VAL B 16 N VAL B 9
SHEET 3 BA 3 VAL B 60 ASN B 62 1 O LYS B 61 N LEU B 17
SHEET 1 BB11 LYS B 19 SER B 22 0
SHEET 2 BB11 PRO B 29 PRO B 37 -1 O VAL B 30 N VAL B 21
SHEET 3 BB11 TYR B 101 THR B 106 -1 O LEU B 102 N VAL B 36
SHEET 4 BB11 VAL B 147 ILE B 151 -1 O VAL B 148 N TYR B 105
SHEET 5 BB11 LEU B 116 ILE B 122 1 O PRO B 117 N VAL B 147
SHEET 6 BB11 GLY B 193 GLU B 203 1 N ASP B 194 O LEU B 116
SHEET 7 BB11 ARG B 225 GLU B 229 1 O ARG B 225 N ILE B 200
SHEET 8 BB11 TYR B 328 ASN B 333 1 O ILE B 329 N SER B 228
SHEET 9 BB11 THR B 425 GLN B 431 1 O TYR B 426 N VAL B 330
SHEET 10 BB11 GLY B 506 GLY B 511 1 O LEU B 508 N GLU B 429
SHEET 11 BB11 GLN B 515 LYS B 518 -1 O GLN B 515 N GLN B 509
SHEET 1 BC 2 MET B 69 CYS B 70 0
SHEET 2 BC 2 PHE B 95 SER B 96 1 N SER B 96 O MET B 69
SHEET 1 BD 2 VAL B 239 ARG B 240 0
SHEET 2 BD 2 THR B 303 VAL B 304 1 O THR B 303 N ARG B 240
SHEET 1 CA 3 VAL C 8 VAL C 9 0
SHEET 2 CA 3 ARG C 15 LEU C 17 -1 O VAL C 16 N VAL C 9
SHEET 3 CA 3 VAL C 60 ASN C 62 1 O LYS C 61 N LEU C 17
SHEET 1 CB11 LYS C 19 SER C 22 0
SHEET 2 CB11 PRO C 29 PRO C 37 -1 O VAL C 30 N VAL C 21
SHEET 3 CB11 TYR C 101 THR C 106 -1 O LEU C 102 N VAL C 36
SHEET 4 CB11 VAL C 147 ILE C 151 -1 O VAL C 148 N TYR C 105
SHEET 5 CB11 LEU C 116 ILE C 122 1 O PRO C 117 N VAL C 147
SHEET 6 CB11 GLY C 193 GLU C 203 1 N ASP C 194 O LEU C 116
SHEET 7 CB11 ARG C 225 GLU C 229 1 O ARG C 225 N ILE C 200
SHEET 8 CB11 TYR C 328 ASN C 333 1 O ILE C 329 N SER C 228
SHEET 9 CB11 THR C 425 GLN C 431 1 O TYR C 426 N VAL C 330
SHEET 10 CB11 GLY C 506 GLY C 511 1 O LEU C 508 N GLU C 429
SHEET 11 CB11 GLN C 515 LYS C 518 -1 O GLN C 515 N GLN C 509
SHEET 1 CC 2 MET C 69 CYS C 70 0
SHEET 2 CC 2 PHE C 95 SER C 96 1 N SER C 96 O MET C 69
SHEET 1 CD 2 VAL C 239 ARG C 240 0
SHEET 2 CD 2 THR C 303 VAL C 304 1 O THR C 303 N ARG C 240
SHEET 1 DA 3 VAL D 8 VAL D 9 0
SHEET 2 DA 3 ARG D 15 LEU D 17 -1 O VAL D 16 N VAL D 9
SHEET 3 DA 3 VAL D 60 ASN D 62 1 O LYS D 61 N LEU D 17
SHEET 1 DB11 LYS D 19 SER D 22 0
SHEET 2 DB11 PRO D 29 PRO D 37 -1 O VAL D 30 N VAL D 21
SHEET 3 DB11 TYR D 101 THR D 106 -1 O LEU D 102 N VAL D 36
SHEET 4 DB11 VAL D 147 ILE D 151 -1 O VAL D 148 N TYR D 105
SHEET 5 DB11 LEU D 116 ILE D 122 1 O PRO D 117 N VAL D 147
SHEET 6 DB11 GLY D 193 GLU D 203 1 N ASP D 194 O LEU D 116
SHEET 7 DB11 ARG D 225 GLU D 229 1 O ARG D 225 N ILE D 200
SHEET 8 DB11 TYR D 328 ASN D 333 1 O ILE D 329 N SER D 228
SHEET 9 DB11 THR D 425 GLN D 431 1 O TYR D 426 N VAL D 330
SHEET 10 DB11 GLY D 506 GLY D 511 1 O LEU D 508 N GLU D 429
SHEET 11 DB11 GLN D 515 LYS D 518 -1 O GLN D 515 N GLN D 509
SHEET 1 DC 2 MET D 69 CYS D 70 0
SHEET 2 DC 2 PHE D 95 SER D 96 1 N SER D 96 O MET D 69
SHEET 1 DD 2 VAL D 239 ARG D 240 0
SHEET 2 DD 2 THR D 303 VAL D 304 1 O THR D 303 N ARG D 240
SHEET 1 EA 3 VAL E 8 VAL E 9 0
SHEET 2 EA 3 ARG E 15 LEU E 17 -1 O VAL E 16 N VAL E 9
SHEET 3 EA 3 VAL E 60 ASN E 62 1 O LYS E 61 N LEU E 17
SHEET 1 EB11 LYS E 19 SER E 22 0
SHEET 2 EB11 PRO E 29 PRO E 37 -1 O VAL E 30 N VAL E 21
SHEET 3 EB11 TYR E 101 THR E 106 -1 O LEU E 102 N VAL E 36
SHEET 4 EB11 VAL E 147 ILE E 151 -1 O VAL E 148 N TYR E 105
SHEET 5 EB11 LEU E 116 ILE E 122 1 O PRO E 117 N VAL E 147
SHEET 6 EB11 GLY E 193 GLU E 203 1 N ASP E 194 O LEU E 116
SHEET 7 EB11 ARG E 225 GLU E 229 1 O ARG E 225 N ILE E 200
SHEET 8 EB11 TYR E 328 ASN E 333 1 O ILE E 329 N SER E 228
SHEET 9 EB11 THR E 425 GLN E 431 1 O TYR E 426 N VAL E 330
SHEET 10 EB11 GLY E 506 GLY E 511 1 O LEU E 508 N GLU E 429
SHEET 11 EB11 GLN E 515 LYS E 518 -1 O GLN E 515 N GLN E 509
SHEET 1 EC 2 MET E 69 CYS E 70 0
SHEET 2 EC 2 PHE E 95 SER E 96 1 N SER E 96 O MET E 69
SHEET 1 ED 2 VAL E 239 ARG E 240 0
SHEET 2 ED 2 THR E 303 VAL E 304 1 O THR E 303 N ARG E 240
SHEET 1 FA 3 VAL F 8 VAL F 9 0
SHEET 2 FA 3 ARG F 15 LEU F 17 -1 O VAL F 16 N VAL F 9
SHEET 3 FA 3 VAL F 60 ASN F 62 1 O LYS F 61 N LEU F 17
SHEET 1 FB11 LYS F 19 SER F 22 0
SHEET 2 FB11 PRO F 29 PRO F 37 -1 O VAL F 30 N VAL F 21
SHEET 3 FB11 TYR F 101 THR F 106 -1 O LEU F 102 N VAL F 36
SHEET 4 FB11 VAL F 147 ILE F 151 -1 O VAL F 148 N TYR F 105
SHEET 5 FB11 LEU F 116 ILE F 122 1 O PRO F 117 N VAL F 147
SHEET 6 FB11 GLY F 193 GLU F 203 1 N ASP F 194 O LEU F 116
SHEET 7 FB11 ARG F 225 GLU F 229 1 O ARG F 225 N ILE F 200
SHEET 8 FB11 TYR F 328 ASN F 333 1 O ILE F 329 N SER F 228
SHEET 9 FB11 THR F 425 GLN F 431 1 O TYR F 426 N VAL F 330
SHEET 10 FB11 GLY F 506 GLY F 511 1 O LEU F 508 N GLU F 429
SHEET 11 FB11 GLN F 515 LYS F 518 -1 O GLN F 515 N GLN F 509
SHEET 1 FC 2 MET F 69 CYS F 70 0
SHEET 2 FC 2 PHE F 95 SER F 96 1 N SER F 96 O MET F 69
SHEET 1 FD 2 VAL F 239 ARG F 240 0
SHEET 2 FD 2 THR F 303 VAL F 304 1 O THR F 303 N ARG F 240
SSBOND 1 CYS A 70 CYS A 99 1555 1555 1.99
SSBOND 2 CYS A 256 CYS A 267 1555 1555 2.17
SSBOND 3 CYS B 70 CYS B 99 1555 1555 1.98
SSBOND 4 CYS B 256 CYS B 267 1555 1555 2.13
SSBOND 5 CYS C 70 CYS C 99 1555 1555 1.99
SSBOND 6 CYS C 256 CYS C 267 1555 1555 2.15
SSBOND 7 CYS D 70 CYS D 99 1555 1555 1.99
SSBOND 8 CYS D 256 CYS D 267 1555 1555 2.18
SSBOND 9 CYS E 70 CYS E 99 1555 1555 1.99
SSBOND 10 CYS E 256 CYS E 267 1555 1555 2.14
SSBOND 11 CYS F 70 CYS F 99 1555 1555 1.98
SSBOND 12 CYS F 256 CYS F 267 1555 1555 2.19
CRYST1 92.860 188.020 109.500 90.00 96.44 90.00 P 1 21 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010769 0.000000 0.001216 0.00000
SCALE2 0.000000 0.005319 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009190 0.00000
MTRIX1 1 -0.974020 -0.222240 0.043530 9.26110 1
MTRIX2 1 -0.226290 0.947660 -0.225250 41.37080 1
MTRIX3 1 0.008810 -0.229250 -0.973330 197.43523 1
MTRIX1 2 -0.970090 -0.242510 0.010780 11.23982 1
MTRIX2 2 0.106610 -0.465500 -0.878610 261.74030 1
MTRIX3 2 0.218090 -0.851180 0.477420 140.72946 1
MTRIX1 3 -0.999360 0.008690 0.034720 -37.88942 1
MTRIX2 3 0.030940 -0.278090 0.960060 64.84949 1
MTRIX3 3 0.018000 0.960520 0.277640 -59.24981 1
MTRIX1 4 0.982740 0.084070 -0.164760 17.75239 1
MTRIX2 4 -0.060960 -0.693790 -0.717590 275.16031 1
MTRIX3 4 -0.174630 0.715250 -0.676690 70.20776 1
MTRIX1 5 0.972270 0.038490 -0.230660 39.43866 1
MTRIX2 5 0.217440 -0.511760 0.831160 119.08277 1
MTRIX3 5 -0.086050 -0.858270 -0.505940 240.81943 1
TER 4096 LYS A 534
TER 8192 LYS B 534
TER 12288 LYS C 534
TER 16384 LYS D 534
TER 20480 LYS E 534
TER 24576 LYS F 534
MASTER 609 0 0 156 108 0 0 2125087 6 24 252
END |