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HEADER HYDROLASE 09-AUG-04 1VLQ
TITLE CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM
TITLE 2 THERMOTOGA MARITIMA AT 2.10 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 EC: 3.1.1.41;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA MSB8;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: TM0077;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TM0077, ACETYL XYLAN ESTERASE, STRUCTURAL GENOMICS, JCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS
REVDAT 1 24-AUG-04 1VLQ 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS
JRNL TITL CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE
JRNL TITL 2 (TM0077) FROM THERMOTOGA MARITIMA AT 2.10 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 278371
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 14726
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13660
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 727
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 33653
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.71000
REMARK 3 B22 (A**2) : 2.25000
REMARK 3 B33 (A**2) : -1.33000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.82000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.076
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
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): 32148 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 28509 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 43596 ; 1.477 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 66214 ; 0.927 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3852 ; 6.308 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1585 ;30.549 ;23.073
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5085 ;14.046 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 225 ;17.373 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4439 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 36073 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 7284 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6254 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 28475 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 15311 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 16852 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2055 ; 0.163 ; 0.200
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): 10 ; 0.214 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 65 ; 0.333 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.209 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 20879 ; 2.176 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7800 ; 0.198 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31023 ; 2.593 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 14761 ; 4.775 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12573 ; 6.035 ;11.000
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 I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 4 A 320 2
REMARK 3 1 B 4 B 320 2
REMARK 3 1 C 4 C 320 2
REMARK 3 1 D 4 D 320 2
REMARK 3 1 E 4 E 320 2
REMARK 3 1 F 4 F 320 2
REMARK 3 1 G 4 G 320 2
REMARK 3 1 H 4 H 320 2
REMARK 3 1 I 4 I 320 2
REMARK 3 1 J 4 J 320 2
REMARK 3 1 K 4 K 320 2
REMARK 3 1 L 4 L 320 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 F (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 G (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 H (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 I (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 J (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 K (A): 1852 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 L (A): 1852 ; 0.04 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2980 ; 0.26 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2980 ; 0.21 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2980 ; 0.22 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 2980 ; 0.21 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 E (A): 2980 ; 0.24 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 F (A): 2980 ; 0.22 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 G (A): 2980 ; 0.21 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 H (A): 2980 ; 0.21 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 I (A): 2980 ; 0.22 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 J (A): 2980 ; 0.27 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 K (A): 2980 ; 0.30 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 L (A): 2980 ; 0.27 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 1852 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1852 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1852 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1852 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 1852 ; 0.15 ; 0.50
REMARK 3 TIGHT THERMAL 1 F (A**2): 1852 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 G (A**2): 1852 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 H (A**2): 1852 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 1 I (A**2): 1852 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 J (A**2): 1852 ; 0.18 ; 0.50
REMARK 3 TIGHT THERMAL 1 K (A**2): 1852 ; 0.18 ; 0.50
REMARK 3 TIGHT THERMAL 1 L (A**2): 1852 ; 0.20 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2980 ; 0.98 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2980 ; 1.02 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2980 ; 1.05 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 2980 ; 0.92 ; 2.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 2980 ; 0.96 ; 2.00
REMARK 3 MEDIUM THERMAL 1 F (A**2): 2980 ; 0.90 ; 2.00
REMARK 3 MEDIUM THERMAL 1 G (A**2): 2980 ; 0.95 ; 2.00
REMARK 3 MEDIUM THERMAL 1 H (A**2): 2980 ; 1.02 ; 2.00
REMARK 3 MEDIUM THERMAL 1 I (A**2): 2980 ; 0.91 ; 2.00
REMARK 3 MEDIUM THERMAL 1 J (A**2): 2980 ; 1.01 ; 2.00
REMARK 3 MEDIUM THERMAL 1 K (A**2): 2980 ; 1.07 ; 2.00
REMARK 3 MEDIUM THERMAL 1 L (A**2): 2980 ; 1.10 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS 2. THE ACTIVE SITE TRIAD CONSISTS OF SER188,
REMARK 3 HIS303 AND ASP274. THE ELECTRON DENSITY SUGGESTED THERE COULD
REMARK 3 EXIST A PARTIALLY OCCUPIED ACYL INTERMEDIATE ON SER188.
REMARK 3 HOWEVER, IT IS NOT CONCLUSIVE. AS A RESULT, WATER MOLECULES
REMARK 3 WERE MODELLED. 3. THERE IS SOME UNEXPLAINED DENSITY NEAR N-
REMARK 3 TERMINUS 4. RESIDUES 134,135 OF CHAIN D,H,I,J,K,L HAVE POOR
REMARK 3 DENSITY
REMARK 4
REMARK 4 1VLQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-2004.
REMARK 100 THE RCSB ID CODE IS RCSB001990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SSRL ; SSRL
REMARK 200 BEAMLINE : 9-2; 9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918370; 0.918370,0.979126
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : QUANTUM-315 CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA(CCP4 4.2)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 293140
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.43300
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP/AUTOSHARP, SHELX, WARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-300, 10% GLYCEROL, 0.1M
REMARK 280 PHOSPHATE-CITRATE PH 4.2 0.2 M (NH4)2SO4 4.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP,NANODROP, TEMPERATURE 293K
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,1/2+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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 65.47600
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
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 12CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 MSE A -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 324
REMARK 465 GLY A 325
REMARK 465 MSE B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 324
REMARK 465 GLY B 325
REMARK 465 MSE C -11
REMARK 465 GLY C -10
REMARK 465 SER C -9
REMARK 465 ASP C -8
REMARK 465 LYS C -7
REMARK 465 ILE C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MSE C 1
REMARK 465 LYS C 324
REMARK 465 GLY C 325
REMARK 465 MSE D -11
REMARK 465 GLY D -10
REMARK 465 SER D -9
REMARK 465 ASP D -8
REMARK 465 LYS D -7
REMARK 465 ILE D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MSE D 1
REMARK 465 LYS D 324
REMARK 465 GLY D 325
REMARK 465 MSE E -11
REMARK 465 GLY E -10
REMARK 465 SER E -9
REMARK 465 ASP E -8
REMARK 465 LYS E -7
REMARK 465 ILE E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 HIS E 0
REMARK 465 MSE E 1
REMARK 465 LYS E 324
REMARK 465 GLY E 325
REMARK 465 MSE F -11
REMARK 465 GLY F -10
REMARK 465 SER F -9
REMARK 465 ASP F -8
REMARK 465 LYS F -7
REMARK 465 ILE F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 HIS F -1
REMARK 465 HIS F 0
REMARK 465 MSE F 1
REMARK 465 LYS F 324
REMARK 465 GLY F 325
REMARK 465 MSE G -11
REMARK 465 GLY G -10
REMARK 465 SER G -9
REMARK 465 ASP G -8
REMARK 465 LYS G -7
REMARK 465 ILE G -6
REMARK 465 HIS G -5
REMARK 465 HIS G -4
REMARK 465 HIS G -3
REMARK 465 HIS G -2
REMARK 465 HIS G -1
REMARK 465 HIS G 0
REMARK 465 MSE G 1
REMARK 465 LYS G 324
REMARK 465 GLY G 325
REMARK 465 MSE H -11
REMARK 465 GLY H -10
REMARK 465 SER H -9
REMARK 465 ASP H -8
REMARK 465 LYS H -7
REMARK 465 ILE H -6
REMARK 465 HIS H -5
REMARK 465 HIS H -4
REMARK 465 HIS H -3
REMARK 465 HIS H -2
REMARK 465 HIS H -1
REMARK 465 HIS H 0
REMARK 465 MSE H 1
REMARK 465 LYS H 324
REMARK 465 GLY H 325
REMARK 465 MSE I -11
REMARK 465 GLY I -10
REMARK 465 SER I -9
REMARK 465 ASP I -8
REMARK 465 LYS I -7
REMARK 465 ILE I -6
REMARK 465 HIS I -5
REMARK 465 HIS I -4
REMARK 465 HIS I -3
REMARK 465 HIS I -2
REMARK 465 HIS I -1
REMARK 465 HIS I 0
REMARK 465 MSE I 1
REMARK 465 LYS I 324
REMARK 465 GLY I 325
REMARK 465 MSE J -11
REMARK 465 GLY J -10
REMARK 465 SER J -9
REMARK 465 ASP J -8
REMARK 465 LYS J -7
REMARK 465 ILE J -6
REMARK 465 HIS J -5
REMARK 465 HIS J -4
REMARK 465 HIS J -3
REMARK 465 HIS J -2
REMARK 465 HIS J -1
REMARK 465 HIS J 0
REMARK 465 MSE J 1
REMARK 465 LYS J 324
REMARK 465 GLY J 325
REMARK 465 MSE K -11
REMARK 465 GLY K -10
REMARK 465 SER K -9
REMARK 465 ASP K -8
REMARK 465 LYS K -7
REMARK 465 ILE K -6
REMARK 465 HIS K -5
REMARK 465 HIS K -4
REMARK 465 HIS K -3
REMARK 465 HIS K -2
REMARK 465 HIS K -1
REMARK 465 HIS K 0
REMARK 465 MSE K 1
REMARK 465 LYS K 324
REMARK 465 GLY K 325
REMARK 465 MSE L -11
REMARK 465 GLY L -10
REMARK 465 SER L -9
REMARK 465 ASP L -8
REMARK 465 LYS L -7
REMARK 465 ILE L -6
REMARK 465 HIS L -5
REMARK 465 HIS L -4
REMARK 465 HIS L -3
REMARK 465 HIS L -2
REMARK 465 HIS L -1
REMARK 465 HIS L 0
REMARK 465 MSE L 1
REMARK 465 LYS L 324
REMARK 465 GLY L 325
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 9 CG CD OE1 OE2
REMARK 470 LYS A 22 NZ
REMARK 470 GLU A 81 CD OE1 OE2
REMARK 470 GLU B 9 CD OE1 OE2
REMARK 470 GLU B 17 CD OE1 OE2
REMARK 470 LYS B 22 CD CE NZ
REMARK 470 GLU B 79 CG CD OE1 OE2
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 GLN B 222 CD OE1 NE2
REMARK 470 LYS C 22 CD CE NZ
REMARK 470 LYS C 126 CE NZ
REMARK 470 ARG C 153 NE CZ NH1 NH2
REMARK 470 LYS D 22 CD CE NZ
REMARK 470 GLU D 48 CD OE1 OE2
REMARK 470 GLU D 79 CB CG CD OE1 OE2
REMARK 470 LYS D 126 CE NZ
REMARK 470 ARG D 153 NE CZ NH1 NH2
REMARK 470 GLU E 9 CD OE1 OE2
REMARK 470 LYS E 22 CD CE NZ
REMARK 470 GLU F 9 CG CD OE1 OE2
REMARK 470 LYS F 22 CD CE NZ
REMARK 470 GLU F 81 CG CD OE1 OE2
REMARK 470 LYS F 126 CE NZ
REMARK 470 LYS G 22 CD CE NZ
REMARK 470 GLU G 79 CD OE1 OE2
REMARK 470 LYS G 126 CE NZ
REMARK 470 GLU H 9 CD OE1 OE2
REMARK 470 LYS H 22 CD CE NZ
REMARK 470 GLU I 30 CD OE1 OE2
REMARK 470 GLU I 48 CD OE1 OE2
REMARK 470 GLU I 79 CD OE1 OE2
REMARK 470 LYS J 22 CG CD CE NZ
REMARK 470 GLU J 30 CD OE1 OE2
REMARK 470 GLU J 79 CG CD OE1 OE2
REMARK 470 ARG J 153 NE CZ NH1 NH2
REMARK 470 GLU K 9 CG CD OE1 OE2
REMARK 470 LYS K 22 NZ
REMARK 470 GLU K 79 CD OE1 OE2
REMARK 470 LYS K 202 CE NZ
REMARK 470 LYS L 126 CE NZ
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
REMARK 500 OH TYR H 19 OE2 GLU H 21 2.13
REMARK 500 OE1 GLN H 176 O HOH 2005 2.16
REMARK 500 O HOH 604 O HOH 1162 2.16
REMARK 500 O HOH 2256 O HOH 2304 2.18
REMARK 500 OE1 GLU A 34 O HOH 2381 2.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 164 CA ALA A 164 CB -0.109
REMARK 500 ASN E 302 CB ASN E 302 CG 0.099
REMARK 500 VAL E 315 CB VAL E 315 CG1 0.135
REMARK 500 LEU G 51 CG LEU G 51 CD2 0.097
REMARK 500 ALA G 164 CA ALA G 164 CB -0.110
REMARK 500 ASN L 302 CB ASN L 302 CG 0.099
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY D 135 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 LYS J 237 CD - CE - NZ ANGL. DEV. = 10.7 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 188 -119.51 56.91
REMARK 500 SER B 188 -117.62 57.15
REMARK 500 SER C 188 -116.39 58.87
REMARK 500 SER D 188 -119.48 60.26
REMARK 500 SER E 188 -116.21 56.34
REMARK 500 SER F 188 -117.96 58.20
REMARK 500 SER G 188 -119.03 62.47
REMARK 500 SER H 188 -118.45 56.48
REMARK 500 SER J 188 -116.46 59.73
REMARK 500 SER K 188 -118.08 56.72
REMARK 500 SER L 188 -119.57 56.64
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 ALA C 2 PHE C 3 149.36
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 1555 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH 1910 DISTANCE = 6.08 ANGSTROMS
DBREF 1VLQ A 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ B 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ C 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ D 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ E 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ F 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ G 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ H 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ I 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ J 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ K 1 325 GB 15642852 NP_227893 1 325
DBREF 1VLQ L 1 325 GB 15642852 NP_227893 1 325
SEQADV 1VLQ MSE A -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY A -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER A -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP A -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS A -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE A -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS A -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS A -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS A -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS A -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS A -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS A 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE A 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE A 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE A 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE A 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE A 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE A 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE B -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY B -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER B -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP B -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS B -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE B -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS B -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS B -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS B -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS B -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS B -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS B 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE B 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE B 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE B 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE B 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE B 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE B 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE C -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY C -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER C -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP C -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS C -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE C -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS C -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS C -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS C -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS C -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS C -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS C 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE C 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE C 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE C 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE C 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE C 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE C 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE D -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY D -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER D -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP D -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS D -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE D -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS D -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS D -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS D -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS D -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS D -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS D 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE D 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE D 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE D 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE D 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE D 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE D 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE E -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY E -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER E -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP E -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS E -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE E -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS E -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS E -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS E -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS E -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS E -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS E 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE E 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE E 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE E 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE E 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE E 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE E 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE F -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY F -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER F -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP F -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS F -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE F -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS F -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS F -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS F -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS F -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS F -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS F 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE F 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE F 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE F 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE F 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE F 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE F 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE G -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY G -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER G -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP G -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS G -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE G -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS G -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS G -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS G -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS G -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS G -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS G 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE G 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE G 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE G 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE G 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE G 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE G 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE H -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY H -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER H -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP H -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS H -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE H -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS H -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS H -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS H -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS H -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS H -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS H 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE H 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE H 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE H 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE H 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE H 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE H 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE I -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY I -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER I -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP I -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS I -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE I -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS I -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS I -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS I -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS I -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS I -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS I 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE I 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE I 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE I 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE I 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE I 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE I 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE J -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY J -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER J -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP J -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS J -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE J -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS J -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS J -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS J -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS J -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS J -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS J 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE J 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE J 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE J 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE J 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE J 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE J 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE K -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY K -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER K -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP K -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS K -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE K -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS K -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS K -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS K -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS K -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS K -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS K 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE K 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE K 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE K 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE K 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE K 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE K 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQADV 1VLQ MSE L -11 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ GLY L -10 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ SER L -9 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ASP L -8 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ LYS L -7 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ ILE L -6 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS L -5 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS L -4 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS L -3 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS L -2 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS L -1 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ HIS L 0 GB 15642852 LEADER SEQUENCE
SEQADV 1VLQ MSE L 1 GB 15642852 MET 1 MODIFIED RESIDUE
SEQADV 1VLQ MSE L 47 GB 15642852 MET 47 MODIFIED RESIDUE
SEQADV 1VLQ MSE L 108 GB 15642852 MET 108 MODIFIED RESIDUE
SEQADV 1VLQ MSE L 115 GB 15642852 MET 115 MODIFIED RESIDUE
SEQADV 1VLQ MSE L 145 GB 15642852 MET 145 MODIFIED RESIDUE
SEQADV 1VLQ MSE L 273 GB 15642852 MET 273 MODIFIED RESIDUE
SEQRES 1 A 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 A 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 A 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 A 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 A 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 A 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 A 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 A 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 A 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 A 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 A 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 A 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 A 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 A 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 A 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 A 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 A 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 A 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 A 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 A 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 A 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 A 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 A 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 A 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 A 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 B 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 B 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 B 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 B 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 B 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 B 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 B 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 B 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 B 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 B 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 B 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 B 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 B 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 B 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 B 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 B 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 B 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 B 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 B 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 B 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 B 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 B 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 B 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 B 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 B 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 B 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 C 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 C 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 C 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 C 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 C 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 C 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 C 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 C 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 C 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 C 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 C 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 C 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 C 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 C 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 C 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 C 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 C 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 C 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 C 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 C 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 C 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 C 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 C 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 C 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 C 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 C 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 D 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 D 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 D 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 D 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 D 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 D 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 D 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 D 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 D 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 D 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 D 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 D 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 D 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 D 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 D 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 D 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 D 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 D 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 D 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 D 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 D 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 D 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 D 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 D 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 D 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 D 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 E 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 E 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 E 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 E 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 E 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 E 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 E 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 E 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 E 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 E 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 E 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 E 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 E 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 E 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 E 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 E 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 E 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 E 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 E 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 E 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 E 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 E 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 E 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 E 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 E 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 E 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 F 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 F 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 F 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 F 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 F 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 F 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 F 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 F 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 F 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 F 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 F 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 F 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 F 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 F 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 F 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 F 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 F 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 F 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 F 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 F 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 F 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 F 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 F 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 F 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 F 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 F 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 G 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 G 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 G 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 G 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 G 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 G 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 G 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 G 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 G 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 G 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 G 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 G 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 G 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 G 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 G 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 G 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 G 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 G 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 G 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 G 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 G 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 G 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 G 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 G 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 G 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 G 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 H 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 H 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 H 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 H 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 H 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 H 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 H 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 H 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 H 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 H 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 H 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 H 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 H 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 H 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 H 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 H 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 H 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 H 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 H 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 H 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 H 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 H 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 H 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 H 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 H 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 H 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 I 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 I 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 I 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 I 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 I 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 I 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 I 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 I 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 I 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 I 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 I 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 I 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 I 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 I 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 I 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 I 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 I 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 I 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 I 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 I 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 I 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 I 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 I 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 I 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 I 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 I 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 J 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 J 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 J 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 J 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 J 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 J 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 J 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 J 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 J 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 J 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 J 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 J 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 J 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 J 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 J 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 J 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 J 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 J 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 J 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 J 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 J 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 J 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 J 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 J 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 J 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 J 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 K 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 K 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 K 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 K 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 K 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 K 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 K 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 K 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 K 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 K 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 K 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 K 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 K 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 K 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 K 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 K 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 K 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 K 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 K 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 K 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 K 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 K 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 K 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 K 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 K 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 K 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 L 337 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 L 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 L 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 L 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 L 337 ASP PRO VAL PHE GLU ARG MSE GLU SER HIS LEU LYS THR
SEQRES 6 L 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 L 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 L 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 L 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 L 337 PRO SER MSE GLY TYR ILE CYS PHE VAL MSE ASP THR ARG
SEQRES 11 L 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 L 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 L 337 MSE THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 L 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 L 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 L 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 L 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 L 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 L 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 L 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 L 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 L 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MSE ASP
SEQRES 23 L 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 L 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 L 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 L 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
MODRES 1VLQ MSE A 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE A 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE A 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE A 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE A 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE B 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE B 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE B 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE B 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE B 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE C 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE C 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE C 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE C 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE C 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE D 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE D 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE D 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE D 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE D 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE E 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE E 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE E 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE E 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE E 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE F 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE F 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE F 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE F 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE F 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE G 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE G 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE G 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE G 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE G 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE H 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE H 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE H 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE H 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE H 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE I 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE I 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE I 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE I 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE I 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE J 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE J 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE J 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE J 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE J 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE K 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE K 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE K 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE K 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE K 273 MET SELENOMETHIONINE
MODRES 1VLQ MSE L 47 MET SELENOMETHIONINE
MODRES 1VLQ MSE L 108 MET SELENOMETHIONINE
MODRES 1VLQ MSE L 115 MET SELENOMETHIONINE
MODRES 1VLQ MSE L 145 MET SELENOMETHIONINE
MODRES 1VLQ MSE L 273 MET SELENOMETHIONINE
HET MSE A 47 8
HET MSE A 108 8
HET MSE A 115 8
HET MSE A 145 8
HET MSE A 273 8
HET MSE B 47 8
HET MSE B 108 8
HET MSE B 115 8
HET MSE B 145 8
HET MSE B 273 8
HET MSE C 47 8
HET MSE C 108 8
HET MSE C 115 8
HET MSE C 145 8
HET MSE C 273 8
HET MSE D 47 8
HET MSE D 108 8
HET MSE D 115 8
HET MSE D 145 8
HET MSE D 273 8
HET MSE E 47 8
HET MSE E 108 8
HET MSE E 115 8
HET MSE E 145 8
HET MSE E 273 8
HET MSE F 47 8
HET MSE F 108 8
HET MSE F 115 8
HET MSE F 145 8
HET MSE F 273 8
HET MSE G 47 8
HET MSE G 108 8
HET MSE G 115 8
HET MSE G 145 8
HET MSE G 273 8
HET MSE H 47 8
HET MSE H 108 8
HET MSE H 115 8
HET MSE H 145 8
HET MSE H 273 8
HET MSE I 47 8
HET MSE I 108 8
HET MSE I 115 8
HET MSE I 145 8
HET MSE I 273 8
HET MSE J 47 8
HET MSE J 108 8
HET MSE J 115 8
HET MSE J 145 8
HET MSE J 273 8
HET MSE K 47 8
HET MSE K 108 8
HET MSE K 115 8
HET MSE K 145 8
HET MSE K 273 8
HET MSE L 47 8
HET MSE L 108 8
HET MSE L 115 8
HET MSE L 145 8
HET MSE L 273 8
HET GOL 1 6
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
FORMUL 1 MSE 60(C5 H11 N1 O2 SE1)
FORMUL 13 GOL C3 H8 O3
FORMUL 14 HOH *2464(H2 O1)
HELIX 1 1 PRO A 7 LYS A 12 1 6
HELIX 2 2 ASP A 23 LYS A 37 1 15
HELIX 3 3 TYR A 64 GLY A 66 5 3
HELIX 4 4 PHE A 98 TRP A 102 5 5
HELIX 5 5 LEU A 103 MSE A 108 1 6
HELIX 6 6 TYR A 155 SER A 173 1 19
HELIX 7 7 SER A 188 SER A 201 1 14
HELIX 8 8 HIS A 216 VAL A 224 1 9
HELIX 9 9 PRO A 228 HIS A 239 1 12
HELIX 10 10 LYS A 242 TYR A 252 1 11
HELIX 11 11 ASP A 254 ALA A 260 1 7
HELIX 12 12 PRO A 278 TYR A 289 1 12
HELIX 13 13 GLY A 306 GLU A 323 1 18
HELIX 14 14 PRO B 7 LYS B 12 1 6
HELIX 15 15 ASP B 23 LYS B 37 1 15
HELIX 16 16 TYR B 64 GLY B 66 5 3
HELIX 17 17 PHE B 98 TRP B 102 5 5
HELIX 18 18 LEU B 103 MSE B 108 1 6
HELIX 19 19 ASP B 151 THR B 154 5 4
HELIX 20 20 TYR B 155 SER B 173 1 19
HELIX 21 21 SER B 188 SER B 201 1 14
HELIX 22 22 HIS B 216 VAL B 224 1 9
HELIX 23 23 PRO B 228 HIS B 239 1 12
HELIX 24 24 LYS B 242 TYR B 252 1 11
HELIX 25 25 ASP B 254 ALA B 260 1 7
HELIX 26 26 PRO B 278 TYR B 289 1 12
HELIX 27 27 GLY B 306 PHE B 322 1 17
HELIX 28 28 PRO C 7 LYS C 12 1 6
HELIX 29 29 ASP C 23 LYS C 37 1 15
HELIX 30 30 TYR C 64 GLY C 66 5 3
HELIX 31 31 PHE C 98 TRP C 102 5 5
HELIX 32 32 LEU C 103 MSE C 108 1 6
HELIX 33 33 ASP C 151 THR C 154 5 4
HELIX 34 34 TYR C 155 SER C 173 1 19
HELIX 35 35 SER C 188 SER C 201 1 14
HELIX 36 36 HIS C 216 VAL C 224 1 9
HELIX 37 37 TYR C 229 HIS C 239 1 11
HELIX 38 38 LYS C 242 TYR C 252 1 11
HELIX 39 39 ASP C 254 ALA C 260 1 7
HELIX 40 40 PRO C 278 TYR C 289 1 12
HELIX 41 41 GLY C 306 PHE C 322 1 17
HELIX 42 42 PRO D 7 LYS D 12 1 6
HELIX 43 43 ASP D 23 LYS D 37 1 15
HELIX 44 44 TYR D 64 GLY D 66 5 3
HELIX 45 45 PHE D 98 TRP D 102 5 5
HELIX 46 46 LEU D 103 MSE D 108 1 6
HELIX 47 47 TYR D 155 SER D 173 1 19
HELIX 48 48 SER D 188 SER D 201 1 14
HELIX 49 49 HIS D 216 VAL D 224 1 9
HELIX 50 50 PRO D 228 HIS D 239 1 12
HELIX 51 51 LYS D 242 TYR D 252 1 11
HELIX 52 52 ASP D 254 ALA D 260 1 7
HELIX 53 53 PRO D 278 TYR D 289 1 12
HELIX 54 54 GLY D 306 GLU D 323 1 18
HELIX 55 55 PRO E 7 LYS E 12 1 6
HELIX 56 56 ASP E 23 LYS E 37 1 15
HELIX 57 57 TYR E 64 GLY E 66 5 3
HELIX 58 58 PHE E 98 TRP E 102 5 5
HELIX 59 59 LEU E 103 MSE E 108 1 6
HELIX 60 60 ASP E 151 THR E 154 5 4
HELIX 61 61 TYR E 155 SER E 173 1 19
HELIX 62 62 SER E 188 SER E 201 1 14
HELIX 63 63 HIS E 216 VAL E 224 1 9
HELIX 64 64 PRO E 228 HIS E 239 1 12
HELIX 65 65 LYS E 242 TYR E 252 1 11
HELIX 66 66 ASP E 254 ALA E 260 1 7
HELIX 67 67 PRO E 278 TYR E 289 1 12
HELIX 68 68 GLY E 306 GLU E 323 1 18
HELIX 69 69 PRO F 7 LYS F 12 1 6
HELIX 70 70 ASP F 23 LYS F 37 1 15
HELIX 71 71 TYR F 64 GLY F 66 5 3
HELIX 72 72 PHE F 98 TRP F 102 5 5
HELIX 73 73 LEU F 103 MSE F 108 1 6
HELIX 74 74 ASP F 151 THR F 154 5 4
HELIX 75 75 TYR F 155 SER F 173 1 19
HELIX 76 76 SER F 188 SER F 201 1 14
HELIX 77 77 HIS F 216 VAL F 224 1 9
HELIX 78 78 PRO F 228 HIS F 239 1 12
HELIX 79 79 LYS F 242 TYR F 252 1 11
HELIX 80 80 ASP F 254 ALA F 260 1 7
HELIX 81 81 PRO F 278 TYR F 289 1 12
HELIX 82 82 GLY F 306 PHE F 322 1 17
HELIX 83 83 PRO G 7 LYS G 12 1 6
HELIX 84 84 ASP G 23 LYS G 37 1 15
HELIX 85 85 TYR G 64 GLY G 66 5 3
HELIX 86 86 PHE G 98 TRP G 102 5 5
HELIX 87 87 LEU G 103 MSE G 108 1 6
HELIX 88 88 ASP G 151 THR G 154 5 4
HELIX 89 89 TYR G 155 SER G 173 1 19
HELIX 90 90 SER G 188 SER G 201 1 14
HELIX 91 91 HIS G 216 VAL G 224 1 9
HELIX 92 92 TYR G 229 HIS G 239 1 11
HELIX 93 93 LYS G 242 TYR G 252 1 11
HELIX 94 94 ASP G 254 ALA G 260 1 7
HELIX 95 95 PRO G 278 TYR G 289 1 12
HELIX 96 96 GLY G 306 GLU G 323 1 18
HELIX 97 97 PRO H 7 LYS H 12 1 6
HELIX 98 98 ASP H 23 LYS H 37 1 15
HELIX 99 99 TYR H 64 GLY H 66 5 3
HELIX 100 100 PHE H 98 TRP H 102 5 5
HELIX 101 101 LEU H 103 MSE H 108 1 6
HELIX 102 102 ASP H 151 THR H 154 5 4
HELIX 103 103 TYR H 155 SER H 173 1 19
HELIX 104 104 SER H 188 SER H 201 1 14
HELIX 105 105 HIS H 216 VAL H 224 1 9
HELIX 106 106 PRO H 228 HIS H 239 1 12
HELIX 107 107 LYS H 242 TYR H 252 1 11
HELIX 108 108 ASP H 254 ALA H 260 1 7
HELIX 109 109 PRO H 278 TYR H 289 1 12
HELIX 110 110 GLY H 306 GLU H 323 1 18
HELIX 111 111 PRO I 7 LYS I 12 1 6
HELIX 112 112 ASP I 23 LYS I 37 1 15
HELIX 113 113 TYR I 64 GLY I 66 5 3
HELIX 114 114 PHE I 98 TRP I 102 5 5
HELIX 115 115 LEU I 103 MSE I 108 1 6
HELIX 116 116 TYR I 155 SER I 173 1 19
HELIX 117 117 SER I 188 SER I 201 1 14
HELIX 118 118 HIS I 216 VAL I 224 1 9
HELIX 119 119 PRO I 228 HIS I 239 1 12
HELIX 120 120 LYS I 242 TYR I 252 1 11
HELIX 121 121 ASP I 254 ALA I 260 1 7
HELIX 122 122 PRO I 278 TYR I 289 1 12
HELIX 123 123 GLY I 306 PHE I 322 1 17
HELIX 124 124 PRO J 7 LYS J 12 1 6
HELIX 125 125 ASP J 23 LYS J 37 1 15
HELIX 126 126 TYR J 64 GLY J 66 5 3
HELIX 127 127 PHE J 98 TRP J 102 5 5
HELIX 128 128 LEU J 103 MSE J 108 1 6
HELIX 129 129 ASP J 151 THR J 154 5 4
HELIX 130 130 TYR J 155 SER J 173 1 19
HELIX 131 131 SER J 188 SER J 201 1 14
HELIX 132 132 HIS J 216 VAL J 224 1 9
HELIX 133 133 PRO J 228 HIS J 239 1 12
HELIX 134 134 LYS J 242 TYR J 252 1 11
HELIX 135 135 ASP J 254 ALA J 260 1 7
HELIX 136 136 PRO J 278 TYR J 289 1 12
HELIX 137 137 GLY J 306 PHE J 322 1 17
HELIX 138 138 PRO K 7 LYS K 12 1 6
HELIX 139 139 ASP K 23 LYS K 37 1 15
HELIX 140 140 TYR K 64 GLY K 66 5 3
HELIX 141 141 PHE K 98 TRP K 102 5 5
HELIX 142 142 LEU K 103 MSE K 108 1 6
HELIX 143 143 ASP K 151 THR K 154 5 4
HELIX 144 144 TYR K 155 SER K 173 1 19
HELIX 145 145 SER K 188 SER K 201 1 14
HELIX 146 146 HIS K 216 VAL K 224 1 9
HELIX 147 147 PRO K 228 HIS K 239 1 12
HELIX 148 148 LYS K 242 TYR K 252 1 11
HELIX 149 149 ASP K 254 ALA K 260 1 7
HELIX 150 150 PRO K 278 TYR K 289 1 12
HELIX 151 151 GLY K 306 GLU K 323 1 18
HELIX 152 152 PRO L 7 LYS L 12 1 6
HELIX 153 153 ASP L 23 LYS L 37 1 15
HELIX 154 154 TYR L 64 GLY L 66 5 3
HELIX 155 155 PHE L 98 TRP L 102 5 5
HELIX 156 156 LEU L 103 MSE L 108 1 6
HELIX 157 157 ASP L 151 THR L 154 5 4
HELIX 158 158 TYR L 155 SER L 173 1 19
HELIX 159 159 SER L 188 SER L 201 1 14
HELIX 160 160 HIS L 216 VAL L 224 1 9
HELIX 161 161 PRO L 228 HIS L 239 1 12
HELIX 162 162 LYS L 242 TYR L 252 1 11
HELIX 163 163 ASP L 254 ALA L 260 1 7
HELIX 164 164 PRO L 278 TYR L 289 1 12
HELIX 165 165 GLY L 306 GLU L 323 1 18
SHEET 1 A 9 VAL A 43 ARG A 46 0
SHEET 2 A 9 VAL A 54 SER A 62 -1 O THR A 60 N VAL A 43
SHEET 3 A 9 ARG A 68 PRO A 76 -1 O VAL A 75 N GLU A 55
SHEET 4 A 9 ILE A 111 MSE A 115 -1 O VAL A 114 N TRP A 72
SHEET 5 A 9 LEU A 83 GLN A 88 1 N VAL A 86 O ILE A 111
SHEET 6 A 9 VAL A 177 GLY A 187 1 O VAL A 183 N VAL A 87
SHEET 7 A 9 ALA A 206 ASP A 210 1 O ALA A 206 N ILE A 184
SHEET 8 A 9 ALA A 266 GLY A 271 1 O LEU A 267 N LEU A 207
SHEET 9 A 9 LYS A 293 TYR A 298 1 O GLU A 294 N PHE A 268
SHEET 1 B 9 VAL B 43 ARG B 46 0
SHEET 2 B 9 VAL B 54 SER B 62 -1 O THR B 60 N VAL B 43
SHEET 3 B 9 ARG B 68 PRO B 76 -1 O VAL B 75 N GLU B 55
SHEET 4 B 9 ILE B 111 MSE B 115 -1 O VAL B 114 N TRP B 72
SHEET 5 B 9 LEU B 83 GLN B 88 1 N GLN B 88 O PHE B 113
SHEET 6 B 9 VAL B 177 GLY B 187 1 O VAL B 183 N CYS B 85
SHEET 7 B 9 ALA B 206 ASP B 210 1 O ALA B 206 N ILE B 184
SHEET 8 B 9 ALA B 266 GLY B 271 1 O LEU B 267 N CYS B 209
SHEET 9 B 9 LYS B 293 TYR B 298 1 O GLU B 294 N PHE B 268
SHEET 1 C 9 VAL C 43 ARG C 46 0
SHEET 2 C 9 VAL C 54 SER C 62 -1 O THR C 60 N VAL C 43
SHEET 3 C 9 ARG C 68 PRO C 76 -1 O VAL C 75 N GLU C 55
SHEET 4 C 9 ILE C 111 MSE C 115 -1 O VAL C 114 N TRP C 72
SHEET 5 C 9 LEU C 83 GLN C 88 1 N VAL C 86 O ILE C 111
SHEET 6 C 9 VAL C 177 GLY C 187 1 O VAL C 183 N VAL C 87
SHEET 7 C 9 ALA C 206 ASP C 210 1 O ALA C 206 N ILE C 184
SHEET 8 C 9 ALA C 266 GLY C 271 1 O LEU C 267 N LEU C 207
SHEET 9 C 9 LYS C 293 TYR C 298 1 O GLU C 294 N PHE C 268
SHEET 1 D 9 VAL D 43 ARG D 46 0
SHEET 2 D 9 VAL D 54 SER D 62 -1 O THR D 60 N VAL D 43
SHEET 3 D 9 ARG D 68 PRO D 76 -1 O ILE D 69 N PHE D 61
SHEET 4 D 9 ILE D 111 MSE D 115 -1 O VAL D 114 N TRP D 72
SHEET 5 D 9 LEU D 83 GLN D 88 1 N VAL D 86 O ILE D 111
SHEET 6 D 9 VAL D 177 GLY D 187 1 O VAL D 183 N VAL D 87
SHEET 7 D 9 ALA D 206 ASP D 210 1 O ALA D 206 N ILE D 184
SHEET 8 D 9 ALA D 266 GLY D 271 1 O LEU D 267 N LEU D 207
SHEET 9 D 9 LYS D 293 TYR D 298 1 O GLU D 294 N PHE D 268
SHEET 1 E 9 VAL E 43 ARG E 46 0
SHEET 2 E 9 VAL E 54 SER E 62 -1 O THR E 60 N VAL E 43
SHEET 3 E 9 ARG E 68 PRO E 76 -1 O VAL E 75 N GLU E 55
SHEET 4 E 9 ILE E 111 MSE E 115 -1 O VAL E 114 N TRP E 72
SHEET 5 E 9 LEU E 83 GLN E 88 1 N GLN E 88 O PHE E 113
SHEET 6 E 9 VAL E 177 GLY E 187 1 O VAL E 183 N CYS E 85
SHEET 7 E 9 ALA E 206 ASP E 210 1 O LEU E 208 N ILE E 184
SHEET 8 E 9 ALA E 266 GLY E 271 1 O LEU E 267 N CYS E 209
SHEET 9 E 9 LYS E 293 TYR E 298 1 O GLU E 294 N PHE E 268
SHEET 1 F 9 VAL F 43 ARG F 46 0
SHEET 2 F 9 VAL F 54 SER F 62 -1 O THR F 60 N VAL F 43
SHEET 3 F 9 ARG F 68 PRO F 76 -1 O ILE F 69 N PHE F 61
SHEET 4 F 9 ILE F 111 MSE F 115 -1 O VAL F 114 N TRP F 72
SHEET 5 F 9 LEU F 83 GLN F 88 1 N GLN F 88 O PHE F 113
SHEET 6 F 9 VAL F 177 GLY F 187 1 O VAL F 183 N CYS F 85
SHEET 7 F 9 ALA F 206 ASP F 210 1 O LEU F 208 N ILE F 184
SHEET 8 F 9 ALA F 266 GLY F 271 1 O LEU F 267 N CYS F 209
SHEET 9 F 9 LYS F 293 TYR F 298 1 O GLU F 294 N PHE F 268
SHEET 1 G 9 VAL G 43 ARG G 46 0
SHEET 2 G 9 VAL G 54 SER G 62 -1 O THR G 60 N VAL G 43
SHEET 3 G 9 ARG G 68 PRO G 76 -1 O VAL G 75 N GLU G 55
SHEET 4 G 9 ILE G 111 MSE G 115 -1 O VAL G 114 N TRP G 72
SHEET 5 G 9 LEU G 83 GLN G 88 1 N VAL G 86 O ILE G 111
SHEET 6 G 9 VAL G 177 GLY G 187 1 O VAL G 183 N VAL G 87
SHEET 7 G 9 ALA G 206 ASP G 210 1 O ALA G 206 N ILE G 184
SHEET 8 G 9 ALA G 266 GLY G 271 1 O LEU G 267 N LEU G 207
SHEET 9 G 9 LYS G 293 TYR G 298 1 O GLU G 294 N PHE G 268
SHEET 1 H 9 VAL H 43 ARG H 46 0
SHEET 2 H 9 VAL H 54 SER H 62 -1 O THR H 60 N VAL H 43
SHEET 3 H 9 ARG H 68 PRO H 76 -1 O VAL H 75 N GLU H 55
SHEET 4 H 9 ILE H 111 MSE H 115 -1 O VAL H 114 N TRP H 72
SHEET 5 H 9 LEU H 83 GLN H 88 1 N GLN H 88 O PHE H 113
SHEET 6 H 9 VAL H 177 GLY H 187 1 O VAL H 183 N VAL H 87
SHEET 7 H 9 ALA H 206 ASP H 210 1 O ALA H 206 N ILE H 184
SHEET 8 H 9 ALA H 266 GLY H 271 1 O LEU H 267 N CYS H 209
SHEET 9 H 9 LYS H 293 TYR H 298 1 O GLU H 294 N PHE H 268
SHEET 1 I 9 VAL I 43 ARG I 46 0
SHEET 2 I 9 VAL I 54 SER I 62 -1 O THR I 60 N VAL I 43
SHEET 3 I 9 ARG I 68 PRO I 76 -1 O VAL I 75 N GLU I 55
SHEET 4 I 9 ILE I 111 MSE I 115 -1 O VAL I 114 N TRP I 72
SHEET 5 I 9 LEU I 83 GLN I 88 1 N GLN I 88 O PHE I 113
SHEET 6 I 9 VAL I 177 GLY I 187 1 O VAL I 183 N VAL I 87
SHEET 7 I 9 ALA I 206 ASP I 210 1 O ALA I 206 N ILE I 184
SHEET 8 I 9 ALA I 266 GLY I 271 1 O LEU I 267 N LEU I 207
SHEET 9 I 9 LYS I 293 TYR I 298 1 O GLU I 294 N PHE I 268
SHEET 1 J 9 VAL J 43 ARG J 46 0
SHEET 2 J 9 VAL J 54 SER J 62 -1 O THR J 60 N VAL J 43
SHEET 3 J 9 ARG J 68 PRO J 76 -1 O VAL J 75 N GLU J 55
SHEET 4 J 9 ILE J 111 MSE J 115 -1 O VAL J 114 N TRP J 72
SHEET 5 J 9 LEU J 83 GLN J 88 1 N VAL J 86 O ILE J 111
SHEET 6 J 9 VAL J 177 GLY J 187 1 O VAL J 183 N CYS J 85
SHEET 7 J 9 ALA J 206 ASP J 210 1 O ALA J 206 N ILE J 184
SHEET 8 J 9 ALA J 266 GLY J 271 1 O LEU J 267 N CYS J 209
SHEET 9 J 9 LYS J 293 TYR J 298 1 O GLU J 294 N PHE J 268
SHEET 1 K 9 VAL K 43 ARG K 46 0
SHEET 2 K 9 VAL K 54 SER K 62 -1 O THR K 60 N VAL K 43
SHEET 3 K 9 ARG K 68 PRO K 76 -1 O VAL K 75 N GLU K 55
SHEET 4 K 9 ILE K 111 MSE K 115 -1 O VAL K 114 N TRP K 72
SHEET 5 K 9 LEU K 83 GLN K 88 1 N VAL K 86 O ILE K 111
SHEET 6 K 9 VAL K 177 GLY K 187 1 O VAL K 183 N VAL K 87
SHEET 7 K 9 ALA K 206 ASP K 210 1 O ALA K 206 N ILE K 184
SHEET 8 K 9 ALA K 266 GLY K 271 1 O LEU K 267 N CYS K 209
SHEET 9 K 9 LYS K 293 TYR K 298 1 O GLU K 294 N PHE K 268
SHEET 1 L 9 VAL L 43 ARG L 46 0
SHEET 2 L 9 VAL L 54 SER L 62 -1 O THR L 60 N VAL L 43
SHEET 3 L 9 ARG L 68 PRO L 76 -1 O VAL L 75 N GLU L 55
SHEET 4 L 9 ILE L 111 MSE L 115 -1 O VAL L 114 N TRP L 72
SHEET 5 L 9 LEU L 83 TYR L 89 1 N GLN L 88 O PHE L 113
SHEET 6 L 9 VAL L 177 GLY L 187 1 O VAL L 183 N CYS L 85
SHEET 7 L 9 ALA L 206 ASP L 210 1 O ALA L 206 N ILE L 184
SHEET 8 L 9 ALA L 266 GLY L 271 1 O LEU L 267 N LEU L 207
SHEET 9 L 9 LYS L 293 TYR L 298 1 O GLU L 294 N PHE L 268
CISPEP 1 HIS A 227 PRO A 228 0 4.70
CISPEP 2 HIS B 227 PRO B 228 0 4.27
CISPEP 3 HIS C 227 PRO C 228 0 2.79
CISPEP 4 HIS D 227 PRO D 228 0 2.25
CISPEP 5 HIS E 227 PRO E 228 0 1.81
CISPEP 6 HIS F 227 PRO F 228 0 4.95
CISPEP 7 HIS G 227 PRO G 228 0 -1.51
CISPEP 8 HIS H 227 PRO H 228 0 1.92
CISPEP 9 HIS I 227 PRO I 228 0 6.91
CISPEP 10 HIS J 227 PRO J 228 0 4.47
CISPEP 11 HIS K 227 PRO K 228 0 -2.10
CISPEP 12 HIS L 227 PRO L 228 0 1.88
CRYST1 152.640 130.952 157.815 90.00 118.93 90.00 P 1 21 1 24
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 0.006551 0.000000 0.003621 0.00000
SCALE2 0.000000 0.007636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007240 0.00000
TER 2605 GLU A 323
TER 5194 GLU B 323
TER 7794 GLU C 323
TER 10386 GLU D 323
TER 12989 GLU E 323
TER 15585 GLU F 323
TER 18186 GLU G 323
TER 20789 GLU H 323
TER 23389 GLU I 323
TER 25986 GLU J 323
TER 28585 GLU K 323
TER 31195 GLU L 323
MASTER 619 0 61 165 108 0 0 633653 12 486 312
END |