HEADER LIGASE 09-APR-09 3H0M
TITLE STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM AQUIFEX
TITLE 2 AEOLICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A;
COMPND 3 CHAIN: A, D, G, J, M, P, S, V;
COMPND 4 SYNONYM: GLU-ADT SUBUNIT A;
COMPND 5 EC: 6.3.5.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ASPARTYL/GLUTAMYL-TRNA(ASN/GLN) AMIDOTRANSFERASE SUBUNIT B;
COMPND 9 CHAIN: B, E, H, K, N, Q, T, W;
COMPND 10 SYNONYM: ASP/GLU-ADT SUBUNIT B;
COMPND 11 EC: 6.3.5.-;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C;
COMPND 15 CHAIN: C, F, I, L, O, R, U, X;
COMPND 16 SYNONYM: GLU-ADT SUBUNIT C;
COMPND 17 EC: 6.3.5.-;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 STRAIN: VF5;
SOURCE 5 GENE: AQ_247, GATA, GATCA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17B-CA;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 13 ORGANISM_TAXID: 63363;
SOURCE 14 STRAIN: VF5;
SOURCE 15 GENE: AQ_461, GATB;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET17B-B;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 23 ORGANISM_TAXID: 63363;
SOURCE 24 STRAIN: VF5;
SOURCE 25 GENE: GATC, AQ_2149;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET17B-CA
KEYWDS MULTI PROTEIN COMPLEX, LIGASE, PROTEIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WU,W.BU,K.SHEPPARD,M.KITABATAKE,D.SOLL,J.L.SMITH
REVDAT 3 06-SEP-23 3H0M 1 REMARK LINK
REVDAT 2 25-AUG-09 3H0M 1 JRNL
REVDAT 1 21-JUL-09 3H0M 0
JRNL AUTH J.WU,W.BU,K.SHEPPARD,M.KITABATAKE,S.T.KWON,D.SOLL,J.L.SMITH
JRNL TITL INSIGHTS INTO TRNA-DEPENDENT AMIDOTRANSFERASE EVOLUTION AND
JRNL TITL 2 CATALYSIS FROM THE STRUCTURE OF THE AQUIFEX AEOLICUS ENZYME
JRNL REF J.MOL.BIOL. V. 391 703 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19520089
JRNL DOI 10.1016/J.JMB.2009.06.014
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 229209
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) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.254
REMARK 3 FREE R VALUE : 0.305
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 12256
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 32647
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.3520
REMARK 3 BIN FREE R VALUE SET COUNT : 1778
REMARK 3 BIN FREE R VALUE : 0.4000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 62848
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 87
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.10000
REMARK 3 B22 (A**2) : 8.81000
REMARK 3 B33 (A**2) : -4.70000
REMARK 3 B12 (A**2) : 0.42000
REMARK 3 B13 (A**2) : 0.33000
REMARK 3 B23 (A**2) : 1.49000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.910
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.459
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.412
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.982
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 64355 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 86850 ; 1.491 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 7806 ; 7.010 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2936 ;37.852 ;24.496
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 11968 ;20.057 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 400 ;20.316 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 9488 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 48168 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 29888 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 42896 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1945 ; 0.153 ; 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): 138 ; 0.239 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.233 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A D G J M P S V
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 478 3
REMARK 3 1 D 1 D 478 3
REMARK 3 1 G 1 G 478 3
REMARK 3 1 J 1 J 478 3
REMARK 3 1 M 1 M 478 3
REMARK 3 1 P 1 P 478 3
REMARK 3 1 S 1 S 478 3
REMARK 3 1 V 1 V 478 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1912 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1912 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 G (A): 1912 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 J (A): 1912 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 M (A): 1912 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 P (A): 1912 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 S (A): 1912 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 V (A): 1912 ; 0.03 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 1876 ; 0.33 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 1876 ; 0.39 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 G (A): 1876 ; 0.30 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 J (A): 1876 ; 0.34 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 M (A): 1876 ; 0.33 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 P (A): 1876 ; 0.34 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 S (A): 1876 ; 0.33 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 V (A): 1876 ; 0.32 ; 5.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B E H K N Q T W
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 3 B 293 4
REMARK 3 1 E 3 E 293 4
REMARK 3 1 H 3 H 293 4
REMARK 3 1 K 3 K 293 4
REMARK 3 1 N 3 N 293 4
REMARK 3 1 Q 3 Q 293 4
REMARK 3 1 T 3 T 293 4
REMARK 3 1 W 3 W 293 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 2356 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 E (A): 2356 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 H (A): 2356 ; 0.30 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 K (A): 2356 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 N (A): 2356 ; 0.29 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 Q (A): 2356 ; 0.28 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 T (A): 2356 ; 0.27 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 W (A): 2356 ; 0.38 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : B E H K N Q T W
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 294 B 412 4
REMARK 3 1 E 294 E 412 4
REMARK 3 1 H 294 H 412 4
REMARK 3 1 K 294 K 412 4
REMARK 3 1 N 294 N 412 4
REMARK 3 1 Q 294 Q 412 4
REMARK 3 1 T 294 T 412 4
REMARK 3 1 W 294 W 412 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 B (A): 957 ; 0.36 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 E (A): 957 ; 0.36 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 H (A): 957 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 K (A): 957 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 N (A): 957 ; 0.34 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 Q (A): 957 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 T (A): 957 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 W (A): 957 ; 0.32 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : C F I L O R U X
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 2 C 92 4
REMARK 3 1 F 2 F 92 4
REMARK 3 1 I 2 I 92 4
REMARK 3 1 L 2 L 92 4
REMARK 3 1 O 2 O 92 4
REMARK 3 1 R 2 R 92 4
REMARK 3 1 U 2 U 92 4
REMARK 3 1 X 2 X 92 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 C (A): 760 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 F (A): 760 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 I (A): 760 ; 0.30 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 L (A): 760 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 O (A): 760 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 R (A): 760 ; 0.36 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 U (A): 760 ; 0.30 ; 0.50
REMARK 3 MEDIUM POSITIONAL 4 X (A): 760 ; 0.33 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3H0M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052541.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-05
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 : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0274
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 241473
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 39.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.47800
REMARK 200 R SYM FOR SHELL (I) : 0.47800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 2H0L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 RATIO OF PROTEIN SOLUTION (6
REMARK 280 -9MG/ML GATCAB,10MM HEPES, 50UM ZN ACETATE,10MM GLN, 0.6MM ATP)
REMARK 280 MIX WITH WELL SOLUTION (10-12% PEG3350, 10MM MG FORMATE), PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T, U
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: V, W, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 LYS B 413
REMARK 465 GLN B 414
REMARK 465 ILE B 415
REMARK 465 THR B 416
REMARK 465 ASP B 417
REMARK 465 GLU B 418
REMARK 465 ASN B 419
REMARK 465 GLN B 420
REMARK 465 ILE B 421
REMARK 465 LYS B 422
REMARK 465 GLU B 423
REMARK 465 LEU B 424
REMARK 465 VAL B 425
REMARK 465 LYS B 426
REMARK 465 LYS B 427
REMARK 465 ILE B 428
REMARK 465 PHE B 429
REMARK 465 GLU B 430
REMARK 465 LYS B 431
REMARK 465 HIS B 432
REMARK 465 PRO B 433
REMARK 465 LYS B 434
REMARK 465 GLU B 435
REMARK 465 VAL B 436
REMARK 465 GLU B 437
REMARK 465 ARG B 438
REMARK 465 LEU B 439
REMARK 465 LYS B 440
REMARK 465 GLN B 441
REMARK 465 GLY B 442
REMARK 465 GLU B 443
REMARK 465 GLU B 444
REMARK 465 LYS B 445
REMARK 465 LEU B 446
REMARK 465 ILE B 447
REMARK 465 GLY B 448
REMARK 465 PHE B 449
REMARK 465 PHE B 450
REMARK 465 VAL B 451
REMARK 465 GLY B 452
REMARK 465 GLN B 453
REMARK 465 VAL B 454
REMARK 465 MET B 455
REMARK 465 ARG B 456
REMARK 465 GLU B 457
REMARK 465 THR B 458
REMARK 465 ARG B 459
REMARK 465 GLY B 460
REMARK 465 LYS B 461
REMARK 465 ALA B 462
REMARK 465 ASN B 463
REMARK 465 PRO B 464
REMARK 465 GLN B 465
REMARK 465 VAL B 466
REMARK 465 VAL B 467
REMARK 465 ASN B 468
REMARK 465 LYS B 469
REMARK 465 VAL B 470
REMARK 465 ILE B 471
REMARK 465 ARG B 472
REMARK 465 GLU B 473
REMARK 465 LEU B 474
REMARK 465 VAL B 475
REMARK 465 LYS B 476
REMARK 465 GLU B 477
REMARK 465 VAL B 478
REMARK 465 MET C 1
REMARK 465 GLU C 93
REMARK 465 VAL C 94
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 LYS E 413
REMARK 465 GLN E 414
REMARK 465 ILE E 415
REMARK 465 THR E 416
REMARK 465 ASP E 417
REMARK 465 GLU E 418
REMARK 465 ASN E 419
REMARK 465 GLN E 420
REMARK 465 ILE E 421
REMARK 465 LYS E 422
REMARK 465 GLU E 423
REMARK 465 LEU E 424
REMARK 465 VAL E 425
REMARK 465 LYS E 426
REMARK 465 LYS E 427
REMARK 465 ILE E 428
REMARK 465 PHE E 429
REMARK 465 GLU E 430
REMARK 465 LYS E 431
REMARK 465 HIS E 432
REMARK 465 PRO E 433
REMARK 465 LYS E 434
REMARK 465 GLU E 435
REMARK 465 VAL E 436
REMARK 465 GLU E 437
REMARK 465 ARG E 438
REMARK 465 LEU E 439
REMARK 465 LYS E 440
REMARK 465 GLN E 441
REMARK 465 GLY E 442
REMARK 465 GLU E 443
REMARK 465 GLU E 444
REMARK 465 LYS E 445
REMARK 465 LEU E 446
REMARK 465 ILE E 447
REMARK 465 GLY E 448
REMARK 465 PHE E 449
REMARK 465 PHE E 450
REMARK 465 VAL E 451
REMARK 465 GLY E 452
REMARK 465 GLN E 453
REMARK 465 VAL E 454
REMARK 465 MET E 455
REMARK 465 ARG E 456
REMARK 465 GLU E 457
REMARK 465 THR E 458
REMARK 465 ARG E 459
REMARK 465 GLY E 460
REMARK 465 LYS E 461
REMARK 465 ALA E 462
REMARK 465 ASN E 463
REMARK 465 PRO E 464
REMARK 465 GLN E 465
REMARK 465 VAL E 466
REMARK 465 VAL E 467
REMARK 465 ASN E 468
REMARK 465 LYS E 469
REMARK 465 VAL E 470
REMARK 465 ILE E 471
REMARK 465 ARG E 472
REMARK 465 GLU E 473
REMARK 465 LEU E 474
REMARK 465 VAL E 475
REMARK 465 LYS E 476
REMARK 465 GLU E 477
REMARK 465 VAL E 478
REMARK 465 MET F 1
REMARK 465 GLU F 93
REMARK 465 VAL F 94
REMARK 465 MET H 1
REMARK 465 ASN H 2
REMARK 465 LYS H 413
REMARK 465 GLN H 414
REMARK 465 ILE H 415
REMARK 465 THR H 416
REMARK 465 ASP H 417
REMARK 465 GLU H 418
REMARK 465 ASN H 419
REMARK 465 GLN H 420
REMARK 465 ILE H 421
REMARK 465 LYS H 422
REMARK 465 GLU H 423
REMARK 465 LEU H 424
REMARK 465 VAL H 425
REMARK 465 LYS H 426
REMARK 465 LYS H 427
REMARK 465 ILE H 428
REMARK 465 PHE H 429
REMARK 465 GLU H 430
REMARK 465 LYS H 431
REMARK 465 HIS H 432
REMARK 465 PRO H 433
REMARK 465 LYS H 434
REMARK 465 GLU H 435
REMARK 465 VAL H 436
REMARK 465 GLU H 437
REMARK 465 ARG H 438
REMARK 465 LEU H 439
REMARK 465 LYS H 440
REMARK 465 GLN H 441
REMARK 465 GLY H 442
REMARK 465 GLU H 443
REMARK 465 GLU H 444
REMARK 465 LYS H 445
REMARK 465 LEU H 446
REMARK 465 ILE H 447
REMARK 465 GLY H 448
REMARK 465 PHE H 449
REMARK 465 PHE H 450
REMARK 465 VAL H 451
REMARK 465 GLY H 452
REMARK 465 GLN H 453
REMARK 465 VAL H 454
REMARK 465 MET H 455
REMARK 465 ARG H 456
REMARK 465 GLU H 457
REMARK 465 THR H 458
REMARK 465 ARG H 459
REMARK 465 GLY H 460
REMARK 465 LYS H 461
REMARK 465 ALA H 462
REMARK 465 ASN H 463
REMARK 465 PRO H 464
REMARK 465 GLN H 465
REMARK 465 VAL H 466
REMARK 465 VAL H 467
REMARK 465 ASN H 468
REMARK 465 LYS H 469
REMARK 465 VAL H 470
REMARK 465 ILE H 471
REMARK 465 ARG H 472
REMARK 465 GLU H 473
REMARK 465 LEU H 474
REMARK 465 VAL H 475
REMARK 465 LYS H 476
REMARK 465 GLU H 477
REMARK 465 VAL H 478
REMARK 465 MET I 1
REMARK 465 GLU I 93
REMARK 465 VAL I 94
REMARK 465 MET K 1
REMARK 465 ASN K 2
REMARK 465 LYS K 413
REMARK 465 GLN K 414
REMARK 465 ILE K 415
REMARK 465 THR K 416
REMARK 465 ASP K 417
REMARK 465 GLU K 418
REMARK 465 ASN K 419
REMARK 465 GLN K 420
REMARK 465 ILE K 421
REMARK 465 LYS K 422
REMARK 465 GLU K 423
REMARK 465 LEU K 424
REMARK 465 VAL K 425
REMARK 465 LYS K 426
REMARK 465 LYS K 427
REMARK 465 ILE K 428
REMARK 465 PHE K 429
REMARK 465 GLU K 430
REMARK 465 LYS K 431
REMARK 465 HIS K 432
REMARK 465 PRO K 433
REMARK 465 LYS K 434
REMARK 465 GLU K 435
REMARK 465 VAL K 436
REMARK 465 GLU K 437
REMARK 465 ARG K 438
REMARK 465 LEU K 439
REMARK 465 LYS K 440
REMARK 465 GLN K 441
REMARK 465 GLY K 442
REMARK 465 GLU K 443
REMARK 465 GLU K 444
REMARK 465 LYS K 445
REMARK 465 LEU K 446
REMARK 465 ILE K 447
REMARK 465 GLY K 448
REMARK 465 PHE K 449
REMARK 465 PHE K 450
REMARK 465 VAL K 451
REMARK 465 GLY K 452
REMARK 465 GLN K 453
REMARK 465 VAL K 454
REMARK 465 MET K 455
REMARK 465 ARG K 456
REMARK 465 GLU K 457
REMARK 465 THR K 458
REMARK 465 ARG K 459
REMARK 465 GLY K 460
REMARK 465 LYS K 461
REMARK 465 ALA K 462
REMARK 465 ASN K 463
REMARK 465 PRO K 464
REMARK 465 GLN K 465
REMARK 465 VAL K 466
REMARK 465 VAL K 467
REMARK 465 ASN K 468
REMARK 465 LYS K 469
REMARK 465 VAL K 470
REMARK 465 ILE K 471
REMARK 465 ARG K 472
REMARK 465 GLU K 473
REMARK 465 LEU K 474
REMARK 465 VAL K 475
REMARK 465 LYS K 476
REMARK 465 GLU K 477
REMARK 465 VAL K 478
REMARK 465 MET L 1
REMARK 465 GLU L 93
REMARK 465 VAL L 94
REMARK 465 MET N 1
REMARK 465 ASN N 2
REMARK 465 LYS N 413
REMARK 465 GLN N 414
REMARK 465 ILE N 415
REMARK 465 THR N 416
REMARK 465 ASP N 417
REMARK 465 GLU N 418
REMARK 465 ASN N 419
REMARK 465 GLN N 420
REMARK 465 ILE N 421
REMARK 465 LYS N 422
REMARK 465 GLU N 423
REMARK 465 LEU N 424
REMARK 465 VAL N 425
REMARK 465 LYS N 426
REMARK 465 LYS N 427
REMARK 465 ILE N 428
REMARK 465 PHE N 429
REMARK 465 GLU N 430
REMARK 465 LYS N 431
REMARK 465 HIS N 432
REMARK 465 PRO N 433
REMARK 465 LYS N 434
REMARK 465 GLU N 435
REMARK 465 VAL N 436
REMARK 465 GLU N 437
REMARK 465 ARG N 438
REMARK 465 LEU N 439
REMARK 465 LYS N 440
REMARK 465 GLN N 441
REMARK 465 GLY N 442
REMARK 465 GLU N 443
REMARK 465 GLU N 444
REMARK 465 LYS N 445
REMARK 465 LEU N 446
REMARK 465 ILE N 447
REMARK 465 GLY N 448
REMARK 465 PHE N 449
REMARK 465 PHE N 450
REMARK 465 VAL N 451
REMARK 465 GLY N 452
REMARK 465 GLN N 453
REMARK 465 VAL N 454
REMARK 465 MET N 455
REMARK 465 ARG N 456
REMARK 465 GLU N 457
REMARK 465 THR N 458
REMARK 465 ARG N 459
REMARK 465 GLY N 460
REMARK 465 LYS N 461
REMARK 465 ALA N 462
REMARK 465 ASN N 463
REMARK 465 PRO N 464
REMARK 465 GLN N 465
REMARK 465 VAL N 466
REMARK 465 VAL N 467
REMARK 465 ASN N 468
REMARK 465 LYS N 469
REMARK 465 VAL N 470
REMARK 465 ILE N 471
REMARK 465 ARG N 472
REMARK 465 GLU N 473
REMARK 465 LEU N 474
REMARK 465 VAL N 475
REMARK 465 LYS N 476
REMARK 465 GLU N 477
REMARK 465 VAL N 478
REMARK 465 MET O 1
REMARK 465 GLU O 93
REMARK 465 VAL O 94
REMARK 465 MET Q 1
REMARK 465 ASN Q 2
REMARK 465 LYS Q 413
REMARK 465 GLN Q 414
REMARK 465 ILE Q 415
REMARK 465 THR Q 416
REMARK 465 ASP Q 417
REMARK 465 GLU Q 418
REMARK 465 ASN Q 419
REMARK 465 GLN Q 420
REMARK 465 ILE Q 421
REMARK 465 LYS Q 422
REMARK 465 GLU Q 423
REMARK 465 LEU Q 424
REMARK 465 VAL Q 425
REMARK 465 LYS Q 426
REMARK 465 LYS Q 427
REMARK 465 ILE Q 428
REMARK 465 PHE Q 429
REMARK 465 GLU Q 430
REMARK 465 LYS Q 431
REMARK 465 HIS Q 432
REMARK 465 PRO Q 433
REMARK 465 LYS Q 434
REMARK 465 GLU Q 435
REMARK 465 VAL Q 436
REMARK 465 GLU Q 437
REMARK 465 ARG Q 438
REMARK 465 LEU Q 439
REMARK 465 LYS Q 440
REMARK 465 GLN Q 441
REMARK 465 GLY Q 442
REMARK 465 GLU Q 443
REMARK 465 GLU Q 444
REMARK 465 LYS Q 445
REMARK 465 LEU Q 446
REMARK 465 ILE Q 447
REMARK 465 GLY Q 448
REMARK 465 PHE Q 449
REMARK 465 PHE Q 450
REMARK 465 VAL Q 451
REMARK 465 GLY Q 452
REMARK 465 GLN Q 453
REMARK 465 VAL Q 454
REMARK 465 MET Q 455
REMARK 465 ARG Q 456
REMARK 465 GLU Q 457
REMARK 465 THR Q 458
REMARK 465 ARG Q 459
REMARK 465 GLY Q 460
REMARK 465 LYS Q 461
REMARK 465 ALA Q 462
REMARK 465 ASN Q 463
REMARK 465 PRO Q 464
REMARK 465 GLN Q 465
REMARK 465 VAL Q 466
REMARK 465 VAL Q 467
REMARK 465 ASN Q 468
REMARK 465 LYS Q 469
REMARK 465 VAL Q 470
REMARK 465 ILE Q 471
REMARK 465 ARG Q 472
REMARK 465 GLU Q 473
REMARK 465 LEU Q 474
REMARK 465 VAL Q 475
REMARK 465 LYS Q 476
REMARK 465 GLU Q 477
REMARK 465 VAL Q 478
REMARK 465 MET R 1
REMARK 465 GLU R 93
REMARK 465 VAL R 94
REMARK 465 MET T 1
REMARK 465 ASN T 2
REMARK 465 LYS T 413
REMARK 465 GLN T 414
REMARK 465 ILE T 415
REMARK 465 THR T 416
REMARK 465 ASP T 417
REMARK 465 GLU T 418
REMARK 465 ASN T 419
REMARK 465 GLN T 420
REMARK 465 ILE T 421
REMARK 465 LYS T 422
REMARK 465 GLU T 423
REMARK 465 LEU T 424
REMARK 465 VAL T 425
REMARK 465 LYS T 426
REMARK 465 LYS T 427
REMARK 465 ILE T 428
REMARK 465 PHE T 429
REMARK 465 GLU T 430
REMARK 465 LYS T 431
REMARK 465 HIS T 432
REMARK 465 PRO T 433
REMARK 465 LYS T 434
REMARK 465 GLU T 435
REMARK 465 VAL T 436
REMARK 465 GLU T 437
REMARK 465 ARG T 438
REMARK 465 LEU T 439
REMARK 465 LYS T 440
REMARK 465 GLN T 441
REMARK 465 GLY T 442
REMARK 465 GLU T 443
REMARK 465 GLU T 444
REMARK 465 LYS T 445
REMARK 465 LEU T 446
REMARK 465 ILE T 447
REMARK 465 GLY T 448
REMARK 465 PHE T 449
REMARK 465 PHE T 450
REMARK 465 VAL T 451
REMARK 465 GLY T 452
REMARK 465 GLN T 453
REMARK 465 VAL T 454
REMARK 465 MET T 455
REMARK 465 ARG T 456
REMARK 465 GLU T 457
REMARK 465 THR T 458
REMARK 465 ARG T 459
REMARK 465 GLY T 460
REMARK 465 LYS T 461
REMARK 465 ALA T 462
REMARK 465 ASN T 463
REMARK 465 PRO T 464
REMARK 465 GLN T 465
REMARK 465 VAL T 466
REMARK 465 VAL T 467
REMARK 465 ASN T 468
REMARK 465 LYS T 469
REMARK 465 VAL T 470
REMARK 465 ILE T 471
REMARK 465 ARG T 472
REMARK 465 GLU T 473
REMARK 465 LEU T 474
REMARK 465 VAL T 475
REMARK 465 LYS T 476
REMARK 465 GLU T 477
REMARK 465 VAL T 478
REMARK 465 MET U 1
REMARK 465 GLU U 93
REMARK 465 VAL U 94
REMARK 465 MET W 1
REMARK 465 ASN W 2
REMARK 465 LYS W 413
REMARK 465 GLN W 414
REMARK 465 ILE W 415
REMARK 465 THR W 416
REMARK 465 ASP W 417
REMARK 465 GLU W 418
REMARK 465 ASN W 419
REMARK 465 GLN W 420
REMARK 465 ILE W 421
REMARK 465 LYS W 422
REMARK 465 GLU W 423
REMARK 465 LEU W 424
REMARK 465 VAL W 425
REMARK 465 LYS W 426
REMARK 465 LYS W 427
REMARK 465 ILE W 428
REMARK 465 PHE W 429
REMARK 465 GLU W 430
REMARK 465 LYS W 431
REMARK 465 HIS W 432
REMARK 465 PRO W 433
REMARK 465 LYS W 434
REMARK 465 GLU W 435
REMARK 465 VAL W 436
REMARK 465 GLU W 437
REMARK 465 ARG W 438
REMARK 465 LEU W 439
REMARK 465 LYS W 440
REMARK 465 GLN W 441
REMARK 465 GLY W 442
REMARK 465 GLU W 443
REMARK 465 GLU W 444
REMARK 465 LYS W 445
REMARK 465 LEU W 446
REMARK 465 ILE W 447
REMARK 465 GLY W 448
REMARK 465 PHE W 449
REMARK 465 PHE W 450
REMARK 465 VAL W 451
REMARK 465 GLY W 452
REMARK 465 GLN W 453
REMARK 465 VAL W 454
REMARK 465 MET W 455
REMARK 465 ARG W 456
REMARK 465 GLU W 457
REMARK 465 THR W 458
REMARK 465 ARG W 459
REMARK 465 GLY W 460
REMARK 465 LYS W 461
REMARK 465 ALA W 462
REMARK 465 ASN W 463
REMARK 465 PRO W 464
REMARK 465 GLN W 465
REMARK 465 VAL W 466
REMARK 465 VAL W 467
REMARK 465 ASN W 468
REMARK 465 LYS W 469
REMARK 465 VAL W 470
REMARK 465 ILE W 471
REMARK 465 ARG W 472
REMARK 465 GLU W 473
REMARK 465 LEU W 474
REMARK 465 VAL W 475
REMARK 465 LYS W 476
REMARK 465 GLU W 477
REMARK 465 VAL W 478
REMARK 465 MET X 1
REMARK 465 GLU X 93
REMARK 465 VAL X 94
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 PRO B 86 C - N - CA ANGL. DEV. = 9.6 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 LEU A 2 -64.34 83.29
REMARK 500 PHE A 65 -59.99 -28.92
REMARK 500 ASP A 73 32.06 -84.84
REMARK 500 CYS A 84 27.50 47.28
REMARK 500 SER A 125 -15.85 -151.63
REMARK 500 THR A 126 -10.86 80.68
REMARK 500 PHE A 132 149.05 -174.06
REMARK 500 ASP A 139 104.17 -171.36
REMARK 500 SER A 148 45.69 -66.73
REMARK 500 PHE A 199 -75.18 -108.18
REMARK 500 ASP A 318 -5.57 -143.93
REMARK 500 TYR A 367 -90.82 -104.41
REMARK 500 PRO A 401 122.37 -36.53
REMARK 500 GLU A 409 -71.82 -59.78
REMARK 500 ASP A 454 51.64 -102.32
REMARK 500 SER B 95 -148.56 -133.04
REMARK 500 TYR B 97 -109.60 -132.59
REMARK 500 LYS B 99 59.39 72.82
REMARK 500 ASP B 269 126.52 -37.02
REMARK 500 THR B 399 -67.74 -104.22
REMARK 500 GLU C 42 -39.40 -35.27
REMARK 500 PHE C 55 139.78 -178.80
REMARK 500 LEU D 2 -66.50 85.97
REMARK 500 LYS D 58 -51.02 -124.58
REMARK 500 PHE D 65 -63.03 -29.28
REMARK 500 ASP D 73 31.29 -81.28
REMARK 500 CYS D 84 27.60 47.98
REMARK 500 SER D 125 -13.93 -152.07
REMARK 500 THR D 126 -5.61 78.14
REMARK 500 PRO D 137 -9.77 -59.73
REMARK 500 ASP D 139 105.44 -170.33
REMARK 500 SER D 148 44.78 -68.71
REMARK 500 PHE D 199 -69.47 -108.17
REMARK 500 ASP D 318 -4.97 -144.90
REMARK 500 TYR D 367 -92.17 -102.40
REMARK 500 PRO D 401 120.32 -39.12
REMARK 500 ASP D 454 49.45 -99.66
REMARK 500 SER E 95 -143.00 -136.13
REMARK 500 TYR E 97 -110.61 -133.87
REMARK 500 LYS E 99 59.77 75.09
REMARK 500 ASN E 216 71.47 46.96
REMARK 500 LYS E 264 40.81 -80.11
REMARK 500 ASP E 269 122.59 -30.21
REMARK 500 PHE E 273 149.62 -176.89
REMARK 500 THR E 399 -61.59 -107.80
REMARK 500 ASP F 3 157.32 -47.14
REMARK 500 ASN F 47 16.00 82.33
REMARK 500 PHE F 55 131.30 -176.78
REMARK 500 LEU G 2 -64.55 83.78
REMARK 500 PHE G 65 -61.69 -26.72
REMARK 500
REMARK 500 THIS ENTRY HAS 187 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL B 217 ASN B 218 -143.76
REMARK 500 GLY B 411 LEU B 412 -142.01
REMARK 500 TYR E 97 GLU E 98 145.87
REMARK 500 VAL E 217 ASN E 218 -138.43
REMARK 500 THR F 45 GLU F 46 141.34
REMARK 500 SER M 394 PRO M 395 148.13
REMARK 500 GLY T 411 LEU T 412 -145.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 479 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 14 NE2
REMARK 620 2 GLU B 127 OE2 93.1
REMARK 620 3 GLU B 153 OE1 99.9 82.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 25 SG
REMARK 620 2 CYS B 27 SG 116.5
REMARK 620 3 CYS B 40 SG 115.3 84.5
REMARK 620 4 CYS B 43 SG 109.0 110.1 119.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 25 SG
REMARK 620 2 CYS E 27 SG 109.8
REMARK 620 3 CYS E 40 SG 116.7 103.0
REMARK 620 4 CYS E 43 SG 107.2 105.4 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 479 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 14 NE2
REMARK 620 2 GLU H 127 OE2 78.6
REMARK 620 3 GLU H 153 OE1 93.6 80.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 903 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 25 SG
REMARK 620 2 CYS H 27 SG 109.1
REMARK 620 3 CYS H 40 SG 109.6 100.3
REMARK 620 4 CYS H 43 SG 113.3 112.4 111.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 479 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 14 NE2
REMARK 620 2 GLU K 127 OE2 88.6
REMARK 620 3 GLU K 153 OE1 99.2 81.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 904 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 25 SG
REMARK 620 2 CYS K 27 SG 123.5
REMARK 620 3 CYS K 40 SG 114.3 106.2
REMARK 620 4 CYS K 43 SG 105.5 102.1 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 479 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 14 NE2
REMARK 620 2 GLU N 127 OE2 79.5
REMARK 620 3 GLU N 153 OE1 101.0 83.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN N 905 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 25 SG
REMARK 620 2 CYS N 27 SG 119.1
REMARK 620 3 CYS N 40 SG 113.3 103.9
REMARK 620 4 CYS N 43 SG 109.7 101.9 107.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Q 479 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 14 NE2
REMARK 620 2 GLU Q 127 OE2 97.2
REMARK 620 3 GLU Q 153 OE1 99.1 80.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Q 906 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 25 SG
REMARK 620 2 CYS Q 27 SG 126.6
REMARK 620 3 CYS Q 40 SG 112.8 103.9
REMARK 620 4 CYS Q 43 SG 107.7 103.4 98.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG T 479 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS T 14 NE2
REMARK 620 2 GLU T 127 OE2 103.0
REMARK 620 3 GLU T 153 OE1 104.7 107.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN T 907 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 25 SG
REMARK 620 2 CYS T 27 SG 101.8
REMARK 620 3 CYS T 40 SG 109.1 99.3
REMARK 620 4 CYS T 43 SG 118.5 118.8 107.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG W 479 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS W 14 NE2
REMARK 620 2 GLU W 127 OE2 101.7
REMARK 620 3 GLU W 153 OE1 117.3 102.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN W 908 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS W 25 SG
REMARK 620 2 CYS W 27 SG 120.2
REMARK 620 3 CYS W 40 SG 114.3 110.1
REMARK 620 4 CYS W 43 SG 106.5 103.9 99.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN D 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN G 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN J 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN M 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN P 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN S 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN V 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG W 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Q 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN T 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN W 908
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G5I RELATED DB: PDB
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM
REMARK 900 STAPHYLOCOCCUS AUREUS WITH ADP
REMARK 900 RELATED ID: 2G5H RELATED DB: PDB
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM
REMARK 900 STAPHYLOCOCCUS AUREUS WITH MG2+
REMARK 900 RELATED ID: 2F2A RELATED DB: PDB
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM
REMARK 900 STAPHYLOCOCCUS AUREUS WITH MG2+ AND GLN
REMARK 900 RELATED ID: 2DF4 RELATED DB: PDB
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM
REMARK 900 STAPHYLOCOCCUS AUREUS WITH MN2+
REMARK 900 RELATED ID: 2GI3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A
REMARK 900 (TM1272) FROM THERMOTOGA MARITIMA AT 1.80 A RESOLUTION
REMARK 900 RELATED ID: 3H0L RELATED DB: PDB
DBREF 3H0M A 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M B 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M C 1 94 UNP O67904 GATC_AQUAE 1 94
DBREF 3H0M D 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M E 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M F 1 94 UNP O67904 GATC_AQUAE 1 94
DBREF 3H0M G 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M H 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M I 1 94 UNP O67904 GATC_AQUAE 1 94
DBREF 3H0M J 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M K 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M L 1 94 UNP O67904 GATC_AQUAE 1 94
DBREF 3H0M M 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M N 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M O 1 94 UNP O67904 GATC_AQUAE 1 94
DBREF 3H0M P 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M Q 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M R 1 94 UNP O67904 GATC_AQUAE 1 94
DBREF 3H0M S 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M T 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M U 1 94 UNP O67904 GATC_AQUAE 1 94
DBREF 3H0M V 1 478 UNP O66610 GATA_AQUAE 1 478
DBREF 3H0M W 1 478 UNP O66766 GATB_AQUAE 1 478
DBREF 3H0M X 1 94 UNP O67904 GATC_AQUAE 1 94
SEQRES 1 A 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 A 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 A 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 A 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 A 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 A 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 A 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 A 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 A 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 A 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 A 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 A 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 A 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 A 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 A 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 A 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 A 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 A 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 A 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 A 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 A 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 A 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 A 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 A 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 A 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 A 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 A 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 A 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 A 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 A 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 A 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 A 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 A 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 A 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 A 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 A 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 A 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 B 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 B 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 B 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 B 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 B 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 B 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 B 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 B 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 B 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 B 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 B 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 B 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 B 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 B 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 B 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 B 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 B 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 B 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 B 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 B 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 B 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 B 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 B 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 B 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 B 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 B 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 B 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 B 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 B 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 B 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 B 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 B 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 B 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 B 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 B 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 B 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 B 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 C 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 C 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 C 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 C 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 C 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 C 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 C 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 C 94 VAL GLU VAL
SEQRES 1 D 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 D 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 D 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 D 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 D 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 D 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 D 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 D 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 D 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 D 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 D 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 D 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 D 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 D 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 D 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 D 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 D 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 D 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 D 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 D 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 D 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 D 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 D 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 D 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 D 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 D 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 D 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 D 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 D 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 D 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 D 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 D 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 D 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 D 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 D 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 D 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 D 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 E 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 E 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 E 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 E 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 E 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 E 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 E 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 E 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 E 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 E 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 E 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 E 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 E 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 E 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 E 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 E 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 E 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 E 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 E 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 E 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 E 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 E 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 E 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 E 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 E 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 E 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 E 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 E 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 E 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 E 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 E 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 E 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 E 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 E 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 E 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 E 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 E 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 F 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 F 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 F 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 F 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 F 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 F 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 F 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 F 94 VAL GLU VAL
SEQRES 1 G 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 G 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 G 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 G 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 G 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 G 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 G 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 G 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 G 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 G 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 G 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 G 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 G 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 G 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 G 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 G 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 G 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 G 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 G 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 G 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 G 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 G 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 G 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 G 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 G 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 G 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 G 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 G 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 G 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 G 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 G 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 G 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 G 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 G 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 G 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 G 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 G 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 H 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 H 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 H 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 H 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 H 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 H 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 H 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 H 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 H 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 H 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 H 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 H 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 H 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 H 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 H 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 H 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 H 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 H 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 H 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 H 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 H 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 H 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 H 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 H 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 H 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 H 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 H 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 H 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 H 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 H 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 H 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 H 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 H 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 H 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 H 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 H 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 H 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 I 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 I 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 I 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 I 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 I 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 I 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 I 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 I 94 VAL GLU VAL
SEQRES 1 J 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 J 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 J 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 J 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 J 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 J 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 J 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 J 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 J 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 J 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 J 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 J 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 J 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 J 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 J 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 J 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 J 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 J 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 J 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 J 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 J 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 J 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 J 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 J 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 J 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 J 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 J 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 J 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 J 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 J 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 J 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 J 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 J 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 J 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 J 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 J 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 J 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 K 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 K 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 K 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 K 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 K 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 K 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 K 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 K 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 K 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 K 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 K 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 K 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 K 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 K 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 K 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 K 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 K 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 K 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 K 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 K 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 K 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 K 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 K 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 K 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 K 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 K 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 K 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 K 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 K 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 K 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 K 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 K 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 K 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 K 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 K 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 K 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 K 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 L 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 L 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 L 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 L 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 L 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 L 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 L 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 L 94 VAL GLU VAL
SEQRES 1 M 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 M 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 M 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 M 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 M 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 M 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 M 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 M 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 M 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 M 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 M 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 M 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 M 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 M 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 M 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 M 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 M 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 M 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 M 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 M 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 M 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 M 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 M 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 M 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 M 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 M 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 M 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 M 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 M 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 M 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 M 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 M 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 M 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 M 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 M 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 M 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 M 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 N 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 N 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 N 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 N 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 N 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 N 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 N 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 N 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 N 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 N 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 N 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 N 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 N 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 N 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 N 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 N 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 N 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 N 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 N 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 N 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 N 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 N 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 N 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 N 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 N 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 N 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 N 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 N 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 N 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 N 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 N 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 N 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 N 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 N 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 N 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 N 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 N 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 O 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 O 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 O 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 O 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 O 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 O 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 O 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 O 94 VAL GLU VAL
SEQRES 1 P 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 P 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 P 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 P 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 P 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 P 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 P 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 P 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 P 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 P 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 P 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 P 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 P 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 P 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 P 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 P 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 P 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 P 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 P 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 P 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 P 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 P 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 P 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 P 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 P 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 P 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 P 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 P 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 P 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 P 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 P 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 P 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 P 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 P 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 P 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 P 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 P 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 Q 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 Q 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 Q 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 Q 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 Q 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 Q 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 Q 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 Q 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 Q 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 Q 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 Q 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 Q 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 Q 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 Q 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 Q 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 Q 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 Q 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 Q 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 Q 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 Q 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 Q 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 Q 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 Q 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 Q 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 Q 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 Q 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 Q 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 Q 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 Q 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 Q 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 Q 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 Q 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 Q 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 Q 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 Q 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 Q 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 Q 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 R 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 R 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 R 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 R 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 R 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 R 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 R 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 R 94 VAL GLU VAL
SEQRES 1 S 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 S 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 S 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 S 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 S 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 S 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 S 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 S 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 S 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 S 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 S 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 S 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 S 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 S 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 S 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 S 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 S 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 S 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 S 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 S 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 S 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 S 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 S 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 S 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 S 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 S 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 S 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 S 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 S 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 S 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 S 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 S 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 S 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 S 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 S 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 S 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 S 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 T 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 T 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 T 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 T 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 T 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 T 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 T 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 T 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 T 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 T 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 T 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 T 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 T 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 T 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 T 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 T 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 T 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 T 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 T 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 T 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 T 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 T 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 T 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 T 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 T 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 T 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 T 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 T 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 T 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 T 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 T 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 T 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 T 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 T 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 T 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 T 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 T 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 U 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 U 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 U 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 U 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 U 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 U 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 U 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 U 94 VAL GLU VAL
SEQRES 1 V 478 MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU
SEQRES 2 V 478 LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU
SEQRES 3 V 478 SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL
SEQRES 4 V 478 LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS
SEQRES 5 V 478 GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE
SEQRES 6 V 478 GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU
SEQRES 7 V 478 GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN
SEQRES 8 V 478 PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU
SEQRES 9 V 478 LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU
SEQRES 10 V 478 ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA
SEQRES 11 V 478 PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL
SEQRES 12 V 478 PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA
SEQRES 13 V 478 VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY
SEQRES 14 V 478 GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE
SEQRES 15 V 478 GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY
SEQRES 16 V 478 LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL
SEQRES 17 V 478 PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU
SEQRES 18 V 478 VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA
SEQRES 19 V 478 LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS
SEQRES 20 V 478 GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE
SEQRES 21 V 478 PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE
SEQRES 22 V 478 GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU
SEQRES 23 V 478 ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE
SEQRES 24 V 478 PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER
SEQRES 25 V 478 ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG
SEQRES 26 V 478 ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG
SEQRES 27 V 478 THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG
SEQRES 28 V 478 ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR
SEQRES 29 V 478 ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU
SEQRES 30 V 478 ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP
SEQRES 31 V 478 VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS
SEQRES 32 V 478 PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU
SEQRES 33 V 478 SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU
SEQRES 34 V 478 PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU
SEQRES 35 V 478 PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU
SEQRES 36 V 478 THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS
SEQRES 37 V 478 PHE LYS HIS TYR GLU LYS ILE PRO LEU THR
SEQRES 1 W 478 MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE
SEQRES 2 W 478 HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY
SEQRES 3 W 478 CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL
SEQRES 4 W 478 CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE
SEQRES 5 W 478 VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER
SEQRES 6 W 478 LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE
SEQRES 7 W 478 ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY
SEQRES 8 W 478 TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN
SEQRES 9 W 478 GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS
SEQRES 10 W 478 LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA
SEQRES 11 W 478 GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP
SEQRES 12 W 478 LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR
SEQRES 13 W 478 GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE
SEQRES 14 W 478 LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL
SEQRES 15 W 478 SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP
SEQRES 16 W 478 ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE
SEQRES 17 W 478 GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG
SEQRES 18 W 478 PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN
SEQRES 19 W 478 ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU
SEQRES 20 W 478 THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO
SEQRES 21 W 478 MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE
SEQRES 22 W 478 PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU
SEQRES 23 W 478 TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO
SEQRES 24 W 478 ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU
SEQRES 25 W 478 SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU
SEQRES 26 W 478 VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS
SEQRES 27 W 478 GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU
SEQRES 28 W 478 LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU
SEQRES 29 W 478 SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS
SEQRES 30 W 478 LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS
SEQRES 31 W 478 GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO
SEQRES 32 W 478 SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR
SEQRES 33 W 478 ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE
SEQRES 34 W 478 GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY
SEQRES 35 W 478 GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET
SEQRES 36 W 478 ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN
SEQRES 37 W 478 LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL
SEQRES 1 X 94 MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU
SEQRES 2 X 94 ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE
SEQRES 3 X 94 GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN
SEQRES 4 X 94 LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE
SEQRES 5 X 94 GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO
SEQRES 6 X 94 HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA
SEQRES 7 X 94 PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL
SEQRES 8 X 94 VAL GLU VAL
HET GLN A 901 9
HET MG B 479 1
HET ZN B 901 1
HET GLN D 902 9
HET ZN E 902 1
HET GLN G 903 9
HET MG H 479 1
HET ZN H 903 1
HET GLN J 904 9
HET MG K 479 1
HET ZN K 904 1
HET GLN M 905 9
HET MG N 479 1
HET ZN N 905 1
HET GLN P 906 9
HET MG Q 479 1
HET ZN Q 906 1
HET GLN S 907 9
HET MG T 479 1
HET ZN T 907 1
HET GLN V 908 9
HET MG W 479 1
HET ZN W 908 1
HETNAM GLN GLUTAMINE
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
FORMUL 25 GLN 8(C5 H10 N2 O3)
FORMUL 26 MG 7(MG 2+)
FORMUL 27 ZN 8(ZN 2+)
HELIX 1 1 SER A 6 ARG A 16 1 11
HELIX 2 2 SER A 20 LYS A 40 1 21
HELIX 3 3 LEU A 46 SER A 56 1 11
HELIX 4 4 SER A 86 GLU A 90 5 5
HELIX 5 5 ALA A 98 ALA A 107 1 10
HELIX 6 6 ASP A 118 MET A 122 5 5
HELIX 7 7 SER A 148 VAL A 157 1 10
HELIX 8 8 ILE A 172 CYS A 179 1 8
HELIX 9 9 ARG A 212 SER A 224 1 13
HELIX 10 10 GLU A 240 GLU A 244 5 5
HELIX 11 11 GLU A 259 TYR A 263 5 5
HELIX 12 12 GLN A 266 GLU A 283 1 18
HELIX 13 13 HIS A 294 LYS A 296 5 3
HELIX 14 14 TYR A 297 LEU A 314 1 18
HELIX 15 15 ASP A 331 PHE A 344 1 14
HELIX 16 16 GLY A 345 LEU A 359 1 15
HELIX 17 17 TYR A 367 VAL A 389 1 23
HELIX 18 18 ASN A 410 LEU A 416 1 7
HELIX 19 19 SER A 417 ILE A 419 5 3
HELIX 20 20 THR A 421 ALA A 427 1 7
HELIX 21 21 ASP A 454 PHE A 469 1 16
HELIX 22 22 LYS A 470 LYS A 474 5 5
HELIX 23 23 LYS B 55 LEU B 68 1 14
HELIX 24 24 THR B 162 GLY B 181 1 20
HELIX 25 25 ASP B 186 GLY B 190 5 5
HELIX 26 26 SER B 219 GLU B 240 1 22
HELIX 27 27 LYS B 284 ASN B 294 1 11
HELIX 28 28 LEU B 298 TYR B 310 1 13
HELIX 29 29 SER B 313 HIS B 323 1 11
HELIX 30 30 HIS B 323 PHE B 337 1 15
HELIX 31 31 GLU B 339 ASN B 349 1 11
HELIX 32 32 ASP B 350 GLY B 359 1 10
HELIX 33 33 SER B 361 SER B 365 5 5
HELIX 34 34 LYS B 368 GLU B 381 1 14
HELIX 35 35 SER B 385 THR B 399 1 15
HELIX 36 36 THR B 402 LYS B 410 1 9
HELIX 37 37 ASP C 3 ARG C 15 1 13
HELIX 38 38 LYS C 19 ASP C 38 1 20
HELIX 39 39 ASP C 70 MET C 76 1 7
HELIX 40 40 SER D 6 ARG D 16 1 11
HELIX 41 41 SER D 20 LYS D 40 1 21
HELIX 42 42 LEU D 46 SER D 56 1 11
HELIX 43 43 SER D 86 GLU D 90 5 5
HELIX 44 44 ALA D 98 ALA D 107 1 10
HELIX 45 45 ASP D 118 MET D 122 5 5
HELIX 46 46 SER D 148 VAL D 157 1 10
HELIX 47 47 ILE D 172 GLY D 180 1 9
HELIX 48 48 ARG D 212 SER D 224 1 13
HELIX 49 49 GLU D 240 GLU D 244 5 5
HELIX 50 50 GLU D 259 TYR D 263 5 5
HELIX 51 51 GLN D 266 GLY D 284 1 19
HELIX 52 52 HIS D 294 LYS D 296 5 3
HELIX 53 53 TYR D 297 LEU D 314 1 18
HELIX 54 54 ASP D 331 PHE D 344 1 14
HELIX 55 55 GLY D 345 LEU D 359 1 15
HELIX 56 56 TYR D 367 VAL D 389 1 23
HELIX 57 57 ASN D 410 LEU D 416 1 7
HELIX 58 58 SER D 417 ILE D 419 5 3
HELIX 59 59 THR D 421 ALA D 427 1 7
HELIX 60 60 ASP D 454 PHE D 469 1 16
HELIX 61 61 LYS D 470 LYS D 474 5 5
HELIX 62 62 CYS E 40 GLY E 45 1 6
HELIX 63 63 ASN E 54 LEU E 68 1 15
HELIX 64 64 THR E 162 GLY E 181 1 20
HELIX 65 65 ASP E 186 GLY E 190 5 5
HELIX 66 66 SER E 219 GLU E 240 1 22
HELIX 67 67 LYS E 284 ASN E 294 1 11
HELIX 68 68 LEU E 298 GLY E 311 1 14
HELIX 69 69 SER E 313 HIS E 323 1 11
HELIX 70 70 HIS E 323 PHE E 337 1 15
HELIX 71 71 GLU E 339 ASP E 350 1 12
HELIX 72 72 ASP E 350 GLY E 359 1 10
HELIX 73 73 LYS E 368 GLU E 381 1 14
HELIX 74 74 SER E 385 GLY E 400 1 16
HELIX 75 75 THR E 402 LYS E 410 1 9
HELIX 76 76 ASP F 3 ARG F 15 1 13
HELIX 77 77 LYS F 19 ASP F 38 1 20
HELIX 78 78 ASP F 70 MET F 76 1 7
HELIX 79 79 SER G 6 ARG G 16 1 11
HELIX 80 80 SER G 20 LYS G 40 1 21
HELIX 81 81 LEU G 46 SER G 56 1 11
HELIX 82 82 SER G 86 GLU G 90 5 5
HELIX 83 83 ALA G 98 ALA G 107 1 10
HELIX 84 84 ASP G 118 MET G 122 5 5
HELIX 85 85 SER G 148 VAL G 157 1 10
HELIX 86 86 ILE G 172 CYS G 179 1 8
HELIX 87 87 ARG G 212 SER G 224 1 13
HELIX 88 88 GLU G 240 GLU G 244 5 5
HELIX 89 89 GLU G 259 TYR G 263 5 5
HELIX 90 90 GLN G 266 GLU G 283 1 18
HELIX 91 91 HIS G 294 LYS G 296 5 3
HELIX 92 92 TYR G 297 LEU G 314 1 18
HELIX 93 93 ASP G 331 PHE G 344 1 14
HELIX 94 94 GLY G 345 LEU G 359 1 15
HELIX 95 95 TYR G 367 PHE G 386 1 20
HELIX 96 96 ASN G 410 LEU G 416 1 7
HELIX 97 97 SER G 417 ILE G 419 5 3
HELIX 98 98 THR G 421 ALA G 427 1 7
HELIX 99 99 ASP G 454 PHE G 469 1 16
HELIX 100 100 LYS G 470 LYS G 474 5 5
HELIX 101 101 LYS H 55 LEU H 68 1 14
HELIX 102 102 THR H 162 GLY H 181 1 20
HELIX 103 103 ASP H 186 GLY H 190 5 5
HELIX 104 104 SER H 219 GLU H 240 1 22
HELIX 105 105 LYS H 284 ASN H 294 1 11
HELIX 106 106 LEU H 298 GLY H 311 1 14
HELIX 107 107 SER H 313 HIS H 323 1 11
HELIX 108 108 HIS H 323 PHE H 337 1 15
HELIX 109 109 GLU H 339 ASP H 350 1 12
HELIX 110 110 ASP H 350 GLY H 359 1 10
HELIX 111 111 LYS H 368 GLU H 381 1 14
HELIX 112 112 SER H 385 THR H 399 1 15
HELIX 113 113 THR H 402 LYS H 410 1 9
HELIX 114 114 ASP I 3 ARG I 15 1 13
HELIX 115 115 LYS I 19 ASP I 38 1 20
HELIX 116 116 ASP I 70 MET I 76 1 7
HELIX 117 117 SER J 6 ARG J 16 1 11
HELIX 118 118 SER J 20 LYS J 40 1 21
HELIX 119 119 LEU J 46 SER J 56 1 11
HELIX 120 120 SER J 86 GLU J 90 5 5
HELIX 121 121 ALA J 98 ALA J 107 1 10
HELIX 122 122 ASP J 118 MET J 122 5 5
HELIX 123 123 SER J 148 VAL J 157 1 10
HELIX 124 124 ILE J 172 GLY J 180 1 9
HELIX 125 125 ARG J 212 SER J 224 1 13
HELIX 126 126 GLU J 240 GLU J 244 5 5
HELIX 127 127 GLU J 259 TYR J 263 5 5
HELIX 128 128 GLN J 266 GLU J 283 1 18
HELIX 129 129 HIS J 294 LYS J 296 5 3
HELIX 130 130 TYR J 297 LEU J 314 1 18
HELIX 131 131 ASP J 331 PHE J 344 1 14
HELIX 132 132 GLY J 345 LEU J 359 1 15
HELIX 133 133 TYR J 367 PHE J 386 1 20
HELIX 134 134 ASN J 410 LEU J 416 1 7
HELIX 135 135 SER J 417 ILE J 419 5 3
HELIX 136 136 THR J 421 ALA J 427 1 7
HELIX 137 137 ASP J 454 PHE J 469 1 16
HELIX 138 138 LYS J 470 LYS J 474 5 5
HELIX 139 139 LYS K 55 LEU K 68 1 14
HELIX 140 140 THR K 162 GLY K 181 1 20
HELIX 141 141 ASP K 186 GLY K 190 5 5
HELIX 142 142 SER K 219 GLU K 240 1 22
HELIX 143 143 LYS K 284 ASN K 294 1 11
HELIX 144 144 LEU K 298 GLY K 311 1 14
HELIX 145 145 SER K 313 HIS K 323 1 11
HELIX 146 146 HIS K 323 PHE K 337 1 15
HELIX 147 147 GLU K 339 ASP K 350 1 12
HELIX 148 148 ASP K 350 GLY K 359 1 10
HELIX 149 149 LYS K 368 GLU K 381 1 14
HELIX 150 150 SER K 385 THR K 399 1 15
HELIX 151 151 THR K 402 GLU K 409 1 8
HELIX 152 152 ASP L 3 ARG L 15 1 13
HELIX 153 153 LYS L 19 ASP L 38 1 20
HELIX 154 154 GLN L 39 LEU L 43 5 5
HELIX 155 155 ASP L 70 MET L 76 1 7
HELIX 156 156 SER M 6 ARG M 16 1 11
HELIX 157 157 SER M 20 LYS M 40 1 21
HELIX 158 158 LEU M 46 SER M 56 1 11
HELIX 159 159 SER M 86 GLU M 90 5 5
HELIX 160 160 ALA M 98 ALA M 107 1 10
HELIX 161 161 ASP M 118 MET M 122 5 5
HELIX 162 162 SER M 148 VAL M 157 1 10
HELIX 163 163 ILE M 172 CYS M 179 1 8
HELIX 164 164 ARG M 212 SER M 224 1 13
HELIX 165 165 GLU M 240 GLU M 244 5 5
HELIX 166 166 GLU M 259 TYR M 263 5 5
HELIX 167 167 GLN M 266 GLU M 283 1 18
HELIX 168 168 HIS M 294 LYS M 296 5 3
HELIX 169 169 TYR M 297 LEU M 314 1 18
HELIX 170 170 ASP M 331 PHE M 344 1 14
HELIX 171 171 GLY M 345 LEU M 359 1 15
HELIX 172 172 TYR M 367 PHE M 386 1 20
HELIX 173 173 ASN M 410 LEU M 416 1 7
HELIX 174 174 SER M 417 ILE M 419 5 3
HELIX 175 175 THR M 421 ALA M 427 1 7
HELIX 176 176 ASP M 454 PHE M 469 1 16
HELIX 177 177 LYS M 470 LYS M 474 5 5
HELIX 178 178 LYS N 55 LEU N 68 1 14
HELIX 179 179 THR N 162 GLY N 181 1 20
HELIX 180 180 ASP N 186 GLY N 190 5 5
HELIX 181 181 SER N 219 GLU N 240 1 22
HELIX 182 182 LYS N 284 ASN N 294 1 11
HELIX 183 183 LEU N 298 TYR N 310 1 13
HELIX 184 184 SER N 313 HIS N 323 1 11
HELIX 185 185 HIS N 323 VAL N 334 1 12
HELIX 186 186 GLU N 339 ASP N 350 1 12
HELIX 187 187 ASP N 350 GLY N 359 1 10
HELIX 188 188 LYS N 368 GLU N 381 1 14
HELIX 189 189 SER N 385 THR N 399 1 15
HELIX 190 190 THR N 402 LYS N 410 1 9
HELIX 191 191 ASP O 3 ARG O 15 1 13
HELIX 192 192 LYS O 19 ASP O 38 1 20
HELIX 193 193 ASP O 70 MET O 76 1 7
HELIX 194 194 SER P 6 ARG P 16 1 11
HELIX 195 195 SER P 20 LYS P 40 1 21
HELIX 196 196 LEU P 46 SER P 56 1 11
HELIX 197 197 SER P 86 GLU P 90 5 5
HELIX 198 198 ALA P 98 LYS P 106 1 9
HELIX 199 199 ASP P 118 MET P 122 5 5
HELIX 200 200 SER P 148 VAL P 157 1 10
HELIX 201 201 ILE P 172 GLY P 180 1 9
HELIX 202 202 ARG P 212 SER P 224 1 13
HELIX 203 203 GLU P 240 GLU P 244 5 5
HELIX 204 204 GLU P 259 TYR P 263 5 5
HELIX 205 205 GLN P 266 GLU P 283 1 18
HELIX 206 206 HIS P 294 LYS P 296 5 3
HELIX 207 207 TYR P 297 LEU P 314 1 18
HELIX 208 208 ASP P 331 PHE P 344 1 14
HELIX 209 209 GLY P 345 LEU P 359 1 15
HELIX 210 210 TYR P 367 PHE P 386 1 20
HELIX 211 211 ASN P 410 LEU P 416 1 7
HELIX 212 212 SER P 417 ILE P 419 5 3
HELIX 213 213 THR P 421 ALA P 427 1 7
HELIX 214 214 ASP P 454 PHE P 469 1 16
HELIX 215 215 LYS P 470 LYS P 474 5 5
HELIX 216 216 LYS Q 55 LEU Q 68 1 14
HELIX 217 217 THR Q 162 GLY Q 181 1 20
HELIX 218 218 ASP Q 186 GLY Q 190 5 5
HELIX 219 219 SER Q 219 GLU Q 240 1 22
HELIX 220 220 LYS Q 284 ASN Q 294 1 11
HELIX 221 221 LEU Q 298 GLY Q 311 1 14
HELIX 222 222 SER Q 313 HIS Q 323 1 11
HELIX 223 223 HIS Q 323 PHE Q 337 1 15
HELIX 224 224 GLU Q 339 ASP Q 350 1 12
HELIX 225 225 ASP Q 350 GLY Q 359 1 10
HELIX 226 226 LYS Q 368 GLU Q 381 1 14
HELIX 227 227 SER Q 385 THR Q 399 1 15
HELIX 228 228 THR Q 402 GLU Q 409 1 8
HELIX 229 229 ASP R 3 ARG R 15 1 13
HELIX 230 230 LYS R 19 ASP R 38 1 20
HELIX 231 231 ASP R 70 MET R 76 1 7
HELIX 232 232 SER S 6 ARG S 16 1 11
HELIX 233 233 SER S 20 LYS S 40 1 21
HELIX 234 234 LEU S 46 SER S 56 1 11
HELIX 235 235 SER S 86 GLU S 90 5 5
HELIX 236 236 ALA S 98 LYS S 106 1 9
HELIX 237 237 ASP S 118 MET S 122 5 5
HELIX 238 238 SER S 148 VAL S 157 1 10
HELIX 239 239 ILE S 172 GLY S 180 1 9
HELIX 240 240 ARG S 212 SER S 224 1 13
HELIX 241 241 GLU S 240 GLU S 244 5 5
HELIX 242 242 GLU S 259 TYR S 263 5 5
HELIX 243 243 GLN S 266 GLU S 283 1 18
HELIX 244 244 HIS S 294 LYS S 296 5 3
HELIX 245 245 TYR S 297 LEU S 314 1 18
HELIX 246 246 ASP S 331 PHE S 344 1 14
HELIX 247 247 GLY S 345 LEU S 359 1 15
HELIX 248 248 TYR S 367 VAL S 389 1 23
HELIX 249 249 ASN S 410 LEU S 416 1 7
HELIX 250 250 SER S 417 ILE S 419 5 3
HELIX 251 251 THR S 421 ALA S 427 1 7
HELIX 252 252 ASP S 454 PHE S 469 1 16
HELIX 253 253 LYS S 470 LYS S 474 5 5
HELIX 254 254 ASN T 54 LEU T 68 1 15
HELIX 255 255 THR T 162 GLY T 181 1 20
HELIX 256 256 ASP T 186 GLY T 190 5 5
HELIX 257 257 SER T 219 GLU T 240 1 22
HELIX 258 258 LYS T 284 ASN T 294 1 11
HELIX 259 259 LEU T 298 GLY T 311 1 14
HELIX 260 260 SER T 313 HIS T 323 1 11
HELIX 261 261 HIS T 323 PHE T 337 1 15
HELIX 262 262 GLU T 339 ASP T 350 1 12
HELIX 263 263 ASP T 350 GLY T 359 1 10
HELIX 264 264 LYS T 368 GLU T 381 1 14
HELIX 265 265 SER T 385 GLY T 400 1 16
HELIX 266 266 THR T 402 LYS T 410 1 9
HELIX 267 267 ASP U 3 ARG U 15 1 13
HELIX 268 268 LYS U 19 ASP U 38 1 20
HELIX 269 269 GLN U 39 LEU U 43 5 5
HELIX 270 270 ASP U 70 MET U 76 1 7
HELIX 271 271 SER V 6 ARG V 16 1 11
HELIX 272 272 SER V 20 LYS V 40 1 21
HELIX 273 273 LEU V 46 SER V 56 1 11
HELIX 274 274 SER V 86 GLU V 90 5 5
HELIX 275 275 ALA V 98 ALA V 107 1 10
HELIX 276 276 ASP V 118 MET V 122 5 5
HELIX 277 277 SER V 148 VAL V 157 1 10
HELIX 278 278 ILE V 172 CYS V 179 1 8
HELIX 279 279 ARG V 212 SER V 224 1 13
HELIX 280 280 GLU V 240 GLU V 244 5 5
HELIX 281 281 GLU V 259 TYR V 263 5 5
HELIX 282 282 GLN V 266 GLU V 283 1 18
HELIX 283 283 HIS V 294 LYS V 296 5 3
HELIX 284 284 TYR V 297 LEU V 314 1 18
HELIX 285 285 ASP V 331 PHE V 344 1 14
HELIX 286 286 GLY V 345 LEU V 359 1 15
HELIX 287 287 TYR V 367 VAL V 389 1 23
HELIX 288 288 ASN V 410 LEU V 416 1 7
HELIX 289 289 SER V 417 ILE V 419 5 3
HELIX 290 290 THR V 421 ALA V 427 1 7
HELIX 291 291 ASP V 454 PHE V 469 1 16
HELIX 292 292 LYS V 470 LYS V 474 5 5
HELIX 293 293 ASN W 54 LEU W 68 1 15
HELIX 294 294 THR W 162 GLY W 181 1 20
HELIX 295 295 ASP W 186 GLY W 190 5 5
HELIX 296 296 SER W 219 GLU W 240 1 22
HELIX 297 297 LYS W 284 ASN W 294 1 11
HELIX 298 298 LEU W 298 TYR W 310 1 13
HELIX 299 299 SER W 313 HIS W 323 1 11
HELIX 300 300 HIS W 323 PHE W 337 1 15
HELIX 301 301 GLU W 339 ASP W 350 1 12
HELIX 302 302 ASP W 350 GLY W 359 1 10
HELIX 303 303 SER W 361 SER W 365 5 5
HELIX 304 304 LYS W 368 GLU W 381 1 14
HELIX 305 305 SER W 385 GLY W 400 1 16
HELIX 306 306 THR W 402 LYS W 410 1 9
HELIX 307 307 ASP X 3 ARG X 15 1 13
HELIX 308 308 LYS X 19 ASP X 38 1 20
HELIX 309 309 GLN X 39 LEU X 43 5 5
HELIX 310 310 ASP X 70 MET X 76 1 7
SHEET 1 A11 TYR A 42 PRO A 45 0
SHEET 2 A11 LEU A 110 THR A 115 -1 O LYS A 114 N ILE A 43
SHEET 3 A11 PRO A 68 LYS A 72 1 N VAL A 71 O THR A 115
SHEET 4 A11 SER A 163 SER A 166 1 O LEU A 164 N ALA A 70
SHEET 5 A11 ILE A 206 GLY A 210 -1 O PHE A 209 N SER A 163
SHEET 6 A11 ILE A 182 LYS A 185 -1 N ILE A 182 O GLY A 210
SHEET 7 A11 ALA A 431 LYS A 439 -1 O SER A 433 N GLY A 183
SHEET 8 A11 LEU A 442 ILE A 449 -1 O GLY A 446 N ILE A 434
SHEET 9 A11 VAL A 391 PRO A 395 -1 N SER A 394 O GLN A 447
SHEET 10 A11 LYS A 253 PRO A 257 1 N GLY A 255 O ALA A 393
SHEET 11 A11 GLU A 286 VAL A 290 1 O LYS A 288 N ILE A 254
SHEET 1 B 9 GLU B 71 VAL B 72 0
SHEET 2 B 9 ALA B 102 ASN B 110 -1 O THR B 103 N GLU B 71
SHEET 3 B 9 LYS B 116 GLU B 128 -1 O VAL B 119 N VAL B 107
SHEET 4 B 9 PRO B 150 THR B 156 -1 O LEU B 151 N GLU B 127
SHEET 5 B 9 TYR B 5 GLN B 16 -1 N ILE B 13 O ILE B 154
SHEET 6 B 9 LEU B 192 PRO B 202 -1 O SER B 199 N VAL B 8
SHEET 7 B 9 VAL B 212 LYS B 215 -1 O ILE B 214 N ILE B 196
SHEET 8 B 9 THR B 248 ASP B 252 1 O ARG B 249 N GLU B 213
SHEET 9 B 9 LYS B 257 TYR B 259 -1 O TYR B 259 N THR B 250
SHEET 1 C 2 VAL B 53 ASN B 54 0
SHEET 2 C 2 MET C 60 ARG C 61 1 O ARG C 61 N VAL B 53
SHEET 1 D 2 GLU B 75 SER B 76 0
SHEET 2 D 2 LEU B 281 LYS B 282 -1 O LEU B 281 N SER B 76
SHEET 1 E 3 TYR B 92 GLN B 96 0
SHEET 2 E 3 PHE B 78 HIS B 82 -1 N LYS B 81 O GLN B 93
SHEET 3 E 3 PHE B 273 PRO B 274 -1 O PHE B 273 N ARG B 80
SHEET 1 F 4 LYS B 132 GLU B 136 0
SHEET 2 F 4 LYS B 139 ASP B 143 -1 O LEU B 141 N ILE B 134
SHEET 3 F 4 PHE C 85 PRO C 89 -1 O VAL C 88 N THR B 140
SHEET 4 F 4 ARG C 81 LYS C 82 -1 N LYS C 82 O PHE C 85
SHEET 1 G11 TYR D 42 PRO D 45 0
SHEET 2 G11 LEU D 110 THR D 115 -1 O LYS D 114 N ILE D 43
SHEET 3 G11 PRO D 68 LYS D 72 1 N VAL D 71 O THR D 115
SHEET 4 G11 SER D 163 SER D 166 1 O LEU D 164 N ALA D 70
SHEET 5 G11 ILE D 206 GLY D 210 -1 O PHE D 209 N SER D 163
SHEET 6 G11 ILE D 182 LYS D 185 -1 N ILE D 182 O GLY D 210
SHEET 7 G11 ALA D 431 LYS D 439 -1 O SER D 433 N GLY D 183
SHEET 8 G11 LEU D 442 ILE D 449 -1 O GLY D 446 N ILE D 434
SHEET 9 G11 VAL D 391 PRO D 395 -1 N SER D 394 O GLN D 447
SHEET 10 G11 LYS D 253 PRO D 257 1 N GLY D 255 O VAL D 391
SHEET 11 G11 GLU D 286 VAL D 290 1 O LYS D 288 N ILE D 254
SHEET 1 H 9 GLU E 71 VAL E 72 0
SHEET 2 H 9 ALA E 102 ASN E 110 -1 O THR E 103 N GLU E 71
SHEET 3 H 9 LYS E 116 GLU E 128 -1 O VAL E 119 N VAL E 107
SHEET 4 H 9 PRO E 150 THR E 156 -1 O LEU E 151 N GLU E 127
SHEET 5 H 9 TYR E 5 GLN E 16 -1 N ILE E 13 O ILE E 154
SHEET 6 H 9 LEU E 192 PRO E 202 -1 O SER E 199 N VAL E 8
SHEET 7 H 9 VAL E 212 LYS E 215 -1 O ILE E 214 N ILE E 196
SHEET 8 H 9 THR E 248 ASP E 252 1 O ARG E 249 N GLU E 213
SHEET 9 H 9 LYS E 257 TYR E 259 -1 O TYR E 259 N THR E 250
SHEET 1 I 2 GLU E 75 SER E 76 0
SHEET 2 I 2 LEU E 281 LYS E 282 -1 O LEU E 281 N SER E 76
SHEET 1 J 2 PHE E 78 HIS E 82 0
SHEET 2 J 2 TYR E 92 GLN E 96 -1 O GLN E 93 N LYS E 81
SHEET 1 K 4 LYS E 132 GLU E 136 0
SHEET 2 K 4 LYS E 139 ASP E 143 -1 O LEU E 141 N ILE E 134
SHEET 3 K 4 PHE F 85 PRO F 89 -1 O VAL F 88 N THR E 140
SHEET 4 K 4 ARG F 81 LYS F 82 -1 N LYS F 82 O PHE F 85
SHEET 1 L11 TYR G 42 PRO G 45 0
SHEET 2 L11 LEU G 110 THR G 115 -1 O LYS G 114 N THR G 44
SHEET 3 L11 PRO G 68 LYS G 72 1 N VAL G 71 O THR G 115
SHEET 4 L11 SER G 163 SER G 166 1 O LEU G 164 N ALA G 70
SHEET 5 L11 ILE G 206 GLY G 210 -1 O PHE G 209 N SER G 163
SHEET 6 L11 ILE G 182 LYS G 185 -1 N ILE G 184 O VAL G 208
SHEET 7 L11 ALA G 431 LYS G 439 -1 O ALA G 431 N LYS G 185
SHEET 8 L11 LEU G 442 ILE G 449 -1 O GLY G 446 N ILE G 434
SHEET 9 L11 VAL G 391 PRO G 395 -1 N ILE G 392 O ILE G 449
SHEET 10 L11 LYS G 253 PRO G 257 1 N GLY G 255 O VAL G 391
SHEET 11 L11 GLU G 286 VAL G 290 1 O LYS G 288 N ILE G 254
SHEET 1 M 9 GLU H 71 VAL H 72 0
SHEET 2 M 9 ALA H 102 ASN H 110 -1 O THR H 103 N GLU H 71
SHEET 3 M 9 LYS H 116 GLU H 128 -1 O VAL H 119 N VAL H 107
SHEET 4 M 9 PRO H 150 THR H 156 -1 O LEU H 151 N GLU H 127
SHEET 5 M 9 TYR H 5 GLN H 16 -1 N ILE H 13 O ILE H 154
SHEET 6 M 9 LEU H 192 PRO H 202 -1 O SER H 199 N VAL H 8
SHEET 7 M 9 VAL H 212 LYS H 215 -1 O ILE H 214 N ILE H 196
SHEET 8 M 9 GLU H 247 ASP H 252 1 O ARG H 249 N GLU H 213
SHEET 9 M 9 LYS H 257 TYR H 259 -1 O TYR H 259 N THR H 250
SHEET 1 N 2 VAL H 53 ASN H 54 0
SHEET 2 N 2 MET I 60 ARG I 61 1 O ARG I 61 N VAL H 53
SHEET 1 O 2 GLU H 75 SER H 76 0
SHEET 2 O 2 LEU H 281 LYS H 282 -1 O LEU H 281 N SER H 76
SHEET 1 P 2 PHE H 78 HIS H 82 0
SHEET 2 P 2 TYR H 92 GLN H 96 -1 O GLN H 93 N LYS H 81
SHEET 1 Q 4 LYS H 132 GLU H 136 0
SHEET 2 Q 4 LYS H 139 ASP H 143 -1 O LEU H 141 N ILE H 134
SHEET 3 Q 4 PHE I 85 PRO I 89 -1 O VAL I 88 N THR H 140
SHEET 4 Q 4 ARG I 81 LYS I 82 -1 N LYS I 82 O PHE I 85
SHEET 1 R11 TYR J 42 PRO J 45 0
SHEET 2 R11 LEU J 110 THR J 115 -1 O LYS J 114 N ILE J 43
SHEET 3 R11 PRO J 68 LYS J 72 1 N VAL J 71 O THR J 115
SHEET 4 R11 SER J 163 SER J 166 1 O LEU J 164 N ALA J 70
SHEET 5 R11 ILE J 206 GLY J 210 -1 O PHE J 209 N SER J 163
SHEET 6 R11 ILE J 182 LYS J 185 -1 N ILE J 182 O GLY J 210
SHEET 7 R11 ALA J 431 LYS J 439 -1 O ALA J 431 N LYS J 185
SHEET 8 R11 LEU J 442 ILE J 449 -1 O GLY J 446 N ILE J 434
SHEET 9 R11 VAL J 391 PRO J 395 -1 N SER J 394 O GLN J 447
SHEET 10 R11 LYS J 253 PRO J 257 1 N GLY J 255 O VAL J 391
SHEET 11 R11 GLU J 286 VAL J 290 1 O LYS J 288 N ILE J 254
SHEET 1 S 9 GLU K 71 VAL K 72 0
SHEET 2 S 9 ALA K 102 ASN K 110 -1 O THR K 103 N GLU K 71
SHEET 3 S 9 LYS K 116 GLU K 128 -1 O VAL K 119 N VAL K 107
SHEET 4 S 9 PRO K 150 THR K 156 -1 O LEU K 151 N GLU K 127
SHEET 5 S 9 TYR K 5 GLN K 16 -1 N ILE K 13 O ILE K 154
SHEET 6 S 9 LEU K 192 PRO K 202 -1 O ASN K 197 N GLY K 10
SHEET 7 S 9 VAL K 212 LYS K 215 -1 O ILE K 214 N ILE K 196
SHEET 8 S 9 THR K 248 ASP K 252 1 O ARG K 249 N GLU K 213
SHEET 9 S 9 LYS K 257 TYR K 259 -1 O TYR K 259 N THR K 250
SHEET 1 T 2 VAL K 53 ASN K 54 0
SHEET 2 T 2 MET L 60 ARG L 61 1 O ARG L 61 N VAL K 53
SHEET 1 U 2 GLU K 75 SER K 76 0
SHEET 2 U 2 LEU K 281 LYS K 282 -1 O LEU K 281 N SER K 76
SHEET 1 V 2 PHE K 78 HIS K 82 0
SHEET 2 V 2 TYR K 92 GLN K 96 -1 O GLN K 93 N LYS K 81
SHEET 1 W 4 LYS K 132 GLU K 136 0
SHEET 2 W 4 LYS K 139 ASP K 143 -1 O LEU K 141 N ILE K 134
SHEET 3 W 4 PHE L 85 PRO L 89 -1 O VAL L 88 N THR K 140
SHEET 4 W 4 ARG L 81 LYS L 82 -1 N LYS L 82 O PHE L 85
SHEET 1 X11 TYR M 42 PRO M 45 0
SHEET 2 X11 LEU M 110 THR M 115 -1 O LYS M 114 N ILE M 43
SHEET 3 X11 PRO M 68 LYS M 72 1 N VAL M 71 O THR M 115
SHEET 4 X11 SER M 163 SER M 166 1 O LEU M 164 N ALA M 70
SHEET 5 X11 ILE M 206 GLY M 210 -1 O PHE M 209 N SER M 163
SHEET 6 X11 ILE M 182 LYS M 185 -1 N ILE M 184 O VAL M 208
SHEET 7 X11 ALA M 431 LYS M 439 -1 O ALA M 431 N LYS M 185
SHEET 8 X11 LEU M 442 ILE M 449 -1 O GLY M 446 N ILE M 434
SHEET 9 X11 VAL M 391 PRO M 395 -1 N SER M 394 O GLN M 447
SHEET 10 X11 LYS M 253 PRO M 257 1 N GLY M 255 O VAL M 391
SHEET 11 X11 GLU M 286 VAL M 290 1 O LYS M 288 N ILE M 254
SHEET 1 Y 9 GLU N 71 VAL N 72 0
SHEET 2 Y 9 ALA N 102 ASN N 110 -1 O THR N 103 N GLU N 71
SHEET 3 Y 9 LYS N 116 GLU N 128 -1 O VAL N 119 N VAL N 107
SHEET 4 Y 9 PRO N 150 THR N 156 -1 O LEU N 151 N GLU N 127
SHEET 5 Y 9 TYR N 5 GLN N 16 -1 N ILE N 13 O ILE N 154
SHEET 6 Y 9 LEU N 192 PRO N 202 -1 O SER N 199 N VAL N 8
SHEET 7 Y 9 VAL N 212 LYS N 215 -1 O ILE N 214 N ILE N 196
SHEET 8 Y 9 THR N 248 ASP N 252 1 O ARG N 249 N LYS N 215
SHEET 9 Y 9 LYS N 257 TYR N 259 -1 O TYR N 259 N THR N 250
SHEET 1 Z 2 VAL N 53 ASN N 54 0
SHEET 2 Z 2 MET O 60 ARG O 61 1 O ARG O 61 N VAL N 53
SHEET 1 AA 2 GLU N 75 SER N 76 0
SHEET 2 AA 2 LEU N 281 LYS N 282 -1 O LEU N 281 N SER N 76
SHEET 1 AB 2 PHE N 78 HIS N 82 0
SHEET 2 AB 2 TYR N 92 GLN N 96 -1 O GLN N 93 N LYS N 81
SHEET 1 AC 4 LYS N 132 GLU N 136 0
SHEET 2 AC 4 LYS N 139 ASP N 143 -1 O LEU N 141 N ILE N 134
SHEET 3 AC 4 PHE O 85 PRO O 89 -1 O PHE O 86 N VAL N 142
SHEET 4 AC 4 ARG O 81 LYS O 82 -1 N LYS O 82 O PHE O 85
SHEET 1 AD11 TYR P 42 PRO P 45 0
SHEET 2 AD11 LEU P 110 THR P 115 -1 O LYS P 114 N ILE P 43
SHEET 3 AD11 PRO P 68 LYS P 72 1 N VAL P 71 O THR P 115
SHEET 4 AD11 SER P 163 SER P 166 1 O LEU P 164 N ALA P 70
SHEET 5 AD11 ILE P 206 GLY P 210 -1 O PHE P 209 N SER P 163
SHEET 6 AD11 ILE P 182 LYS P 185 -1 N ILE P 184 O VAL P 208
SHEET 7 AD11 ALA P 431 LYS P 439 -1 O ALA P 431 N LYS P 185
SHEET 8 AD11 LEU P 442 ILE P 449 -1 O GLY P 446 N ILE P 434
SHEET 9 AD11 VAL P 391 PRO P 395 -1 N SER P 394 O GLN P 447
SHEET 10 AD11 LYS P 253 PRO P 257 1 N GLY P 255 O VAL P 391
SHEET 11 AD11 GLU P 286 VAL P 290 1 O LYS P 288 N ILE P 254
SHEET 1 AE 9 GLU Q 71 VAL Q 72 0
SHEET 2 AE 9 ALA Q 102 ASN Q 110 -1 O THR Q 103 N GLU Q 71
SHEET 3 AE 9 LYS Q 116 GLU Q 128 -1 O VAL Q 119 N VAL Q 107
SHEET 4 AE 9 PRO Q 150 THR Q 156 -1 O LEU Q 151 N GLU Q 127
SHEET 5 AE 9 TYR Q 5 GLN Q 16 -1 N ILE Q 13 O ILE Q 154
SHEET 6 AE 9 LEU Q 192 PRO Q 202 -1 O ASN Q 197 N GLY Q 10
SHEET 7 AE 9 VAL Q 212 LYS Q 215 -1 O ILE Q 214 N ILE Q 196
SHEET 8 AE 9 GLU Q 247 ASP Q 252 1 O ARG Q 249 N GLU Q 213
SHEET 9 AE 9 LYS Q 257 TYR Q 259 -1 O TYR Q 259 N THR Q 250
SHEET 1 AF 2 VAL Q 53 ASN Q 54 0
SHEET 2 AF 2 MET R 60 ARG R 61 1 O ARG R 61 N VAL Q 53
SHEET 1 AG 2 GLU Q 75 SER Q 76 0
SHEET 2 AG 2 LEU Q 281 LYS Q 282 -1 O LEU Q 281 N SER Q 76
SHEET 1 AH 2 PHE Q 78 HIS Q 82 0
SHEET 2 AH 2 TYR Q 92 GLN Q 96 -1 O GLN Q 93 N LYS Q 81
SHEET 1 AI 4 LYS Q 132 GLU Q 136 0
SHEET 2 AI 4 LYS Q 139 ASP Q 143 -1 O LEU Q 141 N ILE Q 134
SHEET 3 AI 4 PHE R 85 PRO R 89 -1 O VAL R 88 N THR Q 140
SHEET 4 AI 4 ARG R 81 LYS R 82 -1 N LYS R 82 O PHE R 85
SHEET 1 AJ11 TYR S 42 PRO S 45 0
SHEET 2 AJ11 LEU S 110 THR S 115 -1 O LYS S 114 N ILE S 43
SHEET 3 AJ11 PRO S 68 LYS S 72 1 N VAL S 71 O THR S 115
SHEET 4 AJ11 SER S 163 SER S 166 1 O LEU S 164 N ALA S 70
SHEET 5 AJ11 ILE S 206 GLY S 210 -1 O PHE S 209 N SER S 163
SHEET 6 AJ11 ILE S 182 LYS S 185 -1 N ILE S 182 O GLY S 210
SHEET 7 AJ11 ALA S 431 LYS S 439 -1 O SER S 433 N GLY S 183
SHEET 8 AJ11 LEU S 442 ILE S 449 -1 O GLY S 446 N ILE S 434
SHEET 9 AJ11 VAL S 391 PRO S 395 -1 N SER S 394 O GLN S 447
SHEET 10 AJ11 LYS S 253 PRO S 257 1 N GLY S 255 O VAL S 391
SHEET 11 AJ11 GLU S 286 VAL S 290 1 O LYS S 288 N ILE S 254
SHEET 1 AK 9 GLU T 71 VAL T 72 0
SHEET 2 AK 9 ALA T 102 ASN T 110 -1 O THR T 103 N GLU T 71
SHEET 3 AK 9 LYS T 116 GLU T 128 -1 O VAL T 119 N VAL T 107
SHEET 4 AK 9 PRO T 150 THR T 156 -1 O LEU T 151 N GLU T 127
SHEET 5 AK 9 TYR T 5 GLN T 16 -1 N ILE T 13 O ILE T 154
SHEET 6 AK 9 LEU T 192 PRO T 202 -1 O SER T 199 N VAL T 8
SHEET 7 AK 9 VAL T 212 LYS T 215 -1 O VAL T 212 N VAL T 198
SHEET 8 AK 9 GLU T 247 ASP T 252 1 O ARG T 249 N GLU T 213
SHEET 9 AK 9 LYS T 257 PRO T 260 -1 O TYR T 259 N THR T 250
SHEET 1 AL 2 GLU T 75 SER T 76 0
SHEET 2 AL 2 LEU T 281 LYS T 282 -1 O LEU T 281 N SER T 76
SHEET 1 AM 2 PHE T 78 HIS T 82 0
SHEET 2 AM 2 TYR T 92 GLN T 96 -1 O GLN T 93 N LYS T 81
SHEET 1 AN 4 LYS T 132 GLU T 136 0
SHEET 2 AN 4 LYS T 139 ASP T 143 -1 O LEU T 141 N ILE T 134
SHEET 3 AN 4 PHE U 85 PRO U 89 -1 O VAL U 88 N THR T 140
SHEET 4 AN 4 ARG U 81 LYS U 82 -1 N LYS U 82 O PHE U 85
SHEET 1 AO11 TYR V 42 PRO V 45 0
SHEET 2 AO11 LEU V 110 THR V 115 -1 O LYS V 114 N ILE V 43
SHEET 3 AO11 PRO V 68 LYS V 72 1 N VAL V 71 O THR V 115
SHEET 4 AO11 SER V 163 SER V 166 1 O LEU V 164 N ALA V 70
SHEET 5 AO11 ILE V 206 GLY V 210 -1 O PHE V 209 N SER V 163
SHEET 6 AO11 ILE V 182 LYS V 185 -1 N ILE V 182 O GLY V 210
SHEET 7 AO11 ALA V 431 LYS V 439 -1 O SER V 433 N GLY V 183
SHEET 8 AO11 LEU V 442 ILE V 449 -1 O GLY V 446 N ILE V 434
SHEET 9 AO11 VAL V 391 PRO V 395 -1 N SER V 394 O GLN V 447
SHEET 10 AO11 LYS V 253 PRO V 257 1 N GLY V 255 O VAL V 391
SHEET 11 AO11 GLU V 286 VAL V 290 1 O LYS V 288 N ILE V 254
SHEET 1 AP 9 GLU W 71 VAL W 72 0
SHEET 2 AP 9 ALA W 102 ASN W 110 -1 O THR W 103 N GLU W 71
SHEET 3 AP 9 LYS W 116 GLU W 128 -1 O VAL W 119 N VAL W 107
SHEET 4 AP 9 PRO W 150 THR W 156 -1 O LEU W 151 N GLU W 127
SHEET 5 AP 9 TYR W 5 GLN W 16 -1 N ILE W 13 O ILE W 154
SHEET 6 AP 9 LEU W 192 PRO W 202 -1 O SER W 199 N VAL W 8
SHEET 7 AP 9 VAL W 212 LYS W 215 -1 O ILE W 214 N ILE W 196
SHEET 8 AP 9 THR W 248 ASP W 252 1 O ARG W 249 N GLU W 213
SHEET 9 AP 9 LYS W 257 TYR W 259 -1 O TYR W 259 N THR W 250
SHEET 1 AQ 2 GLU W 75 SER W 76 0
SHEET 2 AQ 2 LEU W 281 LYS W 282 -1 O LEU W 281 N SER W 76
SHEET 1 AR 3 TYR W 92 GLN W 96 0
SHEET 2 AR 3 PHE W 78 HIS W 82 -1 N LYS W 81 O GLN W 93
SHEET 3 AR 3 PHE W 273 PRO W 274 -1 O PHE W 273 N ARG W 80
SHEET 1 AS 4 LYS W 132 GLU W 136 0
SHEET 2 AS 4 LYS W 139 ASP W 143 -1 O LEU W 141 N ILE W 134
SHEET 3 AS 4 PHE X 85 PRO X 89 -1 O VAL X 88 N THR W 140
SHEET 4 AS 4 ARG X 81 LYS X 82 -1 N LYS X 82 O PHE X 85
LINK OG SER A 171 CD GLN A 901 1555 1555 1.95
LINK OG SER D 171 CD GLN D 902 1555 1555 1.56
LINK OG SER G 171 CD GLN G 903 1555 1555 1.85
LINK OG SER J 171 CD GLN J 904 1555 1555 1.50
LINK OG SER M 171 CD GLN M 905 1555 1555 1.90
LINK OG SER P 171 CD GLN P 906 1555 1555 1.55
LINK OG SER S 171 CD GLN S 907 1555 1555 1.75
LINK OG SER V 171 CD GLN V 908 1555 1555 1.91
LINK NE2 HIS B 14 MG MG B 479 1555 1555 2.04
LINK SG CYS B 25 ZN ZN B 901 1555 1555 2.27
LINK SG CYS B 27 ZN ZN B 901 1555 1555 2.12
LINK SG CYS B 40 ZN ZN B 901 1555 1555 2.65
LINK SG CYS B 43 ZN ZN B 901 1555 1555 2.60
LINK OE2 GLU B 127 MG MG B 479 1555 1555 2.16
LINK OE1 GLU B 153 MG MG B 479 1555 1555 2.77
LINK SG CYS E 25 ZN ZN E 902 1555 1555 2.34
LINK SG CYS E 27 ZN ZN E 902 1555 1555 2.33
LINK SG CYS E 40 ZN ZN E 902 1555 1555 2.33
LINK SG CYS E 43 ZN ZN E 902 1555 1555 2.08
LINK NE2 HIS H 14 MG MG H 479 1555 1555 2.02
LINK SG CYS H 25 ZN ZN H 903 1555 1555 2.35
LINK SG CYS H 27 ZN ZN H 903 1555 1555 2.25
LINK SG CYS H 40 ZN ZN H 903 1555 1555 2.41
LINK SG CYS H 43 ZN ZN H 903 1555 1555 2.07
LINK OE2 GLU H 127 MG MG H 479 1555 1555 2.40
LINK OE1 GLU H 153 MG MG H 479 1555 1555 2.16
LINK NE2 HIS K 14 MG MG K 479 1555 1555 1.73
LINK SG CYS K 25 ZN ZN K 904 1555 1555 2.23
LINK SG CYS K 27 ZN ZN K 904 1555 1555 2.07
LINK SG CYS K 40 ZN ZN K 904 1555 1555 2.37
LINK SG CYS K 43 ZN ZN K 904 1555 1555 2.39
LINK OE2 GLU K 127 MG MG K 479 1555 1555 2.43
LINK OE1 GLU K 153 MG MG K 479 1555 1555 2.60
LINK NE2 HIS N 14 MG MG N 479 1555 1555 1.94
LINK SG CYS N 25 ZN ZN N 905 1555 1555 2.17
LINK SG CYS N 27 ZN ZN N 905 1555 1555 2.20
LINK SG CYS N 40 ZN ZN N 905 1555 1555 2.46
LINK SG CYS N 43 ZN ZN N 905 1555 1555 2.23
LINK OE2 GLU N 127 MG MG N 479 1555 1555 2.23
LINK OE1 GLU N 153 MG MG N 479 1555 1555 2.84
LINK NE2 HIS Q 14 MG MG Q 479 1555 1555 1.79
LINK SG CYS Q 25 ZN ZN Q 906 1555 1555 2.01
LINK SG CYS Q 27 ZN ZN Q 906 1555 1555 2.14
LINK SG CYS Q 40 ZN ZN Q 906 1555 1555 2.46
LINK SG CYS Q 43 ZN ZN Q 906 1555 1555 2.49
LINK OE2 GLU Q 127 MG MG Q 479 1555 1555 2.20
LINK OE1 GLU Q 153 MG MG Q 479 1555 1555 2.28
LINK NE2 HIS T 14 MG MG T 479 1555 1555 2.06
LINK SG CYS T 25 ZN ZN T 907 1555 1555 2.39
LINK SG CYS T 27 ZN ZN T 907 1555 1555 2.16
LINK SG CYS T 40 ZN ZN T 907 1555 1555 2.34
LINK SG CYS T 43 ZN ZN T 907 1555 1555 2.12
LINK OE2 GLU T 127 MG MG T 479 1555 1555 2.39
LINK OE1 GLU T 153 MG MG T 479 1555 1555 1.91
LINK NE2 HIS W 14 MG MG W 479 1555 1555 1.84
LINK SG CYS W 25 ZN ZN W 908 1555 1555 2.34
LINK SG CYS W 27 ZN ZN W 908 1555 1555 2.01
LINK SG CYS W 40 ZN ZN W 908 1555 1555 2.15
LINK SG CYS W 43 ZN ZN W 908 1555 1555 2.34
LINK OE2 GLU W 127 MG MG W 479 1555 1555 1.98
LINK OE1 GLU W 153 MG MG W 479 1555 1555 2.23
CISPEP 1 GLY A 146 SER A 147 0 8.89
CISPEP 2 GLY D 146 SER D 147 0 6.33
CISPEP 3 GLY G 146 SER G 147 0 9.06
CISPEP 4 GLY J 146 SER J 147 0 8.44
CISPEP 5 GLY M 146 SER M 147 0 6.86
CISPEP 6 GLY P 146 SER P 147 0 8.65
CISPEP 7 GLY S 146 SER S 147 0 7.60
CISPEP 8 GLY V 146 SER V 147 0 10.49
SITE 1 AC1 14 ALA A 121 MET A 122 GLY A 123 SER A 124
SITE 2 AC1 14 ASP A 167 THR A 168 GLY A 169 GLY A 170
SITE 3 AC1 14 SER A 171 PHE A 199 TYR A 302 TYR A 303
SITE 4 AC1 14 ARG A 351 ASP A 418
SITE 1 AC2 14 ALA D 121 MET D 122 GLY D 123 SER D 124
SITE 2 AC2 14 ASP D 167 THR D 168 GLY D 169 GLY D 170
SITE 3 AC2 14 SER D 171 PHE D 199 TYR D 302 TYR D 303
SITE 4 AC2 14 ARG D 351 ASP D 418
SITE 1 AC3 14 ALA G 121 MET G 122 GLY G 123 SER G 124
SITE 2 AC3 14 SER G 147 SER G 166 ASP G 167 THR G 168
SITE 3 AC3 14 GLY G 169 SER G 171 PHE G 199 TYR G 302
SITE 4 AC3 14 ARG G 351 ASP G 418
SITE 1 AC4 13 ALA J 121 MET J 122 GLY J 123 ASP J 167
SITE 2 AC4 13 THR J 168 GLY J 169 GLY J 170 SER J 171
SITE 3 AC4 13 PHE J 199 TYR J 302 TYR J 303 ARG J 351
SITE 4 AC4 13 ASP J 418
SITE 1 AC5 12 MET M 122 GLY M 123 SER M 124 ASP M 167
SITE 2 AC5 12 THR M 168 GLY M 169 GLY M 170 SER M 171
SITE 3 AC5 12 PHE M 199 TYR M 302 ARG M 351 ASP M 418
SITE 1 AC6 13 MET P 122 GLY P 123 SER P 124 ASP P 167
SITE 2 AC6 13 THR P 168 GLY P 169 GLY P 170 SER P 171
SITE 3 AC6 13 PHE P 199 TYR P 302 TYR P 303 ARG P 351
SITE 4 AC6 13 ASP P 418
SITE 1 AC7 13 ALA S 121 MET S 122 GLY S 123 SER S 124
SITE 2 AC7 13 SER S 147 ASP S 167 THR S 168 GLY S 169
SITE 3 AC7 13 SER S 171 TYR S 302 TYR S 303 ARG S 351
SITE 4 AC7 13 ASP S 418
SITE 1 AC8 13 MET V 122 GLY V 123 SER V 124 ASP V 167
SITE 2 AC8 13 THR V 168 GLY V 169 GLY V 170 SER V 171
SITE 3 AC8 13 PHE V 199 TYR V 302 TYR V 303 ARG V 351
SITE 4 AC8 13 ASP V 418
SITE 1 AC9 3 HIS B 14 GLU B 127 GLU B 153
SITE 1 BC1 3 HIS H 14 GLU H 127 GLU H 153
SITE 1 BC2 3 HIS K 14 GLU K 127 GLU K 153
SITE 1 BC3 3 HIS N 14 GLU N 127 GLU N 153
SITE 1 BC4 3 HIS Q 14 GLU Q 127 GLU Q 153
SITE 1 BC5 3 HIS T 14 GLU T 127 GLU T 153
SITE 1 BC6 3 HIS W 14 GLU W 127 GLU W 153
SITE 1 BC7 4 CYS B 25 CYS B 27 CYS B 40 CYS B 43
SITE 1 BC8 4 CYS E 25 CYS E 27 CYS E 40 CYS E 43
SITE 1 BC9 4 CYS H 25 CYS H 27 CYS H 40 CYS H 43
SITE 1 CC1 4 CYS K 25 CYS K 27 CYS K 40 CYS K 43
SITE 1 CC2 4 CYS N 25 CYS N 27 CYS N 40 CYS N 43
SITE 1 CC3 4 CYS Q 25 CYS Q 27 CYS Q 40 CYS Q 43
SITE 1 CC4 4 CYS T 25 CYS T 27 CYS T 40 CYS T 43
SITE 1 CC5 4 CYS W 25 CYS W 27 CYS W 40 CYS W 43
CRYST1 128.248 129.856 155.069 90.01 89.96 90.11 P 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007797 0.000015 -0.000006 0.00000
SCALE2 0.000000 0.007701 0.000001 0.00000
SCALE3 0.000000 0.000000 0.006449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
