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HEADER HYDROLASE 23-DEC-03 1RYY
TITLE ACETOBACTER TURBIDANS ALPHA-AMINO ACID ESTER HYDROLASE
TITLE 2 Y206A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMINO ACID ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: ALPHA-AMINO ACID ESTER HYDROLASE;
COMPND 5 EC: 3.1.1.43;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACETOBACTER PASTEURIANUS;
SOURCE 3 GENE: AEHA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBADATY206AMYCHIS
KEYWDS ALPHA/BETA HYDROLASE FOLD, JELLYROLL FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.M.BARENDS
REVDAT 1 22-FEB-05 1RYY 0
JRNL AUTH T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,
JRNL AUTH 2 E.DE VRIES,D.B.JANSSEN,B.W.DIJKSTRA
JRNL TITL ACETOBACTER TURBIDANS ALPHA-AMINO ACID ESTER
JRNL TITL 2 HYDROLASE: HOW A SINGLE MUTATION IMPROVED AN
JRNL TITL 3 ANTIBIOTIC-PRODUCING ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 125204
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6623
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9034
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 463
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 39009
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : 4.51000
REMARK 3 B33 (A**2) : -4.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.309
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.376
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.286
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.779
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 39936 ; 0.003 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 54528 ; 1.271 ; 1.928
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4880 ; 0.518 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5656 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 31776 ; 0.001 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 16941 ; 0.154 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 506 ; 0.096 ; 0.500
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): 65 ; 0.144 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.189 ; 0.500
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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 50 A 60 1
REMARK 3 1 B 50 B 60 1
REMARK 3 1 C 50 C 60 1
REMARK 3 1 D 50 D 60 1
REMARK 3 1 E 50 E 60 1
REMARK 3 1 F 50 F 60 1
REMARK 3 1 G 50 G 60 1
REMARK 3 1 H 50 H 60 1
REMARK 3 2 A 70 A 90 1
REMARK 3 2 B 70 B 90 1
REMARK 3 2 C 70 C 90 1
REMARK 3 2 D 70 D 90 1
REMARK 3 2 E 70 E 90 1
REMARK 3 2 F 70 F 90 1
REMARK 3 2 G 70 G 90 1
REMARK 3 2 H 70 H 90 1
REMARK 3 3 A 110 A 455 1
REMARK 3 3 B 110 B 455 1
REMARK 3 3 C 110 C 455 1
REMARK 3 3 D 110 D 455 1
REMARK 3 3 E 110 E 455 1
REMARK 3 3 F 110 F 455 1
REMARK 3 3 G 110 G 455 1
REMARK 3 3 H 110 H 455 1
REMARK 3 4 A 470 A 666 1
REMARK 3 4 B 470 B 666 1
REMARK 3 4 C 470 C 666 1
REMARK 3 4 D 470 D 666 1
REMARK 3 4 E 470 E 666 1
REMARK 3 4 F 470 F 666 1
REMARK 3 4 G 470 G 666 1
REMARK 3 4 H 470 H 666 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4559 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 4559 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 4559 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 4559 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 4559 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 F (A): 4559 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 G (A): 4559 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 H (A): 4559 ; 0.07 ; 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 50 A 666
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3098 -15.3156 57.9637
REMARK 3 T TENSOR
REMARK 3 T11: 0.1353 T22: 0.0377
REMARK 3 T33: 0.1369 T12: -0.0066
REMARK 3 T13: -0.0253 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.4582 L22: 0.7418
REMARK 3 L33: 0.5982 L12: 0.0720
REMARK 3 L13: -0.0421 L23: -0.2178
REMARK 3 S TENSOR
REMARK 3 S11: 0.0287 S12: 0.0747 S13: -0.0646
REMARK 3 S21: -0.0354 S22: 0.0270 S23: 0.0835
REMARK 3 S31: 0.0579 S32: -0.0388 S33: -0.0557
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 50 B 666
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9050 11.7890 98.2410
REMARK 3 T TENSOR
REMARK 3 T11: 0.1513 T22: 0.0364
REMARK 3 T33: 0.1640 T12: -0.0279
REMARK 3 T13: 0.0584 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.6572 L22: 0.8510
REMARK 3 L33: 0.7251 L12: -0.2130
REMARK 3 L13: 0.2971 L23: -0.1474
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.1459 S13: 0.0977
REMARK 3 S21: 0.0814 S22: 0.0121 S23: 0.1054
REMARK 3 S31: -0.0449 S32: -0.1154 S33: -0.0193
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 50 C 666
REMARK 3 ORIGIN FOR THE GROUP (A): 28.0390 -19.2950 90.4540
REMARK 3 T TENSOR
REMARK 3 T11: 0.1765 T22: 0.0273
REMARK 3 T33: 0.1858 T12: 0.0140
REMARK 3 T13: -0.0635 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.8183 L22: 0.6660
REMARK 3 L33: 0.9509 L12: -0.0493
REMARK 3 L13: -0.1425 L23: 0.1487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0688 S12: -0.0804 S13: -0.1327
REMARK 3 S21: 0.0513 S22: 0.0152 S23: -0.1434
REMARK 3 S31: 0.1163 S32: 0.2024 S33: -0.0840
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 50 D 666
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0940 22.5450 65.7030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1434 T22: 0.0533
REMARK 3 T33: 0.2121 T12: -0.0735
REMARK 3 T13: 0.0639 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.5839 L22: 0.6118
REMARK 3 L33: 0.9462 L12: 0.0811
REMARK 3 L13: 0.1393 L23: 0.2071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0143 S12: 0.0667 S13: 0.2007
REMARK 3 S21: -0.0155 S22: 0.0494 S23: -0.0638
REMARK 3 S31: -0.1427 S32: 0.1803 S33: -0.0637
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 50 E 666
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3420 57.9060 24.0540
REMARK 3 T TENSOR
REMARK 3 T11: 0.2575 T22: 0.6428
REMARK 3 T33: 0.2179 T12: 0.0622
REMARK 3 T13: 0.0795 T23: 0.1295
REMARK 3 L TENSOR
REMARK 3 L11: 0.7242 L22: 1.0549
REMARK 3 L33: 0.6592 L12: -0.0179
REMARK 3 L13: -0.1193 L23: -0.1367
REMARK 3 S TENSOR
REMARK 3 S11: -0.0930 S12: -0.2517 S13: -0.0195
REMARK 3 S21: 0.2264 S22: 0.1556 S23: 0.1917
REMARK 3 S31: -0.0678 S32: -0.1894 S33: -0.0626
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 50 F 666
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0770 63.1710 -24.3060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1987 T22: 0.5373
REMARK 3 T33: 0.1639 T12: -0.1125
REMARK 3 T13: -0.0251 T23: 0.0956
REMARK 3 L TENSOR
REMARK 3 L11: 0.8088 L22: 0.9379
REMARK 3 L33: 0.7466 L12: 0.0586
REMARK 3 L13: -0.1153 L23: -0.1684
REMARK 3 S TENSOR
REMARK 3 S11: -0.0133 S12: -0.0071 S13: -0.1376
REMARK 3 S21: -0.1181 S22: 0.0850 S23: 0.1587
REMARK 3 S31: 0.1698 S32: -0.3476 S33: -0.0717
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 50 G 666
REMARK 3 ORIGIN FOR THE GROUP (A): 73.5990 84.8610 5.2500
REMARK 3 T TENSOR
REMARK 3 T11: 0.2095 T22: 0.3352
REMARK 3 T33: 0.1790 T12: 0.0246
REMARK 3 T13: -0.0060 T23: -0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 0.5223 L22: 0.5920
REMARK 3 L33: 1.3929 L12: -0.0829
REMARK 3 L13: 0.0137 L23: -0.3402
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: -0.2106 S13: 0.1305
REMARK 3 S21: 0.1735 S22: 0.0501 S23: -0.0685
REMARK 3 S31: -0.1446 S32: -0.0510 S33: -0.0320
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 50 H 666
REMARK 3 ORIGIN FOR THE GROUP (A): 74.2900 36.6510 -2.9290
REMARK 3 T TENSOR
REMARK 3 T11: 0.2724 T22: 0.3024
REMARK 3 T33: 0.2837 T12: -0.0373
REMARK 3 T13: 0.0731 T23: 0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 0.7531 L22: 0.7757
REMARK 3 L33: 1.0698 L12: 0.0829
REMARK 3 L13: -0.3746 L23: -0.2681
REMARK 3 S TENSOR
REMARK 3 S11: -0.1622 S12: -0.1226 S13: -0.2328
REMARK 3 S21: -0.1128 S22: 0.0369 S23: -0.0971
REMARK 3 S31: 0.1743 S32: 0.0472 S33: 0.1253
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: TLS REFINEMENT EMPLOYED. THE DENSITY
REMARK 3 FOR RESIDUES 66-70 IN EACH OF THE MONOMERS WAS NOT CLEAR. THUS
REMARK 3 THESE RESIDUES HAVE NOT BEEN MODELLED.
REMARK 4
REMARK 4 1RYY COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-2003.
REMARK 100 THE RCSB ID CODE IS RCSB021164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393
REMARK 200 MONOCHROMATOR : SI CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134932
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06600
REMARK 200 FOR THE DATA SET : 17.2000
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18400
REMARK 200 FOR SHELL : 6.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PEG 4000, AMMONIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,1/2+Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 88.75650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 8 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 ALA A 44
REMARK 465 ASP A 45
REMARK 465 ALA A 46
REMARK 465 ALA A 47
REMARK 465 GLN A 48
REMARK 465 ALA A 49
REMARK 465 HIS A 66
REMARK 465 MET A 67
REMARK 465 PRO A 68
REMARK 465 THR A 69
REMARK 465 ASP A 70
REMARK 465 GLN A 667
REMARK 465 LYS A 668
REMARK 465 LEU A 669
REMARK 465 GLY A 670
REMARK 465 PRO A 671
REMARK 465 GLU A 672
REMARK 465 GLN A 673
REMARK 465 LYS A 674
REMARK 465 LEU A 675
REMARK 465 ILE A 676
REMARK 465 SER A 677
REMARK 465 GLU A 678
REMARK 465 GLU A 679
REMARK 465 ASP A 680
REMARK 465 LEU A 681
REMARK 465 ASN A 682
REMARK 465 SER A 683
REMARK 465 ALA A 684
REMARK 465 VAL A 685
REMARK 465 ASP A 686
REMARK 465 HIS A 687
REMARK 465 HIS A 688
REMARK 465 HIS A 689
REMARK 465 HIS A 690
REMARK 465 HIS A 691
REMARK 465 HIS A 692
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 ALA B 44
REMARK 465 ASP B 45
REMARK 465 ALA B 46
REMARK 465 ALA B 47
REMARK 465 GLN B 48
REMARK 465 ALA B 49
REMARK 465 HIS B 66
REMARK 465 MET B 67
REMARK 465 PRO B 68
REMARK 465 THR B 69
REMARK 465 ASP B 70
REMARK 465 GLN B 667
REMARK 465 LYS B 668
REMARK 465 LEU B 669
REMARK 465 GLY B 670
REMARK 465 PRO B 671
REMARK 465 GLU B 672
REMARK 465 GLN B 673
REMARK 465 LYS B 674
REMARK 465 LEU B 675
REMARK 465 ILE B 676
REMARK 465 SER B 677
REMARK 465 GLU B 678
REMARK 465 GLU B 679
REMARK 465 ASP B 680
REMARK 465 LEU B 681
REMARK 465 ASN B 682
REMARK 465 SER B 683
REMARK 465 ALA B 684
REMARK 465 VAL B 685
REMARK 465 ASP B 686
REMARK 465 HIS B 687
REMARK 465 HIS B 688
REMARK 465 HIS B 689
REMARK 465 HIS B 690
REMARK 465 HIS B 691
REMARK 465 HIS B 692
REMARK 465 ALA C 41
REMARK 465 PRO C 42
REMARK 465 ALA C 43
REMARK 465 ALA C 44
REMARK 465 ASP C 45
REMARK 465 ALA C 46
REMARK 465 ALA C 47
REMARK 465 GLN C 48
REMARK 465 ALA C 49
REMARK 465 HIS C 66
REMARK 465 MET C 67
REMARK 465 PRO C 68
REMARK 465 THR C 69
REMARK 465 ASP C 70
REMARK 465 GLN C 667
REMARK 465 LYS C 668
REMARK 465 LEU C 669
REMARK 465 GLY C 670
REMARK 465 PRO C 671
REMARK 465 GLU C 672
REMARK 465 GLN C 673
REMARK 465 LYS C 674
REMARK 465 LEU C 675
REMARK 465 ILE C 676
REMARK 465 SER C 677
REMARK 465 GLU C 678
REMARK 465 GLU C 679
REMARK 465 ASP C 680
REMARK 465 LEU C 681
REMARK 465 ASN C 682
REMARK 465 SER C 683
REMARK 465 ALA C 684
REMARK 465 VAL C 685
REMARK 465 ASP C 686
REMARK 465 HIS C 687
REMARK 465 HIS C 688
REMARK 465 HIS C 689
REMARK 465 HIS C 690
REMARK 465 HIS C 691
REMARK 465 HIS C 692
REMARK 465 ALA D 41
REMARK 465 PRO D 42
REMARK 465 ALA D 43
REMARK 465 ALA D 44
REMARK 465 ASP D 45
REMARK 465 ALA D 46
REMARK 465 ALA D 47
REMARK 465 GLN D 48
REMARK 465 ALA D 49
REMARK 465 HIS D 66
REMARK 465 MET D 67
REMARK 465 PRO D 68
REMARK 465 THR D 69
REMARK 465 ASP D 70
REMARK 465 GLN D 667
REMARK 465 LYS D 668
REMARK 465 LEU D 669
REMARK 465 GLY D 670
REMARK 465 PRO D 671
REMARK 465 GLU D 672
REMARK 465 GLN D 673
REMARK 465 LYS D 674
REMARK 465 LEU D 675
REMARK 465 ILE D 676
REMARK 465 SER D 677
REMARK 465 GLU D 678
REMARK 465 GLU D 679
REMARK 465 ASP D 680
REMARK 465 LEU D 681
REMARK 465 ASN D 682
REMARK 465 SER D 683
REMARK 465 ALA D 684
REMARK 465 VAL D 685
REMARK 465 ASP D 686
REMARK 465 HIS D 687
REMARK 465 HIS D 688
REMARK 465 HIS D 689
REMARK 465 HIS D 690
REMARK 465 HIS D 691
REMARK 465 HIS D 692
REMARK 465 ALA E 41
REMARK 465 PRO E 42
REMARK 465 ALA E 43
REMARK 465 ALA E 44
REMARK 465 ASP E 45
REMARK 465 ALA E 46
REMARK 465 ALA E 47
REMARK 465 GLN E 48
REMARK 465 ALA E 49
REMARK 465 HIS E 66
REMARK 465 MET E 67
REMARK 465 PRO E 68
REMARK 465 THR E 69
REMARK 465 ASP E 70
REMARK 465 GLN E 667
REMARK 465 LYS E 668
REMARK 465 LEU E 669
REMARK 465 GLY E 670
REMARK 465 PRO E 671
REMARK 465 GLU E 672
REMARK 465 GLN E 673
REMARK 465 LYS E 674
REMARK 465 LEU E 675
REMARK 465 ILE E 676
REMARK 465 SER E 677
REMARK 465 GLU E 678
REMARK 465 GLU E 679
REMARK 465 ASP E 680
REMARK 465 LEU E 681
REMARK 465 ASN E 682
REMARK 465 SER E 683
REMARK 465 ALA E 684
REMARK 465 VAL E 685
REMARK 465 ASP E 686
REMARK 465 HIS E 687
REMARK 465 HIS E 688
REMARK 465 HIS E 689
REMARK 465 HIS E 690
REMARK 465 HIS E 691
REMARK 465 HIS E 692
REMARK 465 ALA F 41
REMARK 465 PRO F 42
REMARK 465 ALA F 43
REMARK 465 ALA F 44
REMARK 465 ASP F 45
REMARK 465 ALA F 46
REMARK 465 ALA F 47
REMARK 465 GLN F 48
REMARK 465 ALA F 49
REMARK 465 HIS F 66
REMARK 465 MET F 67
REMARK 465 PRO F 68
REMARK 465 THR F 69
REMARK 465 ASP F 70
REMARK 465 GLN F 667
REMARK 465 LYS F 668
REMARK 465 LEU F 669
REMARK 465 GLY F 670
REMARK 465 PRO F 671
REMARK 465 GLU F 672
REMARK 465 GLN F 673
REMARK 465 LYS F 674
REMARK 465 LEU F 675
REMARK 465 ILE F 676
REMARK 465 SER F 677
REMARK 465 GLU F 678
REMARK 465 GLU F 679
REMARK 465 ASP F 680
REMARK 465 LEU F 681
REMARK 465 ASN F 682
REMARK 465 SER F 683
REMARK 465 ALA F 684
REMARK 465 VAL F 685
REMARK 465 ASP F 686
REMARK 465 HIS F 687
REMARK 465 HIS F 688
REMARK 465 HIS F 689
REMARK 465 HIS F 690
REMARK 465 HIS F 691
REMARK 465 HIS F 692
REMARK 465 ALA G 41
REMARK 465 PRO G 42
REMARK 465 ALA G 43
REMARK 465 ALA G 44
REMARK 465 ASP G 45
REMARK 465 ALA G 46
REMARK 465 ALA G 47
REMARK 465 GLN G 48
REMARK 465 ALA G 49
REMARK 465 HIS G 66
REMARK 465 MET G 67
REMARK 465 PRO G 68
REMARK 465 THR G 69
REMARK 465 ASP G 70
REMARK 465 GLN G 667
REMARK 465 LYS G 668
REMARK 465 LEU G 669
REMARK 465 GLY G 670
REMARK 465 PRO G 671
REMARK 465 GLU G 672
REMARK 465 GLN G 673
REMARK 465 LYS G 674
REMARK 465 LEU G 675
REMARK 465 ILE G 676
REMARK 465 SER G 677
REMARK 465 GLU G 678
REMARK 465 GLU G 679
REMARK 465 ASP G 680
REMARK 465 LEU G 681
REMARK 465 ASN G 682
REMARK 465 SER G 683
REMARK 465 ALA G 684
REMARK 465 VAL G 685
REMARK 465 ASP G 686
REMARK 465 HIS G 687
REMARK 465 HIS G 688
REMARK 465 HIS G 689
REMARK 465 HIS G 690
REMARK 465 HIS G 691
REMARK 465 HIS G 692
REMARK 465 ALA H 41
REMARK 465 PRO H 42
REMARK 465 ALA H 43
REMARK 465 ALA H 44
REMARK 465 ASP H 45
REMARK 465 ALA H 46
REMARK 465 ALA H 47
REMARK 465 GLN H 48
REMARK 465 ALA H 49
REMARK 465 HIS H 66
REMARK 465 MET H 67
REMARK 465 PRO H 68
REMARK 465 THR H 69
REMARK 465 ASP H 70
REMARK 465 GLN H 667
REMARK 465 LYS H 668
REMARK 465 LEU H 669
REMARK 465 GLY H 670
REMARK 465 PRO H 671
REMARK 465 GLU H 672
REMARK 465 GLN H 673
REMARK 465 LYS H 674
REMARK 465 LEU H 675
REMARK 465 ILE H 676
REMARK 465 SER H 677
REMARK 465 GLU H 678
REMARK 465 GLU H 679
REMARK 465 ASP H 680
REMARK 465 LEU H 681
REMARK 465 ASN H 682
REMARK 465 SER H 683
REMARK 465 ALA H 684
REMARK 465 VAL H 685
REMARK 465 ASP H 686
REMARK 465 HIS H 687
REMARK 465 HIS H 688
REMARK 465 HIS H 689
REMARK 465 HIS H 690
REMARK 465 HIS H 691
REMARK 465 HIS H 692
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 84 SD MET A 84 CE -0.024
REMARK 500 MET A 201 SD MET A 201 CE 0.026
REMARK 500 THR B 110 CA THR B 110 CB 0.021
REMARK 500 PRO B 172 CB PRO B 172 CG 0.022
REMARK 500 PRO B 462 CB PRO B 462 CG 0.023
REMARK 500 PRO B 495 CB PRO B 495 CG 0.026
REMARK 500 MET B 561 SD MET B 561 CE 0.021
REMARK 500 THR C 110 CA THR C 110 CB 0.021
REMARK 500 MET C 127 SD MET C 127 CE -0.025
REMARK 500 PRO C 495 CB PRO C 495 CG 0.023
REMARK 500 MET C 613 CG MET C 613 SD -0.022
REMARK 500 PRO C 622 CB PRO C 622 CG 0.022
REMARK 500 PRO D 132 CB PRO D 132 CG -0.031
REMARK 500 MET D 258 SD MET D 258 CE -0.037
REMARK 500 PRO D 484 CB PRO D 484 CG 0.024
REMARK 500 MET E 258 SD MET E 258 CE -0.026
REMARK 500 PRO E 435 CB PRO E 435 CG 0.025
REMARK 500 MET F 258 SD MET F 258 CE -0.028
REMARK 500 PRO F 495 CB PRO F 495 CG 0.029
REMARK 500 ILE G 548 CA ILE G 548 CB 0.022
REMARK 500 MET H 258 SD MET H 258 CE -0.021
REMARK 500 PRO H 435 CB PRO H 435 CG 0.023
REMARK 500 PRO H 495 CB PRO H 495 CG 0.025
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 106 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 THR A 110 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 VAL A 121 N - CA - C ANGL. DEV. =-14.0 DEGREES
REMARK 500 ILE A 144 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ASP A 239 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 HIS A 242 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 GLN A 248 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLY A 344 N - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 LEU A 451 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 LEU A 547 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 GLY A 575 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASN A 603 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 PHE A 606 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ILE A 612 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ASN A 627 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 ILE A 660 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 LEU B 106 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 THR B 110 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 VAL B 121 N - CA - C ANGL. DEV. =-14.4 DEGREES
REMARK 500 ASN B 191 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 ASP B 239 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 HIS B 242 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 GLN B 248 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 GLY B 344 N - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG B 369 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 LEU B 451 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 LEU B 547 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 THR B 555 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ILE B 612 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASN B 627 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 LYS B 630 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ILE B 660 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG C 109 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 THR C 110 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 VAL C 121 N - CA - C ANGL. DEV. =-13.8 DEGREES
REMARK 500 ILE C 144 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 MET C 231 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ASP C 239 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 HIS C 242 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 MET C 258 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLY C 344 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU C 451 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 LEU C 547 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASN C 603 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 ILE C 612 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ASN C 627 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ILE C 660 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 THR D 110 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 VAL D 121 N - CA - C ANGL. DEV. =-13.8 DEGREES
REMARK 500 MET D 231 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASP D 239 N - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 HIS D 242 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 GLY D 344 N - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 LEU D 451 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 LEU D 547 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 THR D 555 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 PRO D 559 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASN D 603 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 PHE D 606 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ILE D 612 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ASN D 627 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ILE D 660 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 THR E 110 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 VAL E 121 N - CA - C ANGL. DEV. =-12.4 DEGREES
REMARK 500 ASP E 239 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 HIS E 242 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 GLN E 248 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 GLY E 344 N - CA - C ANGL. DEV. = 10.9 DEGREES
REMARK 500 LEU E 451 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 LEU E 547 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ASN E 603 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ASN E 627 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ILE E 660 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 THR F 110 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 VAL F 121 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 ASP F 239 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 HIS F 242 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 GLY F 344 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 LEU F 451 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 LEU F 547 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASN F 603 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 ILE F 612 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASN F 627 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ILE F 660 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 THR G 110 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 VAL G 121 N - CA - C ANGL. DEV. =-12.9 DEGREES
REMARK 500 ASP G 239 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 HIS G 242 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 GLY G 344 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU G 451 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 LEU G 547 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASN G 603 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 ILE G 612 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 ASN G 627 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ILE G 660 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 THR H 110 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 VAL H 121 N - CA - C ANGL. DEV. =-12.4 DEGREES
REMARK 500 ASP H 239 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 HIS H 242 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 GLY H 344 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU H 451 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 LEU H 547 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 ASN H 603 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 ASN H 627 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 154 -108.45 51.20
REMARK 500 SER A 205 -118.82 59.70
REMARK 500 TYR B 154 -112.34 50.35
REMARK 500 SER B 205 -117.36 58.97
REMARK 500 TYR C 154 -111.49 51.88
REMARK 500 SER C 205 -114.66 58.32
REMARK 500 TYR D 154 -109.10 51.86
REMARK 500 SER D 205 -118.36 61.07
REMARK 500 TYR E 154 -112.00 52.09
REMARK 500 SER E 205 -115.92 58.74
REMARK 500 TYR F 154 -108.87 52.34
REMARK 500 SER F 205 -116.61 60.96
REMARK 500 TYR G 154 -108.97 51.16
REMARK 500 SER G 205 -116.77 61.43
REMARK 500 TYR H 154 -109.53 53.47
REMARK 500 SER H 205 -117.11 59.81
DBREF 1RYY A 41 667 GB 18139885 AAL60195 41 667
DBREF 1RYY B 41 667 GB 18139885 AAL60195 41 667
DBREF 1RYY C 41 667 GB 18139885 AAL60195 41 667
DBREF 1RYY D 41 667 GB 18139885 AAL60195 41 667
DBREF 1RYY E 41 667 GB 18139885 AAL60195 41 667
DBREF 1RYY F 41 667 GB 18139885 AAL60195 41 667
DBREF 1RYY G 41 667 GB 18139885 AAL60195 41 667
DBREF 1RYY H 41 667 GB 18139885 AAL60195 41 667
SEQADV 1RYY ALA A 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS A 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU A 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY A 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO A 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU A 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN A 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS A 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU A 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE A 676 GB 18139885 MYC TAG
SEQADV 1RYY SER A 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU A 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU A 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP A 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU A 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN A 682 GB 18139885 MYC TAG
SEQADV 1RYY SER A 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA A 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL A 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP A 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS A 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS A 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS A 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS A 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS A 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS A 692 GB 18139885 HIS TAG
SEQADV 1RYY ALA B 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS B 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU B 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY B 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO B 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU B 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN B 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS B 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU B 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE B 676 GB 18139885 MYC TAG
SEQADV 1RYY SER B 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU B 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU B 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP B 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU B 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN B 682 GB 18139885 MYC TAG
SEQADV 1RYY SER B 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA B 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL B 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP B 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS B 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS B 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS B 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS B 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS B 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS B 692 GB 18139885 HIS TAG
SEQADV 1RYY ALA C 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS C 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU C 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY C 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO C 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU C 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN C 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS C 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU C 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE C 676 GB 18139885 MYC TAG
SEQADV 1RYY SER C 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU C 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU C 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP C 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU C 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN C 682 GB 18139885 MYC TAG
SEQADV 1RYY SER C 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA C 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL C 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP C 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS C 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS C 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS C 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS C 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS C 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS C 692 GB 18139885 HIS TAG
SEQADV 1RYY ALA D 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS D 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU D 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY D 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO D 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU D 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN D 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS D 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU D 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE D 676 GB 18139885 MYC TAG
SEQADV 1RYY SER D 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU D 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU D 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP D 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU D 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN D 682 GB 18139885 MYC TAG
SEQADV 1RYY SER D 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA D 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL D 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP D 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS D 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS D 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS D 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS D 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS D 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS D 692 GB 18139885 HIS TAG
SEQADV 1RYY ALA E 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS E 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU E 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY E 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO E 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU E 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN E 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS E 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU E 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE E 676 GB 18139885 MYC TAG
SEQADV 1RYY SER E 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU E 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU E 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP E 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU E 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN E 682 GB 18139885 MYC TAG
SEQADV 1RYY SER E 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA E 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL E 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP E 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS E 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS E 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS E 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS E 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS E 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS E 692 GB 18139885 HIS TAG
SEQADV 1RYY ALA F 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS F 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU F 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY F 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO F 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU F 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN F 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS F 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU F 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE F 676 GB 18139885 MYC TAG
SEQADV 1RYY SER F 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU F 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU F 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP F 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU F 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN F 682 GB 18139885 MYC TAG
SEQADV 1RYY SER F 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA F 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL F 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP F 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS F 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS F 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS F 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS F 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS F 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS F 692 GB 18139885 HIS TAG
SEQADV 1RYY ALA G 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS G 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU G 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY G 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO G 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU G 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN G 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS G 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU G 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE G 676 GB 18139885 MYC TAG
SEQADV 1RYY SER G 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU G 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU G 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP G 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU G 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN G 682 GB 18139885 MYC TAG
SEQADV 1RYY SER G 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA G 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL G 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP G 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS G 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS G 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS G 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS G 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS G 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS G 692 GB 18139885 HIS TAG
SEQADV 1RYY ALA H 206 GB 18139885 TYR 206 ENGINEERED
SEQADV 1RYY LYS H 668 GB 18139885 MYC TAG
SEQADV 1RYY LEU H 669 GB 18139885 MYC TAG
SEQADV 1RYY GLY H 670 GB 18139885 MYC TAG
SEQADV 1RYY PRO H 671 GB 18139885 MYC TAG
SEQADV 1RYY GLU H 672 GB 18139885 MYC TAG
SEQADV 1RYY GLN H 673 GB 18139885 MYC TAG
SEQADV 1RYY LYS H 674 GB 18139885 MYC TAG
SEQADV 1RYY LEU H 675 GB 18139885 MYC TAG
SEQADV 1RYY ILE H 676 GB 18139885 MYC TAG
SEQADV 1RYY SER H 677 GB 18139885 MYC TAG
SEQADV 1RYY GLU H 678 GB 18139885 MYC TAG
SEQADV 1RYY GLU H 679 GB 18139885 MYC TAG
SEQADV 1RYY ASP H 680 GB 18139885 MYC TAG
SEQADV 1RYY LEU H 681 GB 18139885 MYC TAG
SEQADV 1RYY ASN H 682 GB 18139885 MYC TAG
SEQADV 1RYY SER H 683 GB 18139885 MYC TAG
SEQADV 1RYY ALA H 684 GB 18139885 MYC TAG
SEQADV 1RYY VAL H 685 GB 18139885 MYC TAG
SEQADV 1RYY ASP H 686 GB 18139885 MYC TAG
SEQADV 1RYY HIS H 687 GB 18139885 HIS TAG
SEQADV 1RYY HIS H 688 GB 18139885 HIS TAG
SEQADV 1RYY HIS H 689 GB 18139885 HIS TAG
SEQADV 1RYY HIS H 690 GB 18139885 HIS TAG
SEQADV 1RYY HIS H 691 GB 18139885 HIS TAG
SEQADV 1RYY HIS H 692 GB 18139885 HIS TAG
SEQRES 1 A 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 A 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 A 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 A 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 A 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 A 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 A 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 A 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 A 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 A 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 A 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 A 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 A 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 A 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 A 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 A 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 A 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 A 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 A 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 A 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 A 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 A 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 A 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 A 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 A 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 A 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 A 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 A 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 A 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 A 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 A 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 A 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 A 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 A 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 A 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 A 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 A 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 A 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 A 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 A 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 A 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 A 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 A 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 A 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 A 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 A 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 A 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 A 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 A 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 A 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 A 652 HIS HIS
SEQRES 1 B 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 B 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 B 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 B 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 B 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 B 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 B 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 B 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 B 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 B 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 B 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 B 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 B 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 B 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 B 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 B 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 B 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 B 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 B 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 B 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 B 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 B 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 B 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 B 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 B 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 B 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 B 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 B 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 B 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 B 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 B 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 B 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 B 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 B 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 B 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 B 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 B 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 B 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 B 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 B 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 B 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 B 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 B 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 B 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 B 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 B 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 B 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 B 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 B 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 B 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 B 652 HIS HIS
SEQRES 1 C 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 C 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 C 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 C 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 C 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 C 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 C 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 C 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 C 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 C 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 C 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 C 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 C 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 C 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 C 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 C 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 C 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 C 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 C 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 C 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 C 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 C 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 C 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 C 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 C 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 C 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 C 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 C 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 C 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 C 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 C 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 C 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 C 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 C 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 C 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 C 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 C 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 C 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 C 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 C 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 C 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 C 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 C 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 C 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 C 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 C 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 C 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 C 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 C 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 C 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 C 652 HIS HIS
SEQRES 1 D 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 D 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 D 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 D 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 D 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 D 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 D 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 D 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 D 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 D 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 D 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 D 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 D 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 D 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 D 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 D 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 D 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 D 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 D 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 D 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 D 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 D 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 D 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 D 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 D 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 D 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 D 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 D 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 D 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 D 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 D 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 D 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 D 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 D 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 D 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 D 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 D 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 D 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 D 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 D 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 D 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 D 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 D 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 D 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 D 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 D 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 D 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 D 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 D 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 D 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 D 652 HIS HIS
SEQRES 1 E 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 E 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 E 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 E 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 E 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 E 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 E 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 E 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 E 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 E 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 E 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 E 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 E 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 E 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 E 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 E 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 E 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 E 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 E 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 E 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 E 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 E 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 E 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 E 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 E 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 E 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 E 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 E 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 E 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 E 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 E 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 E 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 E 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 E 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 E 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 E 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 E 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 E 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 E 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 E 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 E 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 E 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 E 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 E 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 E 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 E 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 E 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 E 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 E 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 E 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 E 652 HIS HIS
SEQRES 1 F 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 F 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 F 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 F 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 F 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 F 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 F 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 F 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 F 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 F 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 F 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 F 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 F 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 F 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 F 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 F 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 F 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 F 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 F 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 F 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 F 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 F 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 F 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 F 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 F 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 F 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 F 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 F 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 F 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 F 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 F 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 F 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 F 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 F 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 F 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 F 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 F 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 F 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 F 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 F 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 F 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 F 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 F 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 F 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 F 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 F 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 F 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 F 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 F 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 F 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 F 652 HIS HIS
SEQRES 1 G 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 G 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 G 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 G 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 G 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 G 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 G 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 G 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 G 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 G 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 G 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 G 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 G 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 G 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 G 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 G 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 G 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 G 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 G 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 G 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 G 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 G 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 G 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 G 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 G 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 G 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 G 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 G 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 G 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 G 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 G 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 G 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 G 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 G 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 G 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 G 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 G 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 G 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 G 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 G 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 G 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 G 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 G 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 G 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 G 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 G 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 G 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 G 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 G 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 G 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 G 652 HIS HIS
SEQRES 1 H 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 H 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 H 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 H 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 H 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 H 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 H 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 H 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 H 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 H 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 H 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 H 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 H 652 GLY ARG VAL GLY MET THR GLY SER SER ALA GLU GLY PHE
SEQRES 14 H 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 H 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 H 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 H 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 H 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 H 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 H 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 H 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 H 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 H 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 H 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 H 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 H 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 H 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 H 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 H 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 H 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 H 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 H 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 H 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 H 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 H 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 H 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 H 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 H 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 H 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 H 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 H 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 H 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 H 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 H 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 H 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 H 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 H 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 H 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 H 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 H 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 H 652 HIS HIS
FORMUL 9 HOH *321(H2 O1)
HELIX 1 2 ASN A 113 ALA A 118 1 6
HELIX 2 3 THR A 126 LEU A 131 1 6
HELIX 3 4 PRO A 132 GLY A 134 5 3
HELIX 4 5 ASP A 135 GLY A 141 1 7
HELIX 5 6 ASP A 176 VAL A 192 1 17
HELIX 6 7 ALA A 206 LEU A 215 1 10
HELIX 7 8 GLY A 249 THR A 259 1 11
HELIX 8 9 ASP A 273 GLY A 282 1 10
HELIX 9 10 SER A 283 ALA A 291 1 9
HELIX 10 11 GLY A 292 GLN A 295 5 4
HELIX 11 12 TYR A 296 HIS A 305 1 10
HELIX 12 13 ASP A 309 GLY A 314 1 6
HELIX 13 14 ALA A 316 LYS A 325 1 10
HELIX 14 15 TRP A 343 ALA A 355 1 13
HELIX 15 16 SER A 371 TYR A 375 5 5
HELIX 16 17 ASP A 388 VAL A 397 1 10
HELIX 17 18 VAL A 397 LYS A 407 1 11
HELIX 18 19 GLN A 489 LYS A 494 1 6
HELIX 19 20 PRO A 495 GLN A 499 5 5
HELIX 20 21 GLN A 501 SER A 506 1 6
HELIX 21 22 ASP A 558 GLY A 562 5 5
HELIX 22 23 ARG A 576 ARG A 578 5 3
HELIX 23 24 ASN A 634 ALA A 638 5 5
HELIX 24 25 LYS A 639 TYR A 643 5 5
HELIX 25 26 GLY A 653 ALA A 657 5 5
HELIX 26 28 ASN B 113 ALA B 118 1 6
HELIX 27 29 THR B 126 LEU B 131 1 6
HELIX 28 30 PRO B 132 GLY B 134 5 3
HELIX 29 31 ASP B 135 GLY B 141 1 7
HELIX 30 32 ASP B 176 VAL B 192 1 17
HELIX 31 33 ALA B 206 LEU B 215 1 10
HELIX 32 34 GLY B 249 THR B 259 1 11
HELIX 33 35 ASP B 273 GLY B 282 1 10
HELIX 34 36 SER B 283 ALA B 291 1 9
HELIX 35 37 GLY B 292 GLN B 295 5 4
HELIX 36 38 TYR B 296 HIS B 305 1 10
HELIX 37 39 ASP B 309 GLY B 314 1 6
HELIX 38 40 ALA B 316 LYS B 325 1 10
HELIX 39 41 TRP B 343 ALA B 355 1 13
HELIX 40 42 SER B 371 TYR B 375 5 5
HELIX 41 43 ASP B 388 VAL B 397 1 10
HELIX 42 44 VAL B 397 LYS B 407 1 11
HELIX 43 45 GLN B 489 LYS B 494 1 6
HELIX 44 46 PRO B 495 GLN B 499 5 5
HELIX 45 47 GLN B 501 SER B 506 1 6
HELIX 46 48 ASP B 558 GLY B 562 5 5
HELIX 47 49 ARG B 576 ARG B 578 5 3
HELIX 48 50 ASN B 634 ALA B 638 5 5
HELIX 49 51 LYS B 639 TYR B 643 5 5
HELIX 50 53 ASN C 113 ALA C 118 1 6
HELIX 51 54 THR C 126 LEU C 131 1 6
HELIX 52 55 PRO C 132 GLY C 134 5 3
HELIX 53 56 ASP C 135 GLY C 141 1 7
HELIX 54 57 ASP C 176 VAL C 192 1 17
HELIX 55 58 ALA C 206 LEU C 215 1 10
HELIX 56 59 GLY C 249 THR C 259 1 11
HELIX 57 60 ASP C 273 GLY C 282 1 10
HELIX 58 61 SER C 283 ALA C 291 1 9
HELIX 59 62 GLY C 292 GLN C 295 5 4
HELIX 60 63 TYR C 296 HIS C 305 1 10
HELIX 61 64 ASP C 309 GLY C 314 1 6
HELIX 62 65 ALA C 316 LYS C 325 1 10
HELIX 63 66 TRP C 343 ALA C 355 1 13
HELIX 64 67 SER C 371 TYR C 375 5 5
HELIX 65 68 ASP C 388 VAL C 397 1 10
HELIX 66 69 VAL C 397 LYS C 407 1 11
HELIX 67 70 GLN C 489 LYS C 494 1 6
HELIX 68 71 PRO C 495 GLN C 499 5 5
HELIX 69 72 GLN C 501 SER C 506 1 6
HELIX 70 73 ASP C 558 GLY C 562 5 5
HELIX 71 74 ARG C 576 ARG C 578 5 3
HELIX 72 75 ASN C 634 ALA C 638 5 5
HELIX 73 76 LYS C 639 TYR C 643 5 5
HELIX 74 77 GLY C 653 ALA C 657 5 5
HELIX 75 79 ASN D 113 ALA D 118 1 6
HELIX 76 80 THR D 126 LEU D 131 1 6
HELIX 77 81 PRO D 132 GLY D 134 5 3
HELIX 78 82 ASP D 135 GLY D 141 1 7
HELIX 79 83 ASP D 176 VAL D 192 1 17
HELIX 80 84 ALA D 206 LEU D 215 1 10
HELIX 81 85 GLY D 249 THR D 259 1 11
HELIX 82 86 ASP D 273 GLY D 282 1 10
HELIX 83 87 SER D 283 ALA D 291 1 9
HELIX 84 88 GLY D 292 GLN D 295 5 4
HELIX 85 89 TYR D 296 HIS D 305 1 10
HELIX 86 90 ASP D 309 GLY D 314 1 6
HELIX 87 91 ALA D 316 LYS D 325 1 10
HELIX 88 92 TRP D 343 ALA D 355 1 13
HELIX 89 93 SER D 371 TYR D 375 5 5
HELIX 90 94 ASP D 388 VAL D 397 1 10
HELIX 91 95 VAL D 397 LYS D 407 1 11
HELIX 92 96 GLN D 489 LYS D 494 1 6
HELIX 93 97 PRO D 495 GLN D 499 5 5
HELIX 94 98 GLN D 501 SER D 506 1 6
HELIX 95 99 ASP D 558 GLY D 562 5 5
HELIX 96 100 ARG D 576 ARG D 578 5 3
HELIX 97 101 ASN D 634 ALA D 638 5 5
HELIX 98 102 LYS D 639 TYR D 643 5 5
HELIX 99 103 GLY D 653 ALA D 657 5 5
HELIX 100 105 ASN E 113 ALA E 118 1 6
HELIX 101 106 THR E 126 LEU E 131 1 6
HELIX 102 107 PRO E 132 GLY E 134 5 3
HELIX 103 108 ASP E 135 GLY E 141 1 7
HELIX 104 109 ASP E 176 VAL E 192 1 17
HELIX 105 110 ALA E 206 LEU E 215 1 10
HELIX 106 111 GLY E 249 THR E 259 1 11
HELIX 107 112 ASP E 273 GLY E 282 1 10
HELIX 108 113 SER E 283 ALA E 291 1 9
HELIX 109 114 GLY E 292 GLN E 295 5 4
HELIX 110 115 TYR E 296 HIS E 305 1 10
HELIX 111 116 ASP E 309 GLY E 314 1 6
HELIX 112 117 ALA E 316 LYS E 325 1 10
HELIX 113 118 TRP E 343 ALA E 355 1 13
HELIX 114 119 SER E 371 TYR E 375 5 5
HELIX 115 120 ASP E 388 VAL E 397 1 10
HELIX 116 121 VAL E 397 LYS E 407 1 11
HELIX 117 122 ASP E 453 HIS E 455 5 3
HELIX 118 123 GLN E 489 LYS E 494 1 6
HELIX 119 124 PRO E 495 GLN E 499 5 5
HELIX 120 125 GLN E 501 SER E 506 1 6
HELIX 121 126 ASP E 558 GLY E 562 5 5
HELIX 122 127 ARG E 576 ARG E 578 5 3
HELIX 123 128 ASN E 634 ALA E 638 5 5
HELIX 124 129 LYS E 639 TYR E 643 5 5
HELIX 125 130 GLY E 653 ALA E 657 5 5
HELIX 126 132 ASN F 113 ALA F 118 1 6
HELIX 127 133 THR F 126 LEU F 131 1 6
HELIX 128 134 PRO F 132 GLY F 134 5 3
HELIX 129 135 ASP F 135 GLY F 141 1 7
HELIX 130 136 ASP F 176 VAL F 192 1 17
HELIX 131 137 ALA F 206 LEU F 215 1 10
HELIX 132 138 GLY F 249 THR F 259 1 11
HELIX 133 139 ASP F 273 GLY F 282 1 10
HELIX 134 140 SER F 283 GLY F 292 1 10
HELIX 135 141 LEU F 293 GLN F 295 5 3
HELIX 136 142 TYR F 296 HIS F 305 1 10
HELIX 137 143 ASP F 309 GLY F 314 1 6
HELIX 138 144 ALA F 316 LYS F 325 1 10
HELIX 139 145 TRP F 343 ALA F 355 1 13
HELIX 140 146 SER F 371 TYR F 375 5 5
HELIX 141 147 ASP F 388 VAL F 397 1 10
HELIX 142 148 VAL F 397 LYS F 407 1 11
HELIX 143 149 ASP F 453 HIS F 455 5 3
HELIX 144 150 GLN F 489 LYS F 494 1 6
HELIX 145 151 PRO F 495 GLN F 499 5 5
HELIX 146 152 GLN F 501 SER F 506 1 6
HELIX 147 153 ASP F 558 GLY F 562 5 5
HELIX 148 154 ARG F 576 ARG F 578 5 3
HELIX 149 155 ASN F 634 ALA F 638 5 5
HELIX 150 156 LYS F 639 TYR F 643 5 5
HELIX 151 157 GLY F 653 ALA F 657 5 5
HELIX 152 159 ASN G 113 ALA G 118 1 6
HELIX 153 160 THR G 126 LEU G 131 1 6
HELIX 154 161 PRO G 132 GLY G 134 5 3
HELIX 155 162 ASP G 135 GLY G 141 1 7
HELIX 156 163 ASP G 176 VAL G 192 1 17
HELIX 157 164 ALA G 206 LEU G 215 1 10
HELIX 158 165 GLY G 249 THR G 259 1 11
HELIX 159 166 ASP G 273 GLY G 282 1 10
HELIX 160 167 SER G 283 ALA G 291 1 9
HELIX 161 168 GLY G 292 GLN G 295 5 4
HELIX 162 169 TYR G 296 HIS G 305 1 10
HELIX 163 170 ASP G 309 GLY G 314 1 6
HELIX 164 171 ALA G 316 LYS G 325 1 10
HELIX 165 172 TRP G 343 ALA G 355 1 13
HELIX 166 173 SER G 371 TYR G 375 5 5
HELIX 167 174 ASP G 388 VAL G 397 1 10
HELIX 168 175 VAL G 397 LYS G 407 1 11
HELIX 169 176 GLN G 489 LYS G 494 1 6
HELIX 170 177 PRO G 495 GLN G 499 5 5
HELIX 171 178 GLN G 501 SER G 506 1 6
HELIX 172 179 ASP G 558 GLY G 562 5 5
HELIX 173 180 ARG G 576 ARG G 578 5 3
HELIX 174 181 ASN G 634 ALA G 638 5 5
HELIX 175 182 LYS G 639 TYR G 643 5 5
HELIX 176 183 GLY G 653 ALA G 657 5 5
HELIX 177 185 ASN H 113 ALA H 118 1 6
HELIX 178 186 THR H 126 LEU H 131 1 6
HELIX 179 187 PRO H 132 GLY H 134 5 3
HELIX 180 188 ASP H 135 GLY H 141 1 7
HELIX 181 189 ASP H 176 VAL H 192 1 17
HELIX 182 190 ALA H 206 LEU H 215 1 10
HELIX 183 191 GLY H 249 THR H 259 1 11
HELIX 184 192 ASP H 273 GLY H 282 1 10
HELIX 185 193 SER H 283 GLY H 292 1 10
HELIX 186 194 LEU H 293 GLN H 295 5 3
HELIX 187 195 TYR H 296 HIS H 305 1 10
HELIX 188 196 ASP H 309 GLY H 314 1 6
HELIX 189 197 ALA H 316 LYS H 325 1 10
HELIX 190 198 TRP H 343 ALA H 355 1 13
HELIX 191 199 SER H 371 TYR H 375 5 5
HELIX 192 200 ASP H 388 VAL H 397 1 10
HELIX 193 201 VAL H 397 LYS H 407 1 11
HELIX 194 202 GLN H 489 LYS H 494 1 6
HELIX 195 203 PRO H 495 GLN H 499 5 5
HELIX 196 204 GLN H 501 SER H 506 1 6
HELIX 197 205 ASP H 558 GLY H 562 5 5
HELIX 198 206 ARG H 576 ARG H 578 5 3
HELIX 199 207 ASN H 634 ALA H 638 5 5
HELIX 200 208 LYS H 639 TYR H 643 5 5
HELIX 201 209 GLY H 653 ALA H 657 5 5
SHEET 1 A 6 TYR A 75 PRO A 83 0
SHEET 2 A 6 LYS A 89 PRO A 97 -1 O LEU A 90 N VAL A 82
SHEET 3 A 6 ILE A 144 ASP A 149 -1 O ARG A 145 N VAL A 95
SHEET 4 A 6 ALA A 103 THR A 110 1 N THR A 110 O GLN A 148
SHEET 5 A 6 SER A 195 SER A 205 1 O GLY A 200 N LEU A 107
SHEET 6 A 6 LEU A 222 PRO A 230 1 O GLU A 228 N GLY A 203
SHEET 1 B 2 PHE A 241 HIS A 242 0
SHEET 2 B 2 ALA A 245 PHE A 246 -1 O ALA A 245 N HIS A 242
SHEET 1 C 4 MET A 330 GLY A 335 0
SHEET 2 C 4 ASN A 361 GLY A 366 1 O VAL A 364 N TRP A 332
SHEET 3 C 4 ALA A 418 ASN A 422 1 O ILE A 419 N LEU A 363
SHEET 4 C 4 LYS A 427 TYR A 431 -1 O LYS A 427 N ASN A 422
SHEET 1 D 2 THR A 379 LEU A 380 0
SHEET 2 D 2 LEU A 383 GLU A 384 -1 O LEU A 383 N LEU A 380
SHEET 1 E 6 GLY A 456 SER A 458 0
SHEET 2 E 6 THR A 447 ALA A 452 -1 N ALA A 452 O GLY A 456
SHEET 3 E 6 SER A 659 LEU A 662 -1 O LEU A 662 N THR A 447
SHEET 4 E 6 VAL A 529 THR A 536 -1 N VAL A 529 O LEU A 661
SHEET 5 E 6 ALA A 646 HIS A 652 -1 O SER A 649 N ALA A 535
SHEET 6 E 6 GLY A 466 SER A 472 -1 N GLY A 466 O HIS A 652
SHEET 1 F 5 GLY A 456 SER A 458 0
SHEET 2 F 5 THR A 447 ALA A 452 -1 N ALA A 452 O GLY A 456
SHEET 3 F 5 SER A 659 LEU A 662 -1 O LEU A 662 N THR A 447
SHEET 4 F 5 VAL A 529 THR A 536 -1 N VAL A 529 O LEU A 661
SHEET 5 F 5 LEU A 593 THR A 598 -1 O TYR A 595 N LEU A 532
SHEET 1 G 4 VAL A 510 GLU A 514 0
SHEET 2 G 4 ARG A 611 GLN A 617 -1 O VAL A 614 N TYR A 513
SHEET 3 G 4 ASP A 542 VAL A 550 -1 N ILE A 548 O MET A 613
SHEET 4 G 4 GLU A 565 ARG A 574 -1 O LEU A 566 N ASP A 549
SHEET 1 H 2 VAL A 522 GLY A 526 0
SHEET 2 H 2 VAL A 602 PHE A 606 -1 O HIS A 604 N VAL A 524
SHEET 1 I 6 TYR B 75 PRO B 83 0
SHEET 2 I 6 LYS B 89 PRO B 97 -1 O THR B 92 N VAL B 80
SHEET 3 I 6 ILE B 144 ASP B 149 -1 O ARG B 145 N VAL B 95
SHEET 4 I 6 ALA B 103 THR B 110 1 N THR B 110 O GLN B 148
SHEET 5 I 6 SER B 195 SER B 205 1 O GLY B 200 N LEU B 107
SHEET 6 I 6 LEU B 222 PRO B 230 1 O ALA B 226 N MET B 201
SHEET 1 J 2 PHE B 241 HIS B 242 0
SHEET 2 J 2 ALA B 245 PHE B 246 -1 O ALA B 245 N HIS B 242
SHEET 1 K 4 MET B 330 GLY B 335 0
SHEET 2 K 4 ASN B 361 GLY B 366 1 O VAL B 364 N TRP B 332
SHEET 3 K 4 ALA B 418 ASN B 422 1 O ILE B 419 N LEU B 363
SHEET 4 K 4 LYS B 427 TYR B 431 -1 O LYS B 427 N ASN B 422
SHEET 1 L 2 THR B 379 LEU B 380 0
SHEET 2 L 2 LEU B 383 GLU B 384 -1 O LEU B 383 N LEU B 380
SHEET 1 M 6 GLY B 456 SER B 458 0
SHEET 2 M 6 THR B 447 ALA B 452 -1 N ALA B 452 O GLY B 456
SHEET 3 M 6 SER B 659 LEU B 662 -1 O LEU B 662 N THR B 447
SHEET 4 M 6 VAL B 529 THR B 536 -1 N VAL B 529 O LEU B 661
SHEET 5 M 6 ALA B 646 HIS B 652 -1 O SER B 649 N ALA B 535
SHEET 6 M 6 GLY B 466 SER B 472 -1 N TYR B 470 O GLN B 648
SHEET 1 N 5 GLY B 456 SER B 458 0
SHEET 2 N 5 THR B 447 ALA B 452 -1 N ALA B 452 O GLY B 456
SHEET 3 N 5 SER B 659 LEU B 662 -1 O LEU B 662 N THR B 447
SHEET 4 N 5 VAL B 529 THR B 536 -1 N VAL B 529 O LEU B 661
SHEET 5 N 5 LEU B 593 THR B 598 -1 O TYR B 595 N LEU B 532
SHEET 1 O 4 VAL B 510 GLU B 514 0
SHEET 2 O 4 ARG B 611 GLN B 617 -1 O VAL B 614 N TYR B 513
SHEET 3 O 4 ASP B 542 VAL B 550 -1 N ILE B 548 O MET B 613
SHEET 4 O 4 GLU B 565 ARG B 574 -1 O LEU B 566 N ASP B 549
SHEET 1 P 3 VAL B 602 PHE B 606 0
SHEET 2 P 3 VAL B 522 GLY B 526 -1 N VAL B 524 O HIS B 604
SHEET 3 P 3 VAL B 664 VAL B 665 -1 O VAL B 665 N ARG B 523
SHEET 1 Q 6 TYR C 75 PRO C 83 0
SHEET 2 Q 6 LYS C 89 PRO C 97 -1 O LEU C 90 N VAL C 82
SHEET 3 Q 6 ILE C 144 ASP C 149 -1 O ARG C 145 N VAL C 95
SHEET 4 Q 6 ALA C 103 THR C 110 1 N THR C 110 O GLN C 148
SHEET 5 Q 6 SER C 195 SER C 205 1 O GLY C 200 N LEU C 107
SHEET 6 Q 6 LEU C 222 PRO C 230 1 O GLU C 228 N GLY C 203
SHEET 1 R 2 PHE C 241 HIS C 242 0
SHEET 2 R 2 ALA C 245 PHE C 246 -1 O ALA C 245 N HIS C 242
SHEET 1 S 4 MET C 330 GLY C 335 0
SHEET 2 S 4 ASN C 361 GLY C 366 1 O VAL C 364 N TRP C 332
SHEET 3 S 4 ALA C 418 ASN C 422 1 O ILE C 419 N LEU C 363
SHEET 4 S 4 LYS C 427 TYR C 431 -1 O LYS C 427 N ASN C 422
SHEET 1 T 2 THR C 379 LEU C 380 0
SHEET 2 T 2 LEU C 383 GLU C 384 -1 O LEU C 383 N LEU C 380
SHEET 1 U 6 GLY C 456 SER C 458 0
SHEET 2 U 6 THR C 447 ALA C 452 -1 N ALA C 452 O GLY C 456
SHEET 3 U 6 SER C 659 LEU C 662 -1 O LEU C 662 N THR C 447
SHEET 4 U 6 VAL C 529 THR C 536 -1 N VAL C 529 O LEU C 661
SHEET 5 U 6 ALA C 646 HIS C 652 -1 O SER C 649 N ALA C 535
SHEET 6 U 6 GLY C 466 SER C 472 -1 N GLY C 466 O HIS C 652
SHEET 1 V 5 GLY C 456 SER C 458 0
SHEET 2 V 5 THR C 447 ALA C 452 -1 N ALA C 452 O GLY C 456
SHEET 3 V 5 SER C 659 LEU C 662 -1 O LEU C 662 N THR C 447
SHEET 4 V 5 VAL C 529 THR C 536 -1 N VAL C 529 O LEU C 661
SHEET 5 V 5 LEU C 593 THR C 598 -1 O TYR C 595 N LEU C 532
SHEET 1 W 4 VAL C 510 GLU C 514 0
SHEET 2 W 4 ARG C 611 GLN C 617 -1 O ILE C 616 N VAL C 511
SHEET 3 W 4 ASP C 542 VAL C 550 -1 N ILE C 548 O MET C 613
SHEET 4 W 4 GLU C 565 ARG C 574 -1 O LEU C 566 N ASP C 549
SHEET 1 X 3 VAL C 602 PHE C 606 0
SHEET 2 X 3 VAL C 522 GLY C 526 -1 N VAL C 522 O PHE C 606
SHEET 3 X 3 VAL C 664 VAL C 665 -1 O VAL C 665 N ARG C 523
SHEET 1 Y 6 TYR D 75 PRO D 83 0
SHEET 2 Y 6 LYS D 89 PRO D 97 -1 O ILE D 96 N ILE D 76
SHEET 3 Y 6 ILE D 144 ASP D 149 -1 O ARG D 145 N VAL D 95
SHEET 4 Y 6 ALA D 103 THR D 110 1 N THR D 110 O GLN D 148
SHEET 5 Y 6 SER D 195 SER D 205 1 O GLY D 200 N LEU D 107
SHEET 6 Y 6 LEU D 222 PRO D 230 1 O GLU D 228 N GLY D 203
SHEET 1 Z 2 PHE D 241 HIS D 242 0
SHEET 2 Z 2 ALA D 245 PHE D 246 -1 O ALA D 245 N HIS D 242
SHEET 1 AA 4 MET D 330 GLY D 335 0
SHEET 2 AA 4 ASN D 361 GLY D 366 1 O VAL D 364 N TRP D 332
SHEET 3 AA 4 ALA D 418 ASN D 422 1 O TYR D 421 N MET D 365
SHEET 4 AA 4 LYS D 427 TYR D 431 -1 O LYS D 427 N ASN D 422
SHEET 1 AB 2 THR D 379 LEU D 380 0
SHEET 2 AB 2 LEU D 383 GLU D 384 -1 O LEU D 383 N LEU D 380
SHEET 1 AC 6 LEU D 457 SER D 458 0
SHEET 2 AC 6 THR D 447 LEU D 451 -1 N TYR D 450 O SER D 458
SHEET 3 AC 6 SER D 659 LEU D 662 -1 O LEU D 662 N THR D 447
SHEET 4 AC 6 VAL D 529 THR D 536 -1 N VAL D 529 O LEU D 661
SHEET 5 AC 6 ALA D 646 HIS D 652 -1 O SER D 649 N ALA D 535
SHEET 6 AC 6 GLY D 466 SER D 472 -1 N GLY D 466 O HIS D 652
SHEET 1 AD 5 LEU D 457 SER D 458 0
SHEET 2 AD 5 THR D 447 LEU D 451 -1 N TYR D 450 O SER D 458
SHEET 3 AD 5 SER D 659 LEU D 662 -1 O LEU D 662 N THR D 447
SHEET 4 AD 5 VAL D 529 THR D 536 -1 N VAL D 529 O LEU D 661
SHEET 5 AD 5 LEU D 593 THR D 598 -1 O TYR D 595 N LEU D 532
SHEET 1 AE 4 VAL D 510 GLU D 514 0
SHEET 2 AE 4 ARG D 611 GLN D 617 -1 O ILE D 616 N VAL D 511
SHEET 3 AE 4 ASP D 542 VAL D 550 -1 N ILE D 548 O MET D 613
SHEET 4 AE 4 GLU D 565 ARG D 574 -1 O LEU D 566 N ASP D 549
SHEET 1 AF 2 VAL D 522 GLY D 526 0
SHEET 2 AF 2 VAL D 602 PHE D 606 -1 O PHE D 606 N VAL D 522
SHEET 1 AG 6 TYR E 75 PRO E 83 0
SHEET 2 AG 6 LYS E 89 PRO E 97 -1 O ILE E 96 N ILE E 76
SHEET 3 AG 6 ILE E 144 ASP E 149 -1 O ARG E 145 N VAL E 95
SHEET 4 AG 6 ALA E 103 THR E 110 1 N THR E 110 O GLN E 148
SHEET 5 AG 6 SER E 195 SER E 205 1 O GLY E 200 N LEU E 107
SHEET 6 AG 6 LEU E 222 PRO E 230 1 O GLU E 228 N GLY E 203
SHEET 1 AH 2 PHE E 241 HIS E 242 0
SHEET 2 AH 2 ALA E 245 PHE E 246 -1 O ALA E 245 N HIS E 242
SHEET 1 AI 4 MET E 330 GLY E 335 0
SHEET 2 AI 4 ASN E 361 GLY E 366 1 O VAL E 364 N TRP E 332
SHEET 3 AI 4 ALA E 418 ASN E 422 1 O TYR E 421 N MET E 365
SHEET 4 AI 4 LYS E 427 TYR E 431 -1 O LYS E 427 N ASN E 422
SHEET 1 AJ 2 THR E 379 LEU E 380 0
SHEET 2 AJ 2 LEU E 383 GLU E 384 -1 O LEU E 383 N LEU E 380
SHEET 1 AK 6 GLY E 456 SER E 458 0
SHEET 2 AK 6 THR E 447 ALA E 452 -1 N ALA E 452 O GLY E 456
SHEET 3 AK 6 SER E 659 LEU E 662 -1 O LEU E 662 N THR E 447
SHEET 4 AK 6 VAL E 529 THR E 536 -1 N VAL E 529 O LEU E 661
SHEET 5 AK 6 ALA E 646 HIS E 652 -1 O SER E 649 N ALA E 535
SHEET 6 AK 6 GLY E 466 SER E 472 -1 N TYR E 470 O GLN E 648
SHEET 1 AL 5 GLY E 456 SER E 458 0
SHEET 2 AL 5 THR E 447 ALA E 452 -1 N ALA E 452 O GLY E 456
SHEET 3 AL 5 SER E 659 LEU E 662 -1 O LEU E 662 N THR E 447
SHEET 4 AL 5 VAL E 529 THR E 536 -1 N VAL E 529 O LEU E 661
SHEET 5 AL 5 LEU E 593 THR E 598 -1 O TYR E 595 N LEU E 532
SHEET 1 AM 4 VAL E 510 GLU E 514 0
SHEET 2 AM 4 ARG E 611 GLN E 617 -1 O VAL E 614 N TYR E 513
SHEET 3 AM 4 ASP E 542 VAL E 550 -1 N ILE E 548 O MET E 613
SHEET 4 AM 4 GLU E 565 ARG E 574 -1 O LEU E 566 N ASP E 549
SHEET 1 AN 3 VAL E 602 PHE E 606 0
SHEET 2 AN 3 VAL E 522 GLY E 526 -1 N VAL E 522 O PHE E 606
SHEET 3 AN 3 VAL E 664 VAL E 665 -1 O VAL E 665 N ARG E 523
SHEET 1 AO 6 TYR F 75 PRO F 83 0
SHEET 2 AO 6 LYS F 89 PRO F 97 -1 O ILE F 96 N ILE F 76
SHEET 3 AO 6 ILE F 144 ASP F 149 -1 O ARG F 145 N VAL F 95
SHEET 4 AO 6 ALA F 103 THR F 110 1 N THR F 110 O GLN F 148
SHEET 5 AO 6 SER F 195 SER F 205 1 O GLY F 200 N LEU F 107
SHEET 6 AO 6 LEU F 222 PRO F 230 1 O ALA F 226 N MET F 201
SHEET 1 AP 2 PHE F 241 HIS F 242 0
SHEET 2 AP 2 ALA F 245 PHE F 246 -1 O ALA F 245 N HIS F 242
SHEET 1 AQ 4 MET F 330 GLY F 335 0
SHEET 2 AQ 4 ASN F 361 GLY F 366 1 O VAL F 364 N TRP F 332
SHEET 3 AQ 4 ALA F 418 ASN F 422 1 O ILE F 419 N LEU F 363
SHEET 4 AQ 4 LYS F 427 TYR F 431 -1 O LYS F 427 N ASN F 422
SHEET 1 AR 2 THR F 379 LEU F 380 0
SHEET 2 AR 2 LEU F 383 GLU F 384 -1 O LEU F 383 N LEU F 380
SHEET 1 AS 6 LEU F 457 SER F 458 0
SHEET 2 AS 6 THR F 447 LEU F 451 -1 N TYR F 450 O SER F 458
SHEET 3 AS 6 SER F 659 LEU F 662 -1 O LEU F 662 N THR F 447
SHEET 4 AS 6 VAL F 529 THR F 536 -1 N VAL F 529 O LEU F 661
SHEET 5 AS 6 ALA F 646 HIS F 652 -1 O SER F 649 N ALA F 535
SHEET 6 AS 6 GLY F 466 SER F 472 -1 N GLY F 466 O HIS F 652
SHEET 1 AT 5 LEU F 457 SER F 458 0
SHEET 2 AT 5 THR F 447 LEU F 451 -1 N TYR F 450 O SER F 458
SHEET 3 AT 5 SER F 659 LEU F 662 -1 O LEU F 662 N THR F 447
SHEET 4 AT 5 VAL F 529 THR F 536 -1 N VAL F 529 O LEU F 661
SHEET 5 AT 5 LEU F 593 THR F 598 -1 O TYR F 595 N LEU F 532
SHEET 1 AU 4 VAL F 510 GLU F 514 0
SHEET 2 AU 4 ARG F 611 GLN F 617 -1 O VAL F 614 N TYR F 513
SHEET 3 AU 4 ASP F 542 VAL F 550 -1 N ILE F 548 O MET F 613
SHEET 4 AU 4 GLU F 565 ARG F 574 -1 O LEU F 566 N ASP F 549
SHEET 1 AV 3 VAL F 602 PHE F 606 0
SHEET 2 AV 3 VAL F 522 GLY F 526 -1 N VAL F 522 O PHE F 606
SHEET 3 AV 3 VAL F 664 VAL F 665 -1 O VAL F 665 N ARG F 523
SHEET 1 AW 6 TYR G 75 PRO G 83 0
SHEET 2 AW 6 LYS G 89 PRO G 97 -1 O ILE G 94 N ARG G 78
SHEET 3 AW 6 ILE G 144 ASP G 149 -1 O PHE G 147 N VAL G 93
SHEET 4 AW 6 ALA G 103 THR G 110 1 N THR G 110 O GLN G 148
SHEET 5 AW 6 SER G 195 SER G 205 1 O GLY G 200 N LEU G 107
SHEET 6 AW 6 LEU G 222 PRO G 230 1 O GLU G 228 N GLY G 203
SHEET 1 AX 2 PHE G 241 HIS G 242 0
SHEET 2 AX 2 ALA G 245 PHE G 246 -1 O ALA G 245 N HIS G 242
SHEET 1 AY 4 MET G 330 GLY G 335 0
SHEET 2 AY 4 ASN G 361 GLY G 366 1 O VAL G 364 N TRP G 332
SHEET 3 AY 4 ALA G 418 ASN G 422 1 O TYR G 421 N MET G 365
SHEET 4 AY 4 LYS G 427 TYR G 431 -1 O LYS G 427 N ASN G 422
SHEET 1 AZ 2 THR G 379 LEU G 380 0
SHEET 2 AZ 2 LEU G 383 GLU G 384 -1 O LEU G 383 N LEU G 380
SHEET 1 BA 6 GLY G 456 SER G 458 0
SHEET 2 BA 6 THR G 447 ALA G 452 -1 N ALA G 452 O GLY G 456
SHEET 3 BA 6 SER G 659 LEU G 662 -1 O LEU G 662 N THR G 447
SHEET 4 BA 6 VAL G 529 THR G 536 -1 N VAL G 529 O LEU G 661
SHEET 5 BA 6 ALA G 646 HIS G 652 -1 O SER G 649 N ALA G 535
SHEET 6 BA 6 GLY G 466 SER G 472 -1 N GLY G 466 O HIS G 652
SHEET 1 BB 5 GLY G 456 SER G 458 0
SHEET 2 BB 5 THR G 447 ALA G 452 -1 N ALA G 452 O GLY G 456
SHEET 3 BB 5 SER G 659 LEU G 662 -1 O LEU G 662 N THR G 447
SHEET 4 BB 5 VAL G 529 THR G 536 -1 N VAL G 529 O LEU G 661
SHEET 5 BB 5 LEU G 593 THR G 598 -1 O TYR G 595 N LEU G 532
SHEET 1 BC 4 VAL G 510 GLU G 514 0
SHEET 2 BC 4 ARG G 611 GLN G 617 -1 O VAL G 614 N TYR G 513
SHEET 3 BC 4 ASP G 542 VAL G 550 -1 N ILE G 548 O MET G 613
SHEET 4 BC 4 GLU G 565 ARG G 574 -1 O LEU G 566 N ASP G 549
SHEET 1 BD 2 VAL G 522 GLY G 526 0
SHEET 2 BD 2 VAL G 602 PHE G 606 -1 O PHE G 606 N VAL G 522
SHEET 1 BE 6 TYR H 75 PRO H 83 0
SHEET 2 BE 6 LYS H 89 PRO H 97 -1 O ILE H 96 N ILE H 76
SHEET 3 BE 6 ILE H 144 ASP H 149 -1 O ARG H 145 N VAL H 95
SHEET 4 BE 6 ALA H 103 THR H 110 1 N THR H 110 O GLN H 148
SHEET 5 BE 6 SER H 195 SER H 205 1 O GLY H 200 N ILE H 105
SHEET 6 BE 6 LEU H 222 PRO H 230 1 O GLU H 228 N GLY H 203
SHEET 1 BF 2 PHE H 241 HIS H 242 0
SHEET 2 BF 2 ALA H 245 PHE H 246 -1 O ALA H 245 N HIS H 242
SHEET 1 BG 4 MET H 330 GLY H 335 0
SHEET 2 BG 4 ASN H 361 GLY H 366 1 O VAL H 364 N TRP H 332
SHEET 3 BG 4 ALA H 418 ASN H 422 1 O TYR H 421 N MET H 365
SHEET 4 BG 4 LYS H 427 TYR H 431 -1 O LYS H 427 N ASN H 422
SHEET 1 BH 2 THR H 379 LEU H 380 0
SHEET 2 BH 2 LEU H 383 GLU H 384 -1 O LEU H 383 N LEU H 380
SHEET 1 BI 6 LEU H 457 SER H 458 0
SHEET 2 BI 6 THR H 447 LEU H 451 -1 N TYR H 450 O SER H 458
SHEET 3 BI 6 SER H 659 LEU H 662 -1 O LEU H 662 N THR H 447
SHEET 4 BI 6 VAL H 529 THR H 536 -1 N VAL H 529 O LEU H 661
SHEET 5 BI 6 ALA H 646 HIS H 652 -1 O SER H 649 N ALA H 535
SHEET 6 BI 6 GLY H 466 SER H 472 -1 N TYR H 470 O GLN H 648
SHEET 1 BJ 5 LEU H 457 SER H 458 0
SHEET 2 BJ 5 THR H 447 LEU H 451 -1 N TYR H 450 O SER H 458
SHEET 3 BJ 5 SER H 659 LEU H 662 -1 O LEU H 662 N THR H 447
SHEET 4 BJ 5 VAL H 529 THR H 536 -1 N VAL H 529 O LEU H 661
SHEET 5 BJ 5 LEU H 593 THR H 598 -1 O TYR H 595 N LEU H 532
SHEET 1 BK 4 VAL H 510 GLU H 514 0
SHEET 2 BK 4 ARG H 611 GLN H 617 -1 O VAL H 614 N TYR H 513
SHEET 3 BK 4 ASP H 542 VAL H 550 -1 N ILE H 548 O MET H 613
SHEET 4 BK 4 GLU H 565 ARG H 574 -1 O LEU H 566 N ASP H 549
SHEET 1 BL 3 VAL H 602 PHE H 606 0
SHEET 2 BL 3 VAL H 522 GLY H 526 -1 N VAL H 524 O HIS H 604
SHEET 3 BL 3 VAL H 664 VAL H 665 -1 O VAL H 665 N ARG H 523
CISPEP 1 TRP A 434 PRO A 435 0 -0.77
CISPEP 2 ARG A 483 PRO A 484 0 -0.27
CISPEP 3 PHE A 621 PRO A 622 0 -0.78
CISPEP 4 TRP B 434 PRO B 435 0 -0.57
CISPEP 5 ARG B 483 PRO B 484 0 -0.42
CISPEP 6 PHE B 621 PRO B 622 0 -0.96
CISPEP 7 TRP C 434 PRO C 435 0 -0.85
CISPEP 8 ARG C 483 PRO C 484 0 -0.03
CISPEP 9 PHE C 621 PRO C 622 0 -0.77
CISPEP 10 TRP D 434 PRO D 435 0 -0.72
CISPEP 11 ARG D 483 PRO D 484 0 -0.36
CISPEP 12 PHE D 621 PRO D 622 0 -0.96
CISPEP 13 TRP E 434 PRO E 435 0 -0.58
CISPEP 14 ARG E 483 PRO E 484 0 -0.13
CISPEP 15 PHE E 621 PRO E 622 0 -0.93
CISPEP 16 TRP F 434 PRO F 435 0 -0.67
CISPEP 17 ARG F 483 PRO F 484 0 -0.24
CISPEP 18 PHE F 621 PRO F 622 0 -0.78
CISPEP 19 TRP G 434 PRO G 435 0 -0.98
CISPEP 20 ARG G 483 PRO G 484 0 -0.10
CISPEP 21 PHE G 621 PRO G 622 0 -0.90
CISPEP 22 TRP H 434 PRO H 435 0 -0.44
CISPEP 23 ARG H 483 PRO H 484 0 -0.18
CISPEP 24 PHE H 621 PRO H 622 0 -0.95
CRYST1 91.649 177.513 169.967 90.00 91.03 90.00 P 1 21 1 16
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 0.010911 0.000000 0.000196 0.00000
SCALE2 0.000000 0.005633 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005884 0.00000
TER 4837 LYS A 666
TER 9674 LYS B 666
TER 14511 LYS C 666
TER 19348 LYS D 666
TER 24185 LYS E 666
TER 29022 LYS F 666
TER 33859 LYS G 666
TER 38696 LYS H 666
MASTER 925 0 0 201 253 0 0 639009 8 0 408
END |