| content |
HEADER STRUCTURAL PROTEIN 07-NOV-19 6L8Q
TITLE COMPLEX STRUCTURE OF BAT CD26 AND MERS-RBD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: SPIKE GLYCOPROTEIN;
COMPND 7 CHAIN: B, D, F, H;
COMPND 8 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYOTIS DAVIDII;
SOURCE 3 ORGANISM_COMMON: DAVID'S MYOTIS;
SOURCE 4 ORGANISM_TAXID: 225400;
SOURCE 5 GENE: MDA_GLEAN10024208;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MIDDLE EAST RESPIRATORY SYNDROME-RELATED
SOURCE 10 CORONAVIRUS;
SOURCE 11 ORGANISM_TAXID: 1335626;
SOURCE 12 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS COMPLEX, CORONAVIRUS, BAT, RECEPTOR, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YUAN
REVDAT 3 29-JUL-20 6L8Q 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 17-JUN-20 6L8Q 1 JRNL
REVDAT 1 04-DEC-19 6L8Q 0
JRNL AUTH Y.YUAN,J.QI,R.PENG,C.LI,G.LU,J.YAN,Q.WANG,G.F.GAO
JRNL TITL MOLECULAR BASIS OF BINDING BETWEEN MIDDLE EAST RESPIRATORY
JRNL TITL 2 SYNDROME CORONAVIRUS AND CD26 FROM SEVEN BAT SPECIES.
JRNL REF J.VIROL. V. 94 2020
JRNL REFN ESSN 1098-5514
JRNL PMID 31776269
JRNL DOI 10.1128/JVI.01387-19
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.LU,Y.HU,Q.WANG,J.QI,F.GAO,Y.LI,Y.ZHANG,W.ZHANG,Y.YUAN,
REMARK 1 AUTH 2 J.BAO,B.ZHANG,Y.SHI,J.YAN,G.F.GAO
REMARK 1 TITL MOLECULAR BASIS OF BINDING BETWEEN NOVEL HUMAN CORONAVIRUS
REMARK 1 TITL 2 MERS-COV AND ITS RECEPTOR CD26.
REMARK 1 REF NATURE V. 500 227 2013
REMARK 1 REFN ESSN 1476-4687
REMARK 1 PMID 23831647
REMARK 1 DOI 10.1038/NATURE12328
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16_3549
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.3
REMARK 3 NUMBER OF REFLECTIONS : 95268
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 4577
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.8100 - 9.6000 0.98 3506 182 0.2178 0.2376
REMARK 3 2 9.6000 - 7.6300 0.99 3525 177 0.1828 0.1902
REMARK 3 3 7.6300 - 6.6700 0.99 3568 178 0.2000 0.2603
REMARK 3 4 6.6700 - 6.0600 1.00 3524 140 0.2011 0.2260
REMARK 3 5 6.0600 - 5.6300 1.00 3545 235 0.1920 0.2482
REMARK 3 6 5.6300 - 5.2900 1.00 3590 123 0.1849 0.1716
REMARK 3 7 5.2900 - 5.0300 1.00 3515 174 0.1608 0.2294
REMARK 3 8 5.0300 - 4.8100 1.00 3480 233 0.1610 0.2077
REMARK 3 9 4.8100 - 4.6300 1.00 3533 167 0.1533 0.2123
REMARK 3 10 4.6300 - 4.4700 1.00 3589 170 0.1531 0.2001
REMARK 3 11 4.4700 - 4.3300 1.00 3571 170 0.1695 0.2082
REMARK 3 12 4.3300 - 4.2000 1.00 3522 188 0.1725 0.2211
REMARK 3 13 4.2000 - 4.0900 1.00 3552 129 0.1936 0.2283
REMARK 3 14 4.0900 - 3.9900 1.00 3542 171 0.1931 0.2385
REMARK 3 15 3.9900 - 3.9000 1.00 3542 178 0.2037 0.2606
REMARK 3 16 3.9000 - 3.8200 0.99 3477 184 0.2160 0.2491
REMARK 3 17 3.8200 - 3.7400 0.95 3367 185 0.2134 0.2252
REMARK 3 18 3.7400 - 3.6700 0.90 3161 207 0.2188 0.2539
REMARK 3 19 3.6700 - 3.6100 0.85 2997 120 0.2371 0.3127
REMARK 3 20 3.6100 - 3.5500 0.81 2921 154 0.2417 0.2736
REMARK 3 21 3.5500 - 3.4900 0.78 2674 164 0.2429 0.2779
REMARK 3 22 3.4900 - 3.4300 0.74 2626 151 0.2425 0.2966
REMARK 3 23 3.4300 - 3.3800 0.72 2496 119 0.2473 0.3035
REMARK 3 24 3.3800 - 3.3400 0.66 2397 102 0.2601 0.3090
REMARK 3 25 3.3400 - 3.2900 0.64 2242 112 0.2584 0.3493
REMARK 3 26 3.2900 - 3.2500 0.60 2157 111 0.2662 0.3963
REMARK 3 27 3.2500 - 3.2100 0.58 2003 107 0.2777 0.3198
REMARK 3 28 3.2100 - 3.1700 0.52 1868 89 0.2850 0.3127
REMARK 3 29 3.1700 - 3.1300 0.49 1739 60 0.2817 0.3472
REMARK 3 30 3.1300 - 3.1000 0.42 1462 97 0.3014 0.3005
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.217
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.597
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.28
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 31574
REMARK 3 ANGLE : 0.651 42975
REMARK 3 CHIRALITY : 0.047 4740
REMARK 3 PLANARITY : 0.004 5461
REMARK 3 DIHEDRAL : 17.235 11526
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 119.6096 31.0895 411.8959
REMARK 3 T TENSOR
REMARK 3 T11: 0.2837 T22: 0.2903
REMARK 3 T33: 0.2731 T12: 0.0467
REMARK 3 T13: 0.0156 T23: 0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 0.3587 L22: 0.5538
REMARK 3 L33: 0.3912 L12: 0.0273
REMARK 3 L13: -0.1124 L23: 0.0448
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: 0.0666 S13: 0.0164
REMARK 3 S21: -0.0490 S22: 0.0363 S23: -0.0155
REMARK 3 S31: -0.0285 S32: -0.0103 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 152.7996 -7.5596 404.5572
REMARK 3 T TENSOR
REMARK 3 T11: 0.3141 T22: 0.4405
REMARK 3 T33: 0.4332 T12: 0.0428
REMARK 3 T13: 0.0022 T23: -0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 0.2298 L22: 0.1577
REMARK 3 L33: 0.0719 L12: -0.0409
REMARK 3 L13: -0.0056 L23: 0.0391
REMARK 3 S TENSOR
REMARK 3 S11: 0.0595 S12: -0.0402 S13: -0.0348
REMARK 3 S21: -0.0342 S22: 0.0469 S23: -0.1285
REMARK 3 S31: -0.0451 S32: 0.0733 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 111.9004 -43.8794 411.8619
REMARK 3 T TENSOR
REMARK 3 T11: 0.2548 T22: 0.2768
REMARK 3 T33: 0.2707 T12: 0.0453
REMARK 3 T13: -0.0190 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 0.3464 L22: 0.5075
REMARK 3 L33: 0.4475 L12: 0.0250
REMARK 3 L13: 0.0816 L23: -0.0408
REMARK 3 S TENSOR
REMARK 3 S11: 0.0219 S12: 0.0743 S13: -0.0229
REMARK 3 S21: -0.0405 S22: 0.0208 S23: 0.0014
REMARK 3 S31: 0.0157 S32: 0.0228 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 78.6777 -5.2361 404.5337
REMARK 3 T TENSOR
REMARK 3 T11: 0.3280 T22: 0.4645
REMARK 3 T33: 0.4455 T12: 0.0527
REMARK 3 T13: 0.0186 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.1743 L22: 0.1403
REMARK 3 L33: 0.0832 L12: -0.0064
REMARK 3 L13: -0.0102 L23: -0.0594
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: -0.0035 S13: 0.0684
REMARK 3 S21: 0.0777 S22: 0.0611 S23: 0.1234
REMARK 3 S31: 0.0528 S32: -0.0900 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): 77.4026 37.6962 366.1734
REMARK 3 T TENSOR
REMARK 3 T11: 0.2255 T22: 0.2185
REMARK 3 T33: 0.2270 T12: -0.0106
REMARK 3 T13: 0.0003 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.2944 L22: 0.4354
REMARK 3 L33: 0.6885 L12: -0.1029
REMARK 3 L13: 0.1161 L23: -0.1462
REMARK 3 S TENSOR
REMARK 3 S11: 0.0253 S12: -0.0177 S13: 0.0094
REMARK 3 S21: 0.0431 S22: -0.0058 S23: -0.0286
REMARK 3 S31: -0.1406 S32: 0.0154 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): 81.9946 -13.1153 373.6525
REMARK 3 T TENSOR
REMARK 3 T11: 0.4106 T22: 0.4005
REMARK 3 T33: 0.3706 T12: 0.0201
REMARK 3 T13: -0.0920 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.0869 L22: 0.1334
REMARK 3 L33: 0.0559 L12: -0.0300
REMARK 3 L13: 0.0343 L23: -0.0499
REMARK 3 S TENSOR
REMARK 3 S11: 0.0683 S12: 0.0873 S13: -0.0030
REMARK 3 S21: -0.1132 S22: 0.0339 S23: -0.0177
REMARK 3 S31: 0.0727 S32: 0.0281 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN G
REMARK 3 ORIGIN FOR THE GROUP (A): 153.9418 -50.4694 366.1165
REMARK 3 T TENSOR
REMARK 3 T11: 0.2983 T22: 0.2884
REMARK 3 T33: 0.2962 T12: -0.0112
REMARK 3 T13: -0.0026 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.2483 L22: 0.3377
REMARK 3 L33: 0.7288 L12: -0.0864
REMARK 3 L13: -0.1642 L23: 0.1983
REMARK 3 S TENSOR
REMARK 3 S11: 0.0166 S12: -0.0145 S13: -0.0099
REMARK 3 S21: 0.0698 S22: 0.0019 S23: 0.0202
REMARK 3 S31: 0.1493 S32: -0.0073 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN H
REMARK 3 ORIGIN FOR THE GROUP (A): 149.3366 0.3315 373.6460
REMARK 3 T TENSOR
REMARK 3 T11: 0.4668 T22: 0.4357
REMARK 3 T33: 0.4690 T12: 0.0353
REMARK 3 T13: 0.0971 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.1119 L22: 0.1269
REMARK 3 L33: 0.0346 L12: 0.0119
REMARK 3 L13: -0.0428 L23: 0.0535
REMARK 3 S TENSOR
REMARK 3 S11: 0.1398 S12: 0.0547 S13: 0.0244
REMARK 3 S21: -0.2107 S22: 0.0108 S23: -0.1084
REMARK 3 S31: -0.0259 S32: 0.0117 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6L8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-NOV-19.
REMARK 100 THE DEPOSITION ID IS D_1300011390.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95308
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.097
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.3
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4630
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4KR0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M IMIDAZOLE MALATE, PH 8.5, 7.5%
REMARK 280 (W/V) PEG 10000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 136.83700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 151970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 113.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, I, J, K, L, M, N,
REMARK 350 AND CHAINS: O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, Q, R, S, T, U
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 57.59476
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 100.11382
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, V, W, X, Y
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 -57.06224
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 100.11382
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 ASP A 37
REMARK 465 HIS A 762
REMARK 465 HIS A 763
REMARK 465 HIS A 764
REMARK 465 HIS A 765
REMARK 465 HIS A 766
REMARK 465 HIS A 767
REMARK 465 GLU B 367
REMARK 465 ALA B 368
REMARK 465 LYS B 369
REMARK 465 PRO B 370
REMARK 465 SER B 371
REMARK 465 GLY B 372
REMARK 465 SER B 373
REMARK 465 VAL B 374
REMARK 465 VAL B 375
REMARK 465 GLU B 376
REMARK 465 GLN B 377
REMARK 465 ALA B 378
REMARK 465 GLU B 379
REMARK 465 GLY B 380
REMARK 465 GLU B 589
REMARK 465 PHE B 590
REMARK 465 ALA B 591
REMARK 465 ASN B 592
REMARK 465 ASP B 593
REMARK 465 THR B 594
REMARK 465 LYS B 595
REMARK 465 ILE B 596
REMARK 465 ALA B 597
REMARK 465 SER B 598
REMARK 465 GLN B 599
REMARK 465 LEU B 600
REMARK 465 GLY B 601
REMARK 465 ASN B 602
REMARK 465 CYS B 603
REMARK 465 VAL B 604
REMARK 465 GLU B 605
REMARK 465 TYR B 606
REMARK 465 HIS B 607
REMARK 465 HIS B 608
REMARK 465 HIS B 609
REMARK 465 HIS B 610
REMARK 465 HIS B 611
REMARK 465 HIS B 612
REMARK 465 ASP C 37
REMARK 465 HIS C 762
REMARK 465 HIS C 763
REMARK 465 HIS C 764
REMARK 465 HIS C 765
REMARK 465 HIS C 766
REMARK 465 HIS C 767
REMARK 465 GLU D 367
REMARK 465 ALA D 368
REMARK 465 LYS D 369
REMARK 465 PRO D 370
REMARK 465 SER D 371
REMARK 465 GLY D 372
REMARK 465 SER D 373
REMARK 465 VAL D 374
REMARK 465 VAL D 375
REMARK 465 GLU D 376
REMARK 465 GLN D 377
REMARK 465 ALA D 378
REMARK 465 GLU D 379
REMARK 465 GLY D 380
REMARK 465 GLU D 589
REMARK 465 PHE D 590
REMARK 465 ALA D 591
REMARK 465 ASN D 592
REMARK 465 ASP D 593
REMARK 465 THR D 594
REMARK 465 LYS D 595
REMARK 465 ILE D 596
REMARK 465 ALA D 597
REMARK 465 SER D 598
REMARK 465 GLN D 599
REMARK 465 LEU D 600
REMARK 465 GLY D 601
REMARK 465 ASN D 602
REMARK 465 CYS D 603
REMARK 465 VAL D 604
REMARK 465 GLU D 605
REMARK 465 TYR D 606
REMARK 465 HIS D 607
REMARK 465 HIS D 608
REMARK 465 HIS D 609
REMARK 465 HIS D 610
REMARK 465 HIS D 611
REMARK 465 HIS D 612
REMARK 465 ASP E 37
REMARK 465 HIS E 762
REMARK 465 HIS E 763
REMARK 465 HIS E 764
REMARK 465 HIS E 765
REMARK 465 HIS E 766
REMARK 465 HIS E 767
REMARK 465 GLU F 367
REMARK 465 ALA F 368
REMARK 465 LYS F 369
REMARK 465 PRO F 370
REMARK 465 SER F 371
REMARK 465 GLY F 372
REMARK 465 SER F 373
REMARK 465 VAL F 374
REMARK 465 VAL F 375
REMARK 465 GLU F 376
REMARK 465 GLN F 377
REMARK 465 ALA F 378
REMARK 465 GLU F 379
REMARK 465 GLY F 380
REMARK 465 GLU F 589
REMARK 465 PHE F 590
REMARK 465 ALA F 591
REMARK 465 ASN F 592
REMARK 465 ASP F 593
REMARK 465 THR F 594
REMARK 465 LYS F 595
REMARK 465 ILE F 596
REMARK 465 ALA F 597
REMARK 465 SER F 598
REMARK 465 GLN F 599
REMARK 465 LEU F 600
REMARK 465 GLY F 601
REMARK 465 ASN F 602
REMARK 465 CYS F 603
REMARK 465 VAL F 604
REMARK 465 GLU F 605
REMARK 465 TYR F 606
REMARK 465 HIS F 607
REMARK 465 HIS F 608
REMARK 465 HIS F 609
REMARK 465 HIS F 610
REMARK 465 HIS F 611
REMARK 465 HIS F 612
REMARK 465 ASP G 37
REMARK 465 HIS G 762
REMARK 465 HIS G 763
REMARK 465 HIS G 764
REMARK 465 HIS G 765
REMARK 465 HIS G 766
REMARK 465 HIS G 767
REMARK 465 GLU H 367
REMARK 465 ALA H 368
REMARK 465 LYS H 369
REMARK 465 PRO H 370
REMARK 465 SER H 371
REMARK 465 GLY H 372
REMARK 465 SER H 373
REMARK 465 VAL H 374
REMARK 465 VAL H 375
REMARK 465 GLU H 376
REMARK 465 GLN H 377
REMARK 465 ALA H 378
REMARK 465 GLU H 379
REMARK 465 GLY H 380
REMARK 465 GLU H 589
REMARK 465 PHE H 590
REMARK 465 ALA H 591
REMARK 465 ASN H 592
REMARK 465 ASP H 593
REMARK 465 THR H 594
REMARK 465 LYS H 595
REMARK 465 ILE H 596
REMARK 465 ALA H 597
REMARK 465 SER H 598
REMARK 465 GLN H 599
REMARK 465 LEU H 600
REMARK 465 GLY H 601
REMARK 465 ASN H 602
REMARK 465 CYS H 603
REMARK 465 VAL H 604
REMARK 465 GLU H 605
REMARK 465 TYR H 606
REMARK 465 HIS H 607
REMARK 465 HIS H 608
REMARK 465 HIS H 609
REMARK 465 HIS H 610
REMARK 465 HIS H 611
REMARK 465 HIS H 612
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 86 CG2
REMARK 470 TYR A 177 O
REMARK 470 LYS A 386 NZ
REMARK 470 THR A 751 CG2
REMARK 470 THR C 86 CG2
REMARK 470 TYR C 177 O
REMARK 470 LYS C 386 NZ
REMARK 470 THR C 751 CG2
REMARK 470 THR E 86 CG2
REMARK 470 TYR E 177 O
REMARK 470 LYS E 386 NZ
REMARK 470 THR E 751 CG2
REMARK 470 THR G 86 CG2
REMARK 470 TYR G 177 O
REMARK 470 LYS G 386 NZ
REMARK 470 THR G 751 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 80 OH TYR A 462 1.59
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 SER A 62 -167.31 -161.79
REMARK 500 HIS A 64 13.04 -152.10
REMARK 500 ASN A 72 -2.56 70.31
REMARK 500 GLN A 95 53.59 -94.79
REMARK 500 PHE A 96 -71.09 -115.62
REMARK 500 LYS A 121 -65.40 -100.18
REMARK 500 HIS A 160 26.31 -141.83
REMARK 500 TYR A 177 51.14 -92.27
REMARK 500 HIS A 185 26.13 -141.63
REMARK 500 ALA A 191 -55.70 -120.36
REMARK 500 ILE A 205 -62.05 -121.95
REMARK 500 LEU A 240 -167.12 -69.88
REMARK 500 ASP A 241 150.46 -42.21
REMARK 500 THR A 275 47.65 -92.84
REMARK 500 LYS A 418 19.09 55.23
REMARK 500 ALA A 543 13.64 54.73
REMARK 500 SER A 625 -18.54 72.37
REMARK 500 TYR A 626 -34.10 -136.47
REMARK 500 PRO A 669 46.58 -78.12
REMARK 500 ASN A 674 25.85 -150.17
REMARK 500 MET A 728 118.37 -162.50
REMARK 500 GLU B 382 117.51 -160.84
REMARK 500 SER B 435 19.53 -140.54
REMARK 500 MET B 452 31.18 -95.57
REMARK 500 SER B 460 -33.17 -131.28
REMARK 500 ASN B 582 79.21 -69.62
REMARK 500 SER C 62 -169.06 -163.45
REMARK 500 ASN C 72 -0.05 66.08
REMARK 500 ASN C 83 121.20 -39.52
REMARK 500 GLN C 95 51.51 -91.81
REMARK 500 PHE C 96 -70.92 -117.55
REMARK 500 LYS C 121 -67.90 -94.81
REMARK 500 HIS C 185 35.65 -140.05
REMARK 500 ALA C 191 -55.48 -120.50
REMARK 500 ILE C 205 -59.17 -122.99
REMARK 500 LEU C 240 -170.90 -69.19
REMARK 500 ASP C 241 150.48 -42.94
REMARK 500 GLU C 242 -17.15 -49.16
REMARK 500 LEU C 277 71.67 59.35
REMARK 500 GLU C 278 151.00 -43.18
REMARK 500 LYS C 418 18.02 56.45
REMARK 500 ALA C 543 16.97 54.97
REMARK 500 ALA C 552 33.67 -93.48
REMARK 500 ARG C 591 11.31 58.77
REMARK 500 PRO C 669 46.76 -77.35
REMARK 500 ASN C 674 28.83 -150.34
REMARK 500 MET C 728 110.61 -160.36
REMARK 500 ILE C 737 4.16 -64.82
REMARK 500 ALA C 738 3.07 -60.65
REMARK 500 MET D 452 30.02 -92.19
REMARK 500
REMARK 500 THIS ENTRY HAS 92 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6L8Q A 37 761 UNP L5LQ33 L5LQ33_MYODS 24 748
DBREF1 6L8Q B 367 606 UNP A0A0A0Q7F3_9BETC
DBREF2 6L8Q B A0A0A0Q7F3 367 606
DBREF 6L8Q C 37 761 UNP L5LQ33 L5LQ33_MYODS 24 748
DBREF1 6L8Q D 367 606 UNP A0A0A0Q7F3_9BETC
DBREF2 6L8Q D A0A0A0Q7F3 367 606
DBREF 6L8Q E 37 761 UNP L5LQ33 L5LQ33_MYODS 24 748
DBREF1 6L8Q F 367 606 UNP A0A0A0Q7F3_9BETC
DBREF2 6L8Q F A0A0A0Q7F3 367 606
DBREF 6L8Q G 37 761 UNP L5LQ33 L5LQ33_MYODS 24 748
DBREF1 6L8Q H 367 606 UNP A0A0A0Q7F3_9BETC
DBREF2 6L8Q H A0A0A0Q7F3 367 606
SEQADV 6L8Q HIS A 762 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS A 763 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS A 764 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS A 765 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS A 766 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS A 767 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS B 607 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS B 608 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS B 609 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS B 610 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS B 611 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS B 612 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS C 762 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS C 763 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS C 764 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS C 765 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS C 766 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS C 767 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS D 607 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS D 608 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS D 609 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS D 610 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS D 611 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS D 612 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS E 762 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS E 763 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS E 764 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS E 765 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS E 766 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS E 767 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS F 607 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS F 608 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS F 609 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS F 610 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS F 611 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS F 612 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS G 762 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS G 763 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS G 764 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS G 765 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS G 766 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS G 767 UNP L5LQ33 EXPRESSION TAG
SEQADV 6L8Q HIS H 607 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS H 608 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS H 609 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS H 610 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS H 611 UNP A0A0A0Q7F EXPRESSION TAG
SEQADV 6L8Q HIS H 612 UNP A0A0A0Q7F EXPRESSION TAG
SEQRES 1 A 731 ASP ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS SER
SEQRES 2 A 731 THR ILE ARG MET ARG ASN TYR ASN LEU ARG TRP ILE SER
SEQRES 3 A 731 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN VAL LEU
SEQRES 4 A 731 LEU PHE ASN ALA ASP HIS GLY ASN SER SER THR PHE LEU
SEQRES 5 A 731 GLU ASN SER THR PHE ASP GLN PHE GLY HIS SER ILE SER
SEQRES 6 A 731 ASP TYR SER VAL SER PRO ASP ARG GLN PHE VAL LEU PHE
SEQRES 7 A 731 GLU TYR ASN TYR VAL LYS LYS TRP ARG HIS SER TYR THR
SEQRES 8 A 731 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 731 ILE THR ALA GLU ARG ILE PRO ASN ASP THR GLN LEU ILE
SEQRES 10 A 731 ARG TRP SER PRO GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 731 ASN ASN ASP VAL TYR VAL LYS ASN ASP PRO TYR SER PRO
SEQRES 12 A 731 SER GLN ARG VAL THR HIS ASP GLY ARG GLU ASP ALA ILE
SEQRES 13 A 731 SER ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 A 731 PHE SER THR HIS SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 731 THR PHE LEU ALA TYR ALA LYS PHE ASN ASP THR ASP VAL
SEQRES 16 A 731 PRO ARG ILE GLU TYR SER VAL TYR LEU ASP GLU SER LEU
SEQRES 17 A 731 GLN TYR PRO LYS THR ILE HIS ILE PRO TYR PRO LYS ALA
SEQRES 18 A 731 GLY ALA LYS ASN PRO THR VAL LYS LEU TYR VAL VAL ASN
SEQRES 19 A 731 THR ASP ASN LEU THR ASP LEU GLU PRO ALA GLN ILE VAL
SEQRES 20 A 731 ALA PRO ALA SER VAL LEU THR GLY ASP HIS TYR LEU CYS
SEQRES 21 A 731 ASP VAL THR TRP ALA THR LYS GLU ARG ILE SER LEU GLN
SEQRES 22 A 731 TRP LEU ARG ARG ILE GLN ASN TYR SER ILE ILE ASP ILE
SEQRES 23 A 731 CYS ASP TYR ASN GLU SER THR PRO LYS TRP ASN CYS LEU
SEQRES 24 A 731 VAL SER ARG GLN HIS ILE GLU THR SER ALA THR GLY TRP
SEQRES 25 A 731 VAL GLY ARG PHE LYS PRO ALA GLU PRO HIS PHE THR SER
SEQRES 26 A 731 ASP GLY ASN SER PHE TYR LYS ILE MET SER ASN SER GLU
SEQRES 27 A 731 GLY TYR LYS HIS ILE CYS LEU PHE GLN ILE ASP LYS PRO
SEQRES 28 A 731 ASP CYS THR PHE ILE THR LYS GLY ALA TRP GLU VAL ILE
SEQRES 29 A 731 GLY ILE GLU ALA LEU THR ASN ASP TYR LEU TYR PHE ILE
SEQRES 30 A 731 SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU
SEQRES 31 A 731 TYR LYS ILE GLN LEU ASN ASN TYR ALA ASN VAL THR CYS
SEQRES 32 A 731 LEU SER CYS GLU LEU ASP PRO GLU ARG CYS GLN TYR TYR
SEQRES 33 A 731 SER ALA SER PHE SER LYS GLY ALA LYS TYR TYR GLN LEU
SEQRES 34 A 731 ARG CYS SER GLY PRO GLN ILE PRO ARG TYR SER LEU HIS
SEQRES 35 A 731 SER SER SER ASN ASP LYS GLU LEU ARG LEU LEU GLU ASN
SEQRES 36 A 731 ASN THR ALA LEU TYR GLU THR LEU GLN ASN ILE GLN MET
SEQRES 37 A 731 PRO ARG LYS THR LEU ASP PHE LEU HIS LEU ASN GLY THR
SEQRES 38 A 731 LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP
SEQRES 39 A 731 LYS SER LYS LYS TYR PRO LEU LEU ILE ASP VAL TYR ALA
SEQRES 40 A 731 GLY PRO CYS SER GLN LYS ALA ASP ALA THR PHE LYS LEU
SEQRES 41 A 731 SER TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE
SEQRES 42 A 731 VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY
SEQRES 43 A 731 ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR
SEQRES 44 A 731 PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA LYS GLN PHE
SEQRES 45 A 731 SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE ALA ILE
SEQRES 46 A 731 TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET VAL
SEQRES 47 A 731 LEU GLY ALA GLY SER HIS VAL PHE LYS CYS GLY ILE ALA
SEQRES 48 A 731 VAL ALA PRO VAL SER ALA TRP GLU PHE TYR ASP SER VAL
SEQRES 49 A 731 TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP
SEQRES 50 A 731 ASN LEU ASP HIS TYR LYS ASN SER THR VAL MET SER ARG
SEQRES 51 A 731 ALA GLU ASN PHE LYS LEU VAL GLU TYR LEU LEU ILE HIS
SEQRES 52 A 731 GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA
SEQRES 53 A 731 GLN ILE THR ARG ALA LEU VAL ASP ALA GLY VAL ASP PHE
SEQRES 54 A 731 GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA
SEQRES 55 A 731 THR SER THR ALA HIS GLN HIS ILE TYR THR HIS MET THR
SEQRES 56 A 731 HIS PHE ILE LYS GLN CYS PHE SER LEU PRO HIS HIS HIS
SEQRES 57 A 731 HIS HIS HIS
SEQRES 1 B 246 GLU ALA LYS PRO SER GLY SER VAL VAL GLU GLN ALA GLU
SEQRES 2 B 246 GLY VAL GLU CYS ASP PHE SER PRO LEU LEU SER GLY THR
SEQRES 3 B 246 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR
SEQRES 4 B 246 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 B 246 SER VAL ASN ASP PHE THR CYS SER GLN ILE SER PRO ALA
SEQRES 6 B 246 ALA ILE ALA SER ASN CYS TYR SER SER LEU ILE LEU ASP
SEQRES 7 B 246 TYR PHE SER TYR PRO LEU SER MET LYS SER ASP LEU SER
SEQRES 8 B 246 VAL SER SER ALA GLY PRO ILE SER GLN PHE ASN TYR LYS
SEQRES 9 B 246 GLN SER PHE SER ASN PRO THR CYS LEU ILE LEU ALA THR
SEQRES 10 B 246 VAL PRO HIS ASN LEU THR THR ILE THR LYS PRO LEU LYS
SEQRES 11 B 246 TYR SER TYR ILE ASN LYS CYS SER ARG LEU LEU SER ASP
SEQRES 12 B 246 ASP ARG THR GLU VAL PRO GLN LEU VAL ASN ALA ASN GLN
SEQRES 13 B 246 TYR SER PRO CYS VAL SER ILE VAL PRO SER THR VAL TRP
SEQRES 14 B 246 GLU ASP GLY ASP TYR TYR ARG LYS GLN LEU SER PRO LEU
SEQRES 15 B 246 GLU GLY GLY GLY TRP LEU VAL ALA SER GLY SER THR VAL
SEQRES 16 B 246 ALA MET THR GLU GLN LEU GLN MET GLY PHE GLY ILE THR
SEQRES 17 B 246 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO LYS
SEQRES 18 B 246 LEU GLU PHE ALA ASN ASP THR LYS ILE ALA SER GLN LEU
SEQRES 19 B 246 GLY ASN CYS VAL GLU TYR HIS HIS HIS HIS HIS HIS
SEQRES 1 C 731 ASP ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS SER
SEQRES 2 C 731 THR ILE ARG MET ARG ASN TYR ASN LEU ARG TRP ILE SER
SEQRES 3 C 731 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN VAL LEU
SEQRES 4 C 731 LEU PHE ASN ALA ASP HIS GLY ASN SER SER THR PHE LEU
SEQRES 5 C 731 GLU ASN SER THR PHE ASP GLN PHE GLY HIS SER ILE SER
SEQRES 6 C 731 ASP TYR SER VAL SER PRO ASP ARG GLN PHE VAL LEU PHE
SEQRES 7 C 731 GLU TYR ASN TYR VAL LYS LYS TRP ARG HIS SER TYR THR
SEQRES 8 C 731 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 731 ILE THR ALA GLU ARG ILE PRO ASN ASP THR GLN LEU ILE
SEQRES 10 C 731 ARG TRP SER PRO GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 731 ASN ASN ASP VAL TYR VAL LYS ASN ASP PRO TYR SER PRO
SEQRES 12 C 731 SER GLN ARG VAL THR HIS ASP GLY ARG GLU ASP ALA ILE
SEQRES 13 C 731 SER ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 C 731 PHE SER THR HIS SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 731 THR PHE LEU ALA TYR ALA LYS PHE ASN ASP THR ASP VAL
SEQRES 16 C 731 PRO ARG ILE GLU TYR SER VAL TYR LEU ASP GLU SER LEU
SEQRES 17 C 731 GLN TYR PRO LYS THR ILE HIS ILE PRO TYR PRO LYS ALA
SEQRES 18 C 731 GLY ALA LYS ASN PRO THR VAL LYS LEU TYR VAL VAL ASN
SEQRES 19 C 731 THR ASP ASN LEU THR ASP LEU GLU PRO ALA GLN ILE VAL
SEQRES 20 C 731 ALA PRO ALA SER VAL LEU THR GLY ASP HIS TYR LEU CYS
SEQRES 21 C 731 ASP VAL THR TRP ALA THR LYS GLU ARG ILE SER LEU GLN
SEQRES 22 C 731 TRP LEU ARG ARG ILE GLN ASN TYR SER ILE ILE ASP ILE
SEQRES 23 C 731 CYS ASP TYR ASN GLU SER THR PRO LYS TRP ASN CYS LEU
SEQRES 24 C 731 VAL SER ARG GLN HIS ILE GLU THR SER ALA THR GLY TRP
SEQRES 25 C 731 VAL GLY ARG PHE LYS PRO ALA GLU PRO HIS PHE THR SER
SEQRES 26 C 731 ASP GLY ASN SER PHE TYR LYS ILE MET SER ASN SER GLU
SEQRES 27 C 731 GLY TYR LYS HIS ILE CYS LEU PHE GLN ILE ASP LYS PRO
SEQRES 28 C 731 ASP CYS THR PHE ILE THR LYS GLY ALA TRP GLU VAL ILE
SEQRES 29 C 731 GLY ILE GLU ALA LEU THR ASN ASP TYR LEU TYR PHE ILE
SEQRES 30 C 731 SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU
SEQRES 31 C 731 TYR LYS ILE GLN LEU ASN ASN TYR ALA ASN VAL THR CYS
SEQRES 32 C 731 LEU SER CYS GLU LEU ASP PRO GLU ARG CYS GLN TYR TYR
SEQRES 33 C 731 SER ALA SER PHE SER LYS GLY ALA LYS TYR TYR GLN LEU
SEQRES 34 C 731 ARG CYS SER GLY PRO GLN ILE PRO ARG TYR SER LEU HIS
SEQRES 35 C 731 SER SER SER ASN ASP LYS GLU LEU ARG LEU LEU GLU ASN
SEQRES 36 C 731 ASN THR ALA LEU TYR GLU THR LEU GLN ASN ILE GLN MET
SEQRES 37 C 731 PRO ARG LYS THR LEU ASP PHE LEU HIS LEU ASN GLY THR
SEQRES 38 C 731 LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP
SEQRES 39 C 731 LYS SER LYS LYS TYR PRO LEU LEU ILE ASP VAL TYR ALA
SEQRES 40 C 731 GLY PRO CYS SER GLN LYS ALA ASP ALA THR PHE LYS LEU
SEQRES 41 C 731 SER TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE
SEQRES 42 C 731 VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY
SEQRES 43 C 731 ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR
SEQRES 44 C 731 PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA LYS GLN PHE
SEQRES 45 C 731 SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE ALA ILE
SEQRES 46 C 731 TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET VAL
SEQRES 47 C 731 LEU GLY ALA GLY SER HIS VAL PHE LYS CYS GLY ILE ALA
SEQRES 48 C 731 VAL ALA PRO VAL SER ALA TRP GLU PHE TYR ASP SER VAL
SEQRES 49 C 731 TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP
SEQRES 50 C 731 ASN LEU ASP HIS TYR LYS ASN SER THR VAL MET SER ARG
SEQRES 51 C 731 ALA GLU ASN PHE LYS LEU VAL GLU TYR LEU LEU ILE HIS
SEQRES 52 C 731 GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA
SEQRES 53 C 731 GLN ILE THR ARG ALA LEU VAL ASP ALA GLY VAL ASP PHE
SEQRES 54 C 731 GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA
SEQRES 55 C 731 THR SER THR ALA HIS GLN HIS ILE TYR THR HIS MET THR
SEQRES 56 C 731 HIS PHE ILE LYS GLN CYS PHE SER LEU PRO HIS HIS HIS
SEQRES 57 C 731 HIS HIS HIS
SEQRES 1 D 246 GLU ALA LYS PRO SER GLY SER VAL VAL GLU GLN ALA GLU
SEQRES 2 D 246 GLY VAL GLU CYS ASP PHE SER PRO LEU LEU SER GLY THR
SEQRES 3 D 246 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR
SEQRES 4 D 246 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 D 246 SER VAL ASN ASP PHE THR CYS SER GLN ILE SER PRO ALA
SEQRES 6 D 246 ALA ILE ALA SER ASN CYS TYR SER SER LEU ILE LEU ASP
SEQRES 7 D 246 TYR PHE SER TYR PRO LEU SER MET LYS SER ASP LEU SER
SEQRES 8 D 246 VAL SER SER ALA GLY PRO ILE SER GLN PHE ASN TYR LYS
SEQRES 9 D 246 GLN SER PHE SER ASN PRO THR CYS LEU ILE LEU ALA THR
SEQRES 10 D 246 VAL PRO HIS ASN LEU THR THR ILE THR LYS PRO LEU LYS
SEQRES 11 D 246 TYR SER TYR ILE ASN LYS CYS SER ARG LEU LEU SER ASP
SEQRES 12 D 246 ASP ARG THR GLU VAL PRO GLN LEU VAL ASN ALA ASN GLN
SEQRES 13 D 246 TYR SER PRO CYS VAL SER ILE VAL PRO SER THR VAL TRP
SEQRES 14 D 246 GLU ASP GLY ASP TYR TYR ARG LYS GLN LEU SER PRO LEU
SEQRES 15 D 246 GLU GLY GLY GLY TRP LEU VAL ALA SER GLY SER THR VAL
SEQRES 16 D 246 ALA MET THR GLU GLN LEU GLN MET GLY PHE GLY ILE THR
SEQRES 17 D 246 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO LYS
SEQRES 18 D 246 LEU GLU PHE ALA ASN ASP THR LYS ILE ALA SER GLN LEU
SEQRES 19 D 246 GLY ASN CYS VAL GLU TYR HIS HIS HIS HIS HIS HIS
SEQRES 1 E 731 ASP ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS SER
SEQRES 2 E 731 THR ILE ARG MET ARG ASN TYR ASN LEU ARG TRP ILE SER
SEQRES 3 E 731 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN VAL LEU
SEQRES 4 E 731 LEU PHE ASN ALA ASP HIS GLY ASN SER SER THR PHE LEU
SEQRES 5 E 731 GLU ASN SER THR PHE ASP GLN PHE GLY HIS SER ILE SER
SEQRES 6 E 731 ASP TYR SER VAL SER PRO ASP ARG GLN PHE VAL LEU PHE
SEQRES 7 E 731 GLU TYR ASN TYR VAL LYS LYS TRP ARG HIS SER TYR THR
SEQRES 8 E 731 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 E 731 ILE THR ALA GLU ARG ILE PRO ASN ASP THR GLN LEU ILE
SEQRES 10 E 731 ARG TRP SER PRO GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 E 731 ASN ASN ASP VAL TYR VAL LYS ASN ASP PRO TYR SER PRO
SEQRES 12 E 731 SER GLN ARG VAL THR HIS ASP GLY ARG GLU ASP ALA ILE
SEQRES 13 E 731 SER ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 E 731 PHE SER THR HIS SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 E 731 THR PHE LEU ALA TYR ALA LYS PHE ASN ASP THR ASP VAL
SEQRES 16 E 731 PRO ARG ILE GLU TYR SER VAL TYR LEU ASP GLU SER LEU
SEQRES 17 E 731 GLN TYR PRO LYS THR ILE HIS ILE PRO TYR PRO LYS ALA
SEQRES 18 E 731 GLY ALA LYS ASN PRO THR VAL LYS LEU TYR VAL VAL ASN
SEQRES 19 E 731 THR ASP ASN LEU THR ASP LEU GLU PRO ALA GLN ILE VAL
SEQRES 20 E 731 ALA PRO ALA SER VAL LEU THR GLY ASP HIS TYR LEU CYS
SEQRES 21 E 731 ASP VAL THR TRP ALA THR LYS GLU ARG ILE SER LEU GLN
SEQRES 22 E 731 TRP LEU ARG ARG ILE GLN ASN TYR SER ILE ILE ASP ILE
SEQRES 23 E 731 CYS ASP TYR ASN GLU SER THR PRO LYS TRP ASN CYS LEU
SEQRES 24 E 731 VAL SER ARG GLN HIS ILE GLU THR SER ALA THR GLY TRP
SEQRES 25 E 731 VAL GLY ARG PHE LYS PRO ALA GLU PRO HIS PHE THR SER
SEQRES 26 E 731 ASP GLY ASN SER PHE TYR LYS ILE MET SER ASN SER GLU
SEQRES 27 E 731 GLY TYR LYS HIS ILE CYS LEU PHE GLN ILE ASP LYS PRO
SEQRES 28 E 731 ASP CYS THR PHE ILE THR LYS GLY ALA TRP GLU VAL ILE
SEQRES 29 E 731 GLY ILE GLU ALA LEU THR ASN ASP TYR LEU TYR PHE ILE
SEQRES 30 E 731 SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU
SEQRES 31 E 731 TYR LYS ILE GLN LEU ASN ASN TYR ALA ASN VAL THR CYS
SEQRES 32 E 731 LEU SER CYS GLU LEU ASP PRO GLU ARG CYS GLN TYR TYR
SEQRES 33 E 731 SER ALA SER PHE SER LYS GLY ALA LYS TYR TYR GLN LEU
SEQRES 34 E 731 ARG CYS SER GLY PRO GLN ILE PRO ARG TYR SER LEU HIS
SEQRES 35 E 731 SER SER SER ASN ASP LYS GLU LEU ARG LEU LEU GLU ASN
SEQRES 36 E 731 ASN THR ALA LEU TYR GLU THR LEU GLN ASN ILE GLN MET
SEQRES 37 E 731 PRO ARG LYS THR LEU ASP PHE LEU HIS LEU ASN GLY THR
SEQRES 38 E 731 LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP
SEQRES 39 E 731 LYS SER LYS LYS TYR PRO LEU LEU ILE ASP VAL TYR ALA
SEQRES 40 E 731 GLY PRO CYS SER GLN LYS ALA ASP ALA THR PHE LYS LEU
SEQRES 41 E 731 SER TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE
SEQRES 42 E 731 VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY
SEQRES 43 E 731 ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR
SEQRES 44 E 731 PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA LYS GLN PHE
SEQRES 45 E 731 SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE ALA ILE
SEQRES 46 E 731 TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET VAL
SEQRES 47 E 731 LEU GLY ALA GLY SER HIS VAL PHE LYS CYS GLY ILE ALA
SEQRES 48 E 731 VAL ALA PRO VAL SER ALA TRP GLU PHE TYR ASP SER VAL
SEQRES 49 E 731 TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP
SEQRES 50 E 731 ASN LEU ASP HIS TYR LYS ASN SER THR VAL MET SER ARG
SEQRES 51 E 731 ALA GLU ASN PHE LYS LEU VAL GLU TYR LEU LEU ILE HIS
SEQRES 52 E 731 GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA
SEQRES 53 E 731 GLN ILE THR ARG ALA LEU VAL ASP ALA GLY VAL ASP PHE
SEQRES 54 E 731 GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA
SEQRES 55 E 731 THR SER THR ALA HIS GLN HIS ILE TYR THR HIS MET THR
SEQRES 56 E 731 HIS PHE ILE LYS GLN CYS PHE SER LEU PRO HIS HIS HIS
SEQRES 57 E 731 HIS HIS HIS
SEQRES 1 F 246 GLU ALA LYS PRO SER GLY SER VAL VAL GLU GLN ALA GLU
SEQRES 2 F 246 GLY VAL GLU CYS ASP PHE SER PRO LEU LEU SER GLY THR
SEQRES 3 F 246 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR
SEQRES 4 F 246 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 F 246 SER VAL ASN ASP PHE THR CYS SER GLN ILE SER PRO ALA
SEQRES 6 F 246 ALA ILE ALA SER ASN CYS TYR SER SER LEU ILE LEU ASP
SEQRES 7 F 246 TYR PHE SER TYR PRO LEU SER MET LYS SER ASP LEU SER
SEQRES 8 F 246 VAL SER SER ALA GLY PRO ILE SER GLN PHE ASN TYR LYS
SEQRES 9 F 246 GLN SER PHE SER ASN PRO THR CYS LEU ILE LEU ALA THR
SEQRES 10 F 246 VAL PRO HIS ASN LEU THR THR ILE THR LYS PRO LEU LYS
SEQRES 11 F 246 TYR SER TYR ILE ASN LYS CYS SER ARG LEU LEU SER ASP
SEQRES 12 F 246 ASP ARG THR GLU VAL PRO GLN LEU VAL ASN ALA ASN GLN
SEQRES 13 F 246 TYR SER PRO CYS VAL SER ILE VAL PRO SER THR VAL TRP
SEQRES 14 F 246 GLU ASP GLY ASP TYR TYR ARG LYS GLN LEU SER PRO LEU
SEQRES 15 F 246 GLU GLY GLY GLY TRP LEU VAL ALA SER GLY SER THR VAL
SEQRES 16 F 246 ALA MET THR GLU GLN LEU GLN MET GLY PHE GLY ILE THR
SEQRES 17 F 246 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO LYS
SEQRES 18 F 246 LEU GLU PHE ALA ASN ASP THR LYS ILE ALA SER GLN LEU
SEQRES 19 F 246 GLY ASN CYS VAL GLU TYR HIS HIS HIS HIS HIS HIS
SEQRES 1 G 731 ASP ARG ARG THR TYR THR LEU ALA ASP TYR LEU LYS SER
SEQRES 2 G 731 THR ILE ARG MET ARG ASN TYR ASN LEU ARG TRP ILE SER
SEQRES 3 G 731 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN VAL LEU
SEQRES 4 G 731 LEU PHE ASN ALA ASP HIS GLY ASN SER SER THR PHE LEU
SEQRES 5 G 731 GLU ASN SER THR PHE ASP GLN PHE GLY HIS SER ILE SER
SEQRES 6 G 731 ASP TYR SER VAL SER PRO ASP ARG GLN PHE VAL LEU PHE
SEQRES 7 G 731 GLU TYR ASN TYR VAL LYS LYS TRP ARG HIS SER TYR THR
SEQRES 8 G 731 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 G 731 ILE THR ALA GLU ARG ILE PRO ASN ASP THR GLN LEU ILE
SEQRES 10 G 731 ARG TRP SER PRO GLU GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 G 731 ASN ASN ASP VAL TYR VAL LYS ASN ASP PRO TYR SER PRO
SEQRES 12 G 731 SER GLN ARG VAL THR HIS ASP GLY ARG GLU ASP ALA ILE
SEQRES 13 G 731 SER ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU ILE
SEQRES 14 G 731 PHE SER THR HIS SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 G 731 THR PHE LEU ALA TYR ALA LYS PHE ASN ASP THR ASP VAL
SEQRES 16 G 731 PRO ARG ILE GLU TYR SER VAL TYR LEU ASP GLU SER LEU
SEQRES 17 G 731 GLN TYR PRO LYS THR ILE HIS ILE PRO TYR PRO LYS ALA
SEQRES 18 G 731 GLY ALA LYS ASN PRO THR VAL LYS LEU TYR VAL VAL ASN
SEQRES 19 G 731 THR ASP ASN LEU THR ASP LEU GLU PRO ALA GLN ILE VAL
SEQRES 20 G 731 ALA PRO ALA SER VAL LEU THR GLY ASP HIS TYR LEU CYS
SEQRES 21 G 731 ASP VAL THR TRP ALA THR LYS GLU ARG ILE SER LEU GLN
SEQRES 22 G 731 TRP LEU ARG ARG ILE GLN ASN TYR SER ILE ILE ASP ILE
SEQRES 23 G 731 CYS ASP TYR ASN GLU SER THR PRO LYS TRP ASN CYS LEU
SEQRES 24 G 731 VAL SER ARG GLN HIS ILE GLU THR SER ALA THR GLY TRP
SEQRES 25 G 731 VAL GLY ARG PHE LYS PRO ALA GLU PRO HIS PHE THR SER
SEQRES 26 G 731 ASP GLY ASN SER PHE TYR LYS ILE MET SER ASN SER GLU
SEQRES 27 G 731 GLY TYR LYS HIS ILE CYS LEU PHE GLN ILE ASP LYS PRO
SEQRES 28 G 731 ASP CYS THR PHE ILE THR LYS GLY ALA TRP GLU VAL ILE
SEQRES 29 G 731 GLY ILE GLU ALA LEU THR ASN ASP TYR LEU TYR PHE ILE
SEQRES 30 G 731 SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN LEU
SEQRES 31 G 731 TYR LYS ILE GLN LEU ASN ASN TYR ALA ASN VAL THR CYS
SEQRES 32 G 731 LEU SER CYS GLU LEU ASP PRO GLU ARG CYS GLN TYR TYR
SEQRES 33 G 731 SER ALA SER PHE SER LYS GLY ALA LYS TYR TYR GLN LEU
SEQRES 34 G 731 ARG CYS SER GLY PRO GLN ILE PRO ARG TYR SER LEU HIS
SEQRES 35 G 731 SER SER SER ASN ASP LYS GLU LEU ARG LEU LEU GLU ASN
SEQRES 36 G 731 ASN THR ALA LEU TYR GLU THR LEU GLN ASN ILE GLN MET
SEQRES 37 G 731 PRO ARG LYS THR LEU ASP PHE LEU HIS LEU ASN GLY THR
SEQRES 38 G 731 LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE ASP
SEQRES 39 G 731 LYS SER LYS LYS TYR PRO LEU LEU ILE ASP VAL TYR ALA
SEQRES 40 G 731 GLY PRO CYS SER GLN LYS ALA ASP ALA THR PHE LYS LEU
SEQRES 41 G 731 SER TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE ILE
SEQRES 42 G 731 VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN GLY
SEQRES 43 G 731 ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY THR
SEQRES 44 G 731 PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA LYS GLN PHE
SEQRES 45 G 731 SER LYS MET GLY PHE VAL ASP ASP LYS ARG ILE ALA ILE
SEQRES 46 G 731 TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET VAL
SEQRES 47 G 731 LEU GLY ALA GLY SER HIS VAL PHE LYS CYS GLY ILE ALA
SEQRES 48 G 731 VAL ALA PRO VAL SER ALA TRP GLU PHE TYR ASP SER VAL
SEQRES 49 G 731 TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU ASP
SEQRES 50 G 731 ASN LEU ASP HIS TYR LYS ASN SER THR VAL MET SER ARG
SEQRES 51 G 731 ALA GLU ASN PHE LYS LEU VAL GLU TYR LEU LEU ILE HIS
SEQRES 52 G 731 GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER ALA
SEQRES 53 G 731 GLN ILE THR ARG ALA LEU VAL ASP ALA GLY VAL ASP PHE
SEQRES 54 G 731 GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE ALA
SEQRES 55 G 731 THR SER THR ALA HIS GLN HIS ILE TYR THR HIS MET THR
SEQRES 56 G 731 HIS PHE ILE LYS GLN CYS PHE SER LEU PRO HIS HIS HIS
SEQRES 57 G 731 HIS HIS HIS
SEQRES 1 H 246 GLU ALA LYS PRO SER GLY SER VAL VAL GLU GLN ALA GLU
SEQRES 2 H 246 GLY VAL GLU CYS ASP PHE SER PRO LEU LEU SER GLY THR
SEQRES 3 H 246 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR
SEQRES 4 H 246 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 H 246 SER VAL ASN ASP PHE THR CYS SER GLN ILE SER PRO ALA
SEQRES 6 H 246 ALA ILE ALA SER ASN CYS TYR SER SER LEU ILE LEU ASP
SEQRES 7 H 246 TYR PHE SER TYR PRO LEU SER MET LYS SER ASP LEU SER
SEQRES 8 H 246 VAL SER SER ALA GLY PRO ILE SER GLN PHE ASN TYR LYS
SEQRES 9 H 246 GLN SER PHE SER ASN PRO THR CYS LEU ILE LEU ALA THR
SEQRES 10 H 246 VAL PRO HIS ASN LEU THR THR ILE THR LYS PRO LEU LYS
SEQRES 11 H 246 TYR SER TYR ILE ASN LYS CYS SER ARG LEU LEU SER ASP
SEQRES 12 H 246 ASP ARG THR GLU VAL PRO GLN LEU VAL ASN ALA ASN GLN
SEQRES 13 H 246 TYR SER PRO CYS VAL SER ILE VAL PRO SER THR VAL TRP
SEQRES 14 H 246 GLU ASP GLY ASP TYR TYR ARG LYS GLN LEU SER PRO LEU
SEQRES 15 H 246 GLU GLY GLY GLY TRP LEU VAL ALA SER GLY SER THR VAL
SEQRES 16 H 246 ALA MET THR GLU GLN LEU GLN MET GLY PHE GLY ILE THR
SEQRES 17 H 246 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO LYS
SEQRES 18 H 246 LEU GLU PHE ALA ASN ASP THR LYS ILE ALA SER GLN LEU
SEQRES 19 H 246 GLY ASN CYS VAL GLU TYR HIS HIS HIS HIS HIS HIS
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET NAG N 2 14
HET BMA N 3 11
HET NAG O 1 14
HET NAG O 2 14
HET NAG P 1 14
HET NAG P 2 14
HET NAG Q 1 14
HET NAG Q 2 14
HET NAG R 1 14
HET NAG R 2 14
HET NAG S 1 14
HET NAG S 2 14
HET BMA S 3 11
HET NAG T 1 14
HET NAG T 2 14
HET NAG U 1 14
HET NAG U 2 14
HET NAG V 1 14
HET NAG V 2 14
HET NAG W 1 14
HET NAG W 2 14
HET BMA W 3 11
HET NAG X 1 14
HET NAG X 2 14
HET NAG Y 1 14
HET NAG Y 2 14
HET NAG A 801 14
HET NAG A 809 14
HET NAG B 701 14
HET NAG C 801 14
HET NAG C 809 14
HET NAG D 701 14
HET NAG E 810 14
HET NAG F 701 14
HET NAG G 801 14
HET NAG G 809 14
HET NAG H 701 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
FORMUL 9 NAG 45(C8 H15 N O6)
FORMUL 10 BMA 4(C6 H12 O6)
HELIX 1 AA1 THR A 42 LYS A 48 1 7
HELIX 2 AA2 ASN A 90 GLN A 95 1 6
HELIX 3 AA3 ASP A 198 ILE A 205 1 8
HELIX 4 AA4 PRO A 285 LEU A 289 5 5
HELIX 5 AA5 VAL A 336 GLN A 339 5 4
HELIX 6 AA6 GLU A 416 MET A 420 5 5
HELIX 7 AA7 LYS A 458 ALA A 460 5 3
HELIX 8 AA8 ASN A 492 ASN A 501 1 10
HELIX 9 AA9 SER A 557 GLU A 566 1 10
HELIX 10 AB1 GLY A 582 HIS A 587 1 6
HELIX 11 AB2 ALA A 588 ASN A 590 5 3
HELIX 12 AB3 THR A 595 MET A 611 1 17
HELIX 13 AB4 TYR A 626 GLY A 636 1 11
HELIX 14 AB5 ASP A 658 GLY A 667 1 10
HELIX 15 AB6 ASN A 674 SER A 681 1 8
HELIX 16 AB7 VAL A 683 VAL A 693 5 11
HELIX 17 AB8 HIS A 707 ALA A 721 1 15
HELIX 18 AB9 THR A 739 PHE A 758 1 20
HELIX 19 AC1 PHE B 385 SER B 390 1 6
HELIX 20 AC2 GLN B 395 PHE B 399 5 5
HELIX 21 AC3 ASN B 410 SER B 416 1 7
HELIX 22 AC4 SER B 429 ALA B 434 1 6
HELIX 23 AC5 PRO B 449 SER B 457 5 9
HELIX 24 AC6 GLY B 462 ASN B 468 1 7
HELIX 25 AC7 SER B 524 ILE B 529 5 6
HELIX 26 AC8 THR C 42 LYS C 48 1 7
HELIX 27 AC9 ASN C 90 GLN C 95 1 6
HELIX 28 AD1 ASP C 198 ILE C 205 1 8
HELIX 29 AD2 PRO C 285 LEU C 289 5 5
HELIX 30 AD3 VAL C 336 GLN C 339 5 4
HELIX 31 AD4 GLU C 416 MET C 420 5 5
HELIX 32 AD5 LYS C 458 ALA C 460 5 3
HELIX 33 AD6 ASN C 492 ASN C 501 1 10
HELIX 34 AD7 SER C 557 ASN C 567 1 11
HELIX 35 AD8 GLY C 582 HIS C 587 1 6
HELIX 36 AD9 ALA C 588 ASN C 590 5 3
HELIX 37 AE1 THR C 595 MET C 611 1 17
HELIX 38 AE2 TRP C 624 GLY C 636 1 13
HELIX 39 AE3 ASP C 658 GLY C 667 1 10
HELIX 40 AE4 ASN C 674 SER C 681 1 8
HELIX 41 AE5 THR C 682 VAL C 693 5 12
HELIX 42 AE6 HIS C 707 ALA C 721 1 15
HELIX 43 AE7 THR C 739 SER C 759 1 21
HELIX 44 AE8 PHE D 385 SER D 390 1 6
HELIX 45 AE9 GLN D 395 PHE D 399 5 5
HELIX 46 AF1 ASN D 410 SER D 416 1 7
HELIX 47 AF2 SER D 429 ALA D 434 1 6
HELIX 48 AF3 PRO D 449 SER D 457 5 9
HELIX 49 AF4 SER D 524 ILE D 529 5 6
HELIX 50 AF5 SER D 546 GLY D 550 5 5
HELIX 51 AF6 THR E 42 LYS E 48 1 7
HELIX 52 AF7 ASP E 198 ILE E 205 1 8
HELIX 53 AF8 GLU E 416 MET E 420 5 5
HELIX 54 AF9 LYS E 458 ALA E 460 5 3
HELIX 55 AG1 ASN E 492 ASN E 501 1 10
HELIX 56 AG2 SER E 557 THR E 565 1 9
HELIX 57 AG3 GLY E 582 HIS E 587 1 6
HELIX 58 AG4 ALA E 588 ASN E 590 5 3
HELIX 59 AG5 THR E 595 MET E 611 1 17
HELIX 60 AG6 TYR E 626 GLY E 636 1 11
HELIX 61 AG7 ALA E 653 TYR E 657 5 5
HELIX 62 AG8 ASP E 658 GLY E 667 1 10
HELIX 63 AG9 ASN E 674 SER E 681 1 8
HELIX 64 AH1 VAL E 683 VAL E 693 5 11
HELIX 65 AH2 HIS E 707 ALA E 721 1 15
HELIX 66 AH3 THR E 739 SER E 759 1 21
HELIX 67 AH4 PHE F 385 SER F 390 1 6
HELIX 68 AH5 GLN F 395 PHE F 399 5 5
HELIX 69 AH6 ASN F 410 SER F 416 1 7
HELIX 70 AH7 SER F 429 ALA F 434 1 6
HELIX 71 AH8 PRO F 449 SER F 457 5 9
HELIX 72 AH9 GLY F 462 ASN F 468 1 7
HELIX 73 AI1 SER F 524 SER F 528 5 5
HELIX 74 AI2 SER F 546 GLY F 550 5 5
HELIX 75 AI3 THR G 42 LYS G 48 1 7
HELIX 76 AI4 GLU G 89 GLN G 95 1 7
HELIX 77 AI5 ASP G 198 ILE G 205 1 8
HELIX 78 AI6 PRO G 285 LEU G 289 5 5
HELIX 79 AI7 VAL G 336 GLN G 339 5 4
HELIX 80 AI8 GLU G 416 MET G 420 5 5
HELIX 81 AI9 LYS G 458 ALA G 460 5 3
HELIX 82 AJ1 ASN G 492 ASN G 501 1 10
HELIX 83 AJ2 SER G 557 THR G 565 1 9
HELIX 84 AJ3 GLY G 582 HIS G 587 1 6
HELIX 85 AJ4 ALA G 588 ASN G 590 5 3
HELIX 86 AJ5 THR G 595 LYS G 610 1 16
HELIX 87 AJ6 TYR G 626 GLY G 636 1 11
HELIX 88 AJ7 ALA G 653 TYR G 657 5 5
HELIX 89 AJ8 ASP G 658 GLY G 667 1 10
HELIX 90 AJ9 ASN G 674 SER G 681 1 8
HELIX 91 AK1 VAL G 683 VAL G 693 5 11
HELIX 92 AK2 HIS G 707 ALA G 721 1 15
HELIX 93 AK3 THR G 739 SER G 759 1 21
HELIX 94 AK4 PHE H 385 SER H 390 1 6
HELIX 95 AK5 GLN H 395 PHE H 399 5 5
HELIX 96 AK6 ASN H 410 LEU H 417 1 8
HELIX 97 AK7 SER H 429 ALA H 434 1 6
HELIX 98 AK8 PRO H 449 SER H 457 5 9
HELIX 99 AK9 GLY H 462 ASN H 468 1 7
HELIX 100 AL1 SER H 524 ILE H 529 5 6
HELIX 101 AL2 SER H 546 GLY H 550 5 5
SHEET 1 AA1 2 ARG A 39 THR A 40 0
SHEET 2 AA1 2 ILE A 502 GLN A 503 1 O GLN A 503 N ARG A 39
SHEET 1 AA2 4 ARG A 59 TRP A 60 0
SHEET 2 AA2 4 GLU A 65 GLN A 70 -1 O LEU A 67 N ARG A 59
SHEET 3 AA2 4 ASN A 73 ASN A 78 -1 O ASN A 73 N GLN A 70
SHEET 4 AA2 4 SER A 84 LEU A 88 -1 O SER A 85 N LEU A 76
SHEET 1 AA3 4 ASP A 102 VAL A 105 0
SHEET 2 AA3 4 PHE A 111 LYS A 120 -1 O LEU A 113 N SER A 104
SHEET 3 AA3 4 TYR A 126 ASP A 134 -1 O TYR A 133 N VAL A 112
SHEET 4 AA3 4 GLN A 139 LEU A 140 -1 O GLN A 139 N ASP A 134
SHEET 1 AA4 4 LEU A 152 TRP A 155 0
SHEET 2 AA4 4 LEU A 162 TRP A 166 -1 O ALA A 163 N ARG A 154
SHEET 3 AA4 4 ASP A 169 LYS A 173 -1 O TYR A 171 N TYR A 164
SHEET 4 AA4 4 GLN A 181 ARG A 182 -1 O GLN A 181 N VAL A 172
SHEET 1 AA5 3 ILE A 192 ASN A 194 0
SHEET 2 AA5 3 PHE A 220 ASN A 227 -1 O PHE A 226 N SER A 193
SHEET 3 AA5 3 LEU A 212 TRP A 214 -1 N TRP A 213 O ALA A 222
SHEET 1 AA6 4 ILE A 192 ASN A 194 0
SHEET 2 AA6 4 PHE A 220 ASN A 227 -1 O PHE A 226 N SER A 193
SHEET 3 AA6 4 THR A 263 ASN A 270 -1 O TYR A 267 N TYR A 223
SHEET 4 AA6 4 ALA A 280 ILE A 282 -1 O ILE A 282 N LEU A 266
SHEET 1 AA7 2 ARG A 233 VAL A 238 0
SHEET 2 AA7 2 LYS A 248 PRO A 253 -1 O ILE A 250 N TYR A 236
SHEET 1 AA8 4 HIS A 293 THR A 302 0
SHEET 2 AA8 4 ARG A 305 ARG A 312 -1 O LEU A 311 N TYR A 294
SHEET 3 AA8 4 TYR A 317 ASN A 326 -1 O CYS A 323 N ILE A 306
SHEET 4 AA8 4 LYS A 331 CYS A 334 -1 O ASN A 333 N ASP A 324
SHEET 1 AA9 4 HIS A 293 THR A 302 0
SHEET 2 AA9 4 ARG A 305 ARG A 312 -1 O LEU A 311 N TYR A 294
SHEET 3 AA9 4 TYR A 317 ASN A 326 -1 O CYS A 323 N ILE A 306
SHEET 4 AA9 4 HIS A 340 THR A 343 -1 O GLU A 342 N SER A 318
SHEET 1 AB1 4 HIS A 358 PHE A 359 0
SHEET 2 AB1 4 SER A 365 SER A 371 -1 O TYR A 367 N HIS A 358
SHEET 3 AB1 4 LYS A 377 GLN A 383 -1 O PHE A 382 N PHE A 366
SHEET 4 AB1 4 CYS A 389 PHE A 391 -1 O THR A 390 N LEU A 381
SHEET 1 AB2 4 VAL A 399 LEU A 405 0
SHEET 2 AB2 4 TYR A 409 SER A 414 -1 O ILE A 413 N ILE A 400
SHEET 3 AB2 4 ASN A 425 GLN A 430 -1 O TYR A 427 N PHE A 412
SHEET 4 AB2 4 VAL A 437 CYS A 439 -1 O THR A 438 N LYS A 428
SHEET 1 AB3 4 TYR A 452 PHE A 456 0
SHEET 2 AB3 4 TYR A 462 CYS A 467 -1 O GLN A 464 N SER A 455
SHEET 3 AB3 4 ARG A 474 SER A 479 -1 O SER A 476 N LEU A 465
SHEET 4 AB3 4 GLU A 485 GLU A 490 -1 O LEU A 486 N LEU A 477
SHEET 1 AB4 8 ARG A 506 LEU A 514 0
SHEET 2 AB4 8 THR A 517 LEU A 525 -1 O LEU A 525 N ARG A 506
SHEET 3 AB4 8 ILE A 569 PHE A 573 -1 O VAL A 570 N ILE A 524
SHEET 4 AB4 8 TYR A 535 VAL A 541 1 N ASP A 540 O ALA A 571
SHEET 5 AB4 8 VAL A 614 TRP A 624 1 O ASP A 615 N TYR A 535
SHEET 6 AB4 8 CYS A 644 VAL A 648 1 O ILE A 646 N GLY A 623
SHEET 7 AB4 8 GLU A 694 GLY A 700 1 O ILE A 698 N ALA A 647
SHEET 8 AB4 8 GLN A 726 TYR A 730 1 O GLN A 726 N TYR A 695
SHEET 1 AB5 5 LYS B 400 PHE B 404 0
SHEET 2 AB5 5 SER B 440 SER B 447 -1 O TYR B 445 N LYS B 400
SHEET 3 AB5 5 GLN B 568 GLN B 576 -1 O THR B 574 N ILE B 442
SHEET 4 AB5 5 THR B 477 THR B 483 -1 N ILE B 480 O PHE B 571
SHEET 5 AB5 5 ASP B 422 SER B 426 -1 N SER B 426 O THR B 477
SHEET 1 AB6 2 CYS B 407 TYR B 409 0
SHEET 2 AB6 2 VAL B 584 PRO B 586 1 O CYS B 585 N TYR B 409
SHEET 1 AB7 4 GLU B 513 PRO B 515 0
SHEET 2 AB7 4 LYS B 496 LEU B 506 -1 N ARG B 505 O VAL B 514
SHEET 3 AB7 4 TRP B 553 ALA B 562 -1 O TRP B 553 N LEU B 506
SHEET 4 AB7 4 TYR B 540 GLN B 544 -1 N TYR B 541 O ALA B 556
SHEET 1 AB8 4 ARG C 59 TRP C 60 0
SHEET 2 AB8 4 GLU C 65 GLN C 70 -1 O LEU C 67 N ARG C 59
SHEET 3 AB8 4 ASN C 73 ASN C 78 -1 O LEU C 75 N TYR C 68
SHEET 4 AB8 4 SER C 84 LEU C 88 -1 O SER C 85 N LEU C 76
SHEET 1 AB9 4 ILE C 100 VAL C 105 0
SHEET 2 AB9 4 PHE C 111 LYS C 120 -1 O GLU C 115 N SER C 101
SHEET 3 AB9 4 TYR C 126 ASP C 134 -1 O SER C 129 N TYR C 116
SHEET 4 AB9 4 GLN C 139 LEU C 140 -1 O GLN C 139 N ASP C 134
SHEET 1 AC1 4 LEU C 152 TRP C 155 0
SHEET 2 AC1 4 LEU C 162 TRP C 166 -1 O ALA C 163 N ARG C 154
SHEET 3 AC1 4 ASP C 169 LYS C 173 -1 O TYR C 171 N TYR C 164
SHEET 4 AC1 4 GLN C 181 ARG C 182 -1 O GLN C 181 N VAL C 172
SHEET 1 AC2 3 ILE C 192 ASN C 194 0
SHEET 2 AC2 3 PHE C 220 ASN C 227 -1 O PHE C 226 N SER C 193
SHEET 3 AC2 3 LEU C 212 TRP C 214 -1 N TRP C 213 O ALA C 222
SHEET 1 AC3 4 ILE C 192 ASN C 194 0
SHEET 2 AC3 4 PHE C 220 ASN C 227 -1 O PHE C 226 N SER C 193
SHEET 3 AC3 4 THR C 263 ASN C 270 -1 O TYR C 267 N TYR C 223
SHEET 4 AC3 4 ALA C 280 GLN C 281 -1 O ALA C 280 N VAL C 268
SHEET 1 AC4 2 ARG C 233 VAL C 238 0
SHEET 2 AC4 2 LYS C 248 PRO C 253 -1 O ILE C 250 N TYR C 236
SHEET 1 AC5 4 HIS C 293 THR C 302 0
SHEET 2 AC5 4 ARG C 305 ARG C 312 -1 O LEU C 311 N TYR C 294
SHEET 3 AC5 4 TYR C 317 ASN C 326 -1 O CYS C 323 N ILE C 306
SHEET 4 AC5 4 LYS C 331 CYS C 334 -1 O LYS C 331 N ASN C 326
SHEET 1 AC6 4 HIS C 293 THR C 302 0
SHEET 2 AC6 4 ARG C 305 ARG C 312 -1 O LEU C 311 N TYR C 294
SHEET 3 AC6 4 TYR C 317 ASN C 326 -1 O CYS C 323 N ILE C 306
SHEET 4 AC6 4 HIS C 340 THR C 343 -1 O GLU C 342 N SER C 318
SHEET 1 AC7 4 HIS C 358 PHE C 359 0
SHEET 2 AC7 4 SER C 365 SER C 371 -1 O TYR C 367 N HIS C 358
SHEET 3 AC7 4 LYS C 377 GLN C 383 -1 O HIS C 378 N MET C 370
SHEET 4 AC7 4 THR C 390 PHE C 391 -1 O THR C 390 N LEU C 381
SHEET 1 AC8 4 VAL C 399 LEU C 405 0
SHEET 2 AC8 4 TYR C 409 SER C 414 -1 O ILE C 413 N ILE C 400
SHEET 3 AC8 4 ASN C 425 GLN C 430 -1 O TYR C 427 N PHE C 412
SHEET 4 AC8 4 VAL C 437 CYS C 439 -1 O THR C 438 N LYS C 428
SHEET 1 AC9 4 TYR C 452 PHE C 456 0
SHEET 2 AC9 4 TYR C 462 CYS C 467 -1 O ARG C 466 N SER C 453
SHEET 3 AC9 4 ARG C 474 SER C 479 -1 O ARG C 474 N CYS C 467
SHEET 4 AC9 4 GLU C 485 GLU C 490 -1 O LEU C 486 N LEU C 477
SHEET 1 AD1 8 ARG C 506 LEU C 514 0
SHEET 2 AD1 8 THR C 517 LEU C 525 -1 O LEU C 525 N ARG C 506
SHEET 3 AD1 8 ILE C 569 ASP C 574 -1 O VAL C 570 N ILE C 524
SHEET 4 AD1 8 TYR C 535 VAL C 541 1 N ASP C 540 O ALA C 571
SHEET 5 AD1 8 VAL C 614 GLY C 623 1 O ASP C 615 N TYR C 535
SHEET 6 AD1 8 CYS C 644 VAL C 648 1 O VAL C 648 N GLY C 623
SHEET 7 AD1 8 GLU C 694 GLY C 700 1 O LEU C 696 N ALA C 647
SHEET 8 AD1 8 GLN C 726 TYR C 730 1 O GLN C 726 N TYR C 695
SHEET 1 AD2 5 LYS D 400 PHE D 404 0
SHEET 2 AD2 5 SER D 440 SER D 447 -1 O LEU D 441 N PHE D 404
SHEET 3 AD2 5 GLN D 568 GLN D 576 -1 O GLY D 572 N ASP D 444
SHEET 4 AD2 5 THR D 477 THR D 483 -1 N ILE D 480 O PHE D 571
SHEET 5 AD2 5 ASP D 422 SER D 426 -1 N SER D 426 O THR D 477
SHEET 1 AD3 2 CYS D 407 TYR D 409 0
SHEET 2 AD3 2 VAL D 584 PRO D 586 1 O CYS D 585 N TYR D 409
SHEET 1 AD4 4 GLU D 513 PRO D 515 0
SHEET 2 AD4 4 LYS D 496 LEU D 506 -1 N ARG D 505 O VAL D 514
SHEET 3 AD4 4 TRP D 553 ALA D 562 -1 O TRP D 553 N LEU D 506
SHEET 4 AD4 4 TYR D 540 GLN D 544 -1 N TYR D 541 O ALA D 556
SHEET 1 AD5 4 LEU E 58 TRP E 60 0
SHEET 2 AD5 4 GLU E 65 GLN E 70 -1 O LEU E 67 N ARG E 59
SHEET 3 AD5 4 ASN E 73 ASN E 78 -1 O ASN E 73 N GLN E 70
SHEET 4 AD5 4 SER E 84 LEU E 88 -1 O SER E 85 N LEU E 76
SHEET 1 AD6 4 ASP E 102 VAL E 105 0
SHEET 2 AD6 4 PHE E 111 LYS E 120 -1 O LEU E 113 N SER E 104
SHEET 3 AD6 4 TYR E 126 ASP E 134 -1 O SER E 129 N TYR E 116
SHEET 4 AD6 4 GLN E 139 LEU E 140 -1 O GLN E 139 N ASP E 134
SHEET 1 AD7 4 LEU E 152 TRP E 155 0
SHEET 2 AD7 4 LEU E 162 TRP E 166 -1 O ALA E 163 N ARG E 154
SHEET 3 AD7 4 ASP E 169 LYS E 173 -1 O LYS E 173 N LEU E 162
SHEET 4 AD7 4 GLN E 181 ARG E 182 -1 O GLN E 181 N VAL E 172
SHEET 1 AD8 3 ILE E 192 ASN E 194 0
SHEET 2 AD8 3 PHE E 220 ASN E 227 -1 O PHE E 226 N SER E 193
SHEET 3 AD8 3 LEU E 212 TRP E 214 -1 N TRP E 213 O ALA E 222
SHEET 1 AD9 4 ILE E 192 ASN E 194 0
SHEET 2 AD9 4 PHE E 220 ASN E 227 -1 O PHE E 226 N SER E 193
SHEET 3 AD9 4 THR E 263 ASN E 270 -1 O TYR E 267 N TYR E 223
SHEET 4 AD9 4 ALA E 280 ILE E 282 -1 O ILE E 282 N LEU E 266
SHEET 1 AE1 2 ARG E 233 VAL E 238 0
SHEET 2 AE1 2 LYS E 248 PRO E 253 -1 O ILE E 250 N TYR E 236
SHEET 1 AE2 4 HIS E 293 THR E 302 0
SHEET 2 AE2 4 ARG E 305 ARG E 312 -1 O LEU E 311 N TYR E 294
SHEET 3 AE2 4 TYR E 317 TYR E 325 -1 O CYS E 323 N ILE E 306
SHEET 4 AE2 4 TRP E 332 THR E 343 -1 O HIS E 340 N ILE E 320
SHEET 1 AE3 4 HIS E 358 PHE E 359 0
SHEET 2 AE3 4 SER E 365 SER E 371 -1 O TYR E 367 N HIS E 358
SHEET 3 AE3 4 LYS E 377 GLN E 383 -1 O PHE E 382 N PHE E 366
SHEET 4 AE3 4 CYS E 389 PHE E 391 -1 O THR E 390 N LEU E 381
SHEET 1 AE4 4 VAL E 399 LEU E 405 0
SHEET 2 AE4 4 TYR E 409 SER E 414 -1 O ILE E 413 N ILE E 400
SHEET 3 AE4 4 ASN E 425 GLN E 430 -1 O TYR E 427 N PHE E 412
SHEET 4 AE4 4 VAL E 437 CYS E 439 -1 O THR E 438 N LYS E 428
SHEET 1 AE5 4 TYR E 452 PHE E 456 0
SHEET 2 AE5 4 TYR E 462 CYS E 467 -1 O ARG E 466 N SER E 453
SHEET 3 AE5 4 ARG E 474 SER E 479 -1 O SER E 476 N LEU E 465
SHEET 4 AE5 4 GLU E 485 GLU E 490 -1 O GLU E 490 N TYR E 475
SHEET 1 AE6 8 ARG E 506 LEU E 514 0
SHEET 2 AE6 8 THR E 517 LEU E 525 -1 O LEU E 525 N ARG E 506
SHEET 3 AE6 8 ILE E 569 ASP E 574 -1 O VAL E 570 N ILE E 524
SHEET 4 AE6 8 TYR E 535 VAL E 541 1 N LEU E 538 O ILE E 569
SHEET 5 AE6 8 VAL E 614 TRP E 624 1 O ALA E 620 N LEU E 537
SHEET 6 AE6 8 CYS E 644 VAL E 648 1 O ILE E 646 N ILE E 621
SHEET 7 AE6 8 GLU E 694 GLY E 700 1 O LEU E 696 N ALA E 647
SHEET 8 AE6 8 GLN E 726 TYR E 730 1 O GLN E 726 N TYR E 695
SHEET 1 AE7 5 LYS F 400 PHE F 404 0
SHEET 2 AE7 5 SER F 440 SER F 447 -1 O LEU F 443 N LEU F 402
SHEET 3 AE7 5 GLN F 568 GLN F 576 -1 O GLY F 572 N ASP F 444
SHEET 4 AE7 5 THR F 477 THR F 483 -1 N ILE F 480 O PHE F 571
SHEET 5 AE7 5 SER F 419 SER F 426 -1 N THR F 424 O LEU F 479
SHEET 1 AE8 2 ASN F 408 TYR F 409 0
SHEET 2 AE8 2 CYS F 585 PRO F 586 1 O CYS F 585 N TYR F 409
SHEET 1 AE9 4 GLU F 513 PRO F 515 0
SHEET 2 AE9 4 TYR F 497 LEU F 506 -1 N ARG F 505 O VAL F 514
SHEET 3 AE9 4 TRP F 553 VAL F 561 -1 O TRP F 553 N LEU F 506
SHEET 4 AE9 4 TYR F 540 GLN F 544 -1 N TYR F 541 O ALA F 556
SHEET 1 AF1 4 ARG G 59 TRP G 60 0
SHEET 2 AF1 4 GLU G 65 GLN G 70 -1 O LEU G 67 N ARG G 59
SHEET 3 AF1 4 ASN G 73 ASN G 78 -1 O LEU G 75 N TYR G 68
SHEET 4 AF1 4 SER G 84 LEU G 88 -1 O SER G 85 N LEU G 76
SHEET 1 AF2 4 ASP G 102 VAL G 105 0
SHEET 2 AF2 4 PHE G 111 LYS G 120 -1 O GLU G 115 N ASP G 102
SHEET 3 AF2 4 TYR G 126 ASP G 134 -1 O SER G 129 N TYR G 116
SHEET 4 AF2 4 GLN G 139 LEU G 140 -1 O GLN G 139 N ASP G 134
SHEET 1 AF3 4 LEU G 152 TRP G 155 0
SHEET 2 AF3 4 LEU G 162 TRP G 166 -1 O ALA G 163 N ARG G 154
SHEET 3 AF3 4 ASP G 169 LYS G 173 -1 O LYS G 173 N LEU G 162
SHEET 4 AF3 4 GLN G 181 ARG G 182 -1 O GLN G 181 N VAL G 172
SHEET 1 AF4 3 ILE G 192 ASN G 194 0
SHEET 2 AF4 3 PHE G 220 ASN G 227 -1 O PHE G 226 N SER G 193
SHEET 3 AF4 3 LEU G 212 TRP G 214 -1 N TRP G 213 O ALA G 222
SHEET 1 AF5 4 ILE G 192 ASN G 194 0
SHEET 2 AF5 4 PHE G 220 ASN G 227 -1 O PHE G 226 N SER G 193
SHEET 3 AF5 4 THR G 263 ASN G 270 -1 O TYR G 267 N TYR G 223
SHEET 4 AF5 4 ALA G 280 ILE G 282 -1 O ILE G 282 N LEU G 266
SHEET 1 AF6 2 ARG G 233 VAL G 238 0
SHEET 2 AF6 2 LYS G 248 PRO G 253 -1 O LYS G 248 N VAL G 238
SHEET 1 AF7 4 HIS G 293 THR G 302 0
SHEET 2 AF7 4 ARG G 305 ARG G 312 -1 O LEU G 311 N TYR G 294
SHEET 3 AF7 4 TYR G 317 TYR G 325 -1 O ILE G 319 N TRP G 310
SHEET 4 AF7 4 TRP G 332 CYS G 334 -1 O ASN G 333 N ASP G 324
SHEET 1 AF8 4 HIS G 293 THR G 302 0
SHEET 2 AF8 4 ARG G 305 ARG G 312 -1 O LEU G 311 N TYR G 294
SHEET 3 AF8 4 TYR G 317 TYR G 325 -1 O ILE G 319 N TRP G 310
SHEET 4 AF8 4 HIS G 340 THR G 343 -1 O GLU G 342 N SER G 318
SHEET 1 AF9 4 HIS G 358 PHE G 359 0
SHEET 2 AF9 4 SER G 365 SER G 371 -1 O TYR G 367 N HIS G 358
SHEET 3 AF9 4 LYS G 377 GLN G 383 -1 O CYS G 380 N LYS G 368
SHEET 4 AF9 4 CYS G 389 PHE G 391 -1 O THR G 390 N LEU G 381
SHEET 1 AG1 4 VAL G 399 LEU G 405 0
SHEET 2 AG1 4 TYR G 409 SER G 414 -1 O ILE G 413 N ILE G 400
SHEET 3 AG1 4 ASN G 425 GLN G 430 -1 O TYR G 427 N PHE G 412
SHEET 4 AG1 4 VAL G 437 CYS G 439 -1 O THR G 438 N LYS G 428
SHEET 1 AG2 4 TYR G 452 PHE G 456 0
SHEET 2 AG2 4 TYR G 462 CYS G 467 -1 O ARG G 466 N SER G 453
SHEET 3 AG2 4 ARG G 474 SER G 479 -1 O SER G 476 N LEU G 465
SHEET 4 AG2 4 GLU G 485 GLU G 490 -1 O LEU G 486 N LEU G 477
SHEET 1 AG3 8 ARG G 506 LEU G 514 0
SHEET 2 AG3 8 THR G 517 LEU G 525 -1 O LEU G 525 N ARG G 506
SHEET 3 AG3 8 ILE G 569 PHE G 573 -1 O VAL G 570 N ILE G 524
SHEET 4 AG3 8 TYR G 535 VAL G 541 1 N LEU G 538 O ILE G 569
SHEET 5 AG3 8 VAL G 614 TRP G 624 1 O ALA G 620 N ILE G 539
SHEET 6 AG3 8 CYS G 644 VAL G 648 1 O ILE G 646 N ILE G 621
SHEET 7 AG3 8 GLU G 694 GLY G 700 1 O LEU G 696 N ALA G 647
SHEET 8 AG3 8 GLN G 726 TYR G 730 1 O GLN G 726 N LEU G 697
SHEET 1 AG4 5 LYS H 400 PHE H 404 0
SHEET 2 AG4 5 SER H 440 SER H 447 -1 O LEU H 441 N PHE H 404
SHEET 3 AG4 5 GLN H 568 GLN H 576 -1 O GLY H 572 N ASP H 444
SHEET 4 AG4 5 THR H 477 THR H 483 -1 N ILE H 480 O PHE H 571
SHEET 5 AG4 5 SER H 419 SER H 426 -1 N SER H 426 O THR H 477
SHEET 1 AG5 2 ASN H 408 TYR H 409 0
SHEET 2 AG5 2 CYS H 585 PRO H 586 1 O CYS H 585 N TYR H 409
SHEET 1 AG6 4 GLU H 513 PRO H 515 0
SHEET 2 AG6 4 TYR H 497 LEU H 506 -1 N ARG H 505 O VAL H 514
SHEET 3 AG6 4 TRP H 553 VAL H 561 -1 O VAL H 555 N SER H 504
SHEET 4 AG6 4 TYR H 540 GLN H 544 -1 N TYR H 541 O ALA H 556
SSBOND 1 CYS A 323 CYS A 334 1555 1555 2.03
SSBOND 2 CYS A 380 CYS A 389 1555 1555 2.03
SSBOND 3 CYS A 439 CYS A 442 1555 1555 2.03
SSBOND 4 CYS A 449 CYS A 467 1555 1555 2.03
SSBOND 5 CYS A 644 CYS A 757 1555 1555 2.03
SSBOND 6 CYS B 383 CYS B 407 1555 1555 2.03
SSBOND 7 CYS B 425 CYS B 478 1555 1555 2.03
SSBOND 8 CYS B 437 CYS B 585 1555 1555 2.03
SSBOND 9 CYS B 503 CYS B 526 1555 1555 2.03
SSBOND 10 CYS C 323 CYS C 334 1555 1555 2.03
SSBOND 11 CYS C 380 CYS C 389 1555 1555 2.03
SSBOND 12 CYS C 439 CYS C 442 1555 1555 2.03
SSBOND 13 CYS C 449 CYS C 467 1555 1555 2.03
SSBOND 14 CYS C 644 CYS C 757 1555 1555 2.03
SSBOND 15 CYS D 383 CYS D 407 1555 1555 2.04
SSBOND 16 CYS D 425 CYS D 478 1555 1555 2.03
SSBOND 17 CYS D 437 CYS D 585 1555 1555 2.03
SSBOND 18 CYS D 503 CYS D 526 1555 1555 2.03
SSBOND 19 CYS E 323 CYS E 334 1555 1555 2.03
SSBOND 20 CYS E 380 CYS E 389 1555 1555 2.03
SSBOND 21 CYS E 439 CYS E 442 1555 1555 2.03
SSBOND 22 CYS E 449 CYS E 467 1555 1555 2.03
SSBOND 23 CYS E 644 CYS E 757 1555 1555 2.03
SSBOND 24 CYS F 383 CYS F 407 1555 1555 2.04
SSBOND 25 CYS F 425 CYS F 478 1555 1555 2.03
SSBOND 26 CYS F 437 CYS F 585 1555 1555 2.03
SSBOND 27 CYS F 503 CYS F 526 1555 1555 2.03
SSBOND 28 CYS G 323 CYS G 334 1555 1555 2.04
SSBOND 29 CYS G 380 CYS G 389 1555 1555 2.03
SSBOND 30 CYS G 439 CYS G 442 1555 1555 2.03
SSBOND 31 CYS G 449 CYS G 467 1555 1555 1.99
SSBOND 32 CYS G 644 CYS G 757 1555 1555 2.03
SSBOND 33 CYS H 383 CYS H 407 1555 1555 2.03
SSBOND 34 CYS H 425 CYS H 478 1555 1555 2.03
SSBOND 35 CYS H 437 CYS H 585 1555 1555 2.03
SSBOND 36 CYS H 503 CYS H 526 1555 1555 2.03
LINK ND2 ASN A 83 C1 NAG A 801 1555 1555 1.44
LINK ND2 ASN A 90 C1 NAG A 809 1555 1555 1.44
LINK ND2 ASN A 217 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN A 227 C1 NAG J 1 1555 1555 1.43
LINK ND2 ASN A 316 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN A 491 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN B 410 C1 NAG B 701 1555 1555 1.44
LINK ND2 ASN C 83 C1 NAG C 801 1555 1555 1.44
LINK ND2 ASN C 90 C1 NAG C 809 1555 1555 1.44
LINK ND2 ASN C 217 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN C 227 C1 NAG N 1 1555 1555 1.43
LINK ND2 ASN C 316 C1 NAG O 1 1555 1555 1.44
LINK ND2 ASN C 491 C1 NAG P 1 1555 1555 1.44
LINK ND2 ASN D 410 C1 NAG D 701 1555 1555 1.44
LINK ND2 ASN E 83 C1 NAG Q 1 1555 1555 1.44
LINK ND2 ASN E 90 C1 NAG E 810 1555 1555 1.44
LINK ND2 ASN E 217 C1 NAG R 1 1555 1555 1.44
LINK ND2 ASN E 227 C1 NAG S 1 1555 1555 1.43
LINK ND2 ASN E 316 C1 NAG T 1 1555 1555 1.43
LINK ND2 ASN E 491 C1 NAG U 1 1555 1555 1.43
LINK ND2 ASN F 410 C1 NAG F 701 1555 1555 1.44
LINK ND2 ASN G 83 C1 NAG G 801 1555 1555 1.43
LINK ND2 ASN G 90 C1 NAG G 809 1555 1555 1.44
LINK ND2 ASN G 217 C1 NAG V 1 1555 1555 1.44
LINK ND2 ASN G 227 C1 NAG W 1 1555 1555 1.43
LINK ND2 ASN G 316 C1 NAG X 1 1555 1555 1.43
LINK ND2 ASN G 491 C1 NAG Y 1 1555 1555 1.46
LINK ND2 ASN H 410 C1 NAG H 701 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.46
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45
LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.47
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44
LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44
LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45
LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.47
LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44
LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44
LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44
LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45
LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.47
LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44
LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44
CISPEP 1 THR A 329 PRO A 330 0 -10.19
CISPEP 2 GLY A 469 PRO A 470 0 0.61
CISPEP 3 THR C 329 PRO C 330 0 -10.43
CISPEP 4 GLY C 469 PRO C 470 0 -0.53
CISPEP 5 THR E 329 PRO E 330 0 4.27
CISPEP 6 GLY E 469 PRO E 470 0 0.39
CISPEP 7 THR G 329 PRO G 330 0 0.47
CISPEP 8 GLY G 469 PRO G 470 0 1.92
CRYST1 114.657 273.674 115.234 90.00 119.68 90.00 P 1 21 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 0.008722 0.000000 0.004971 0.00000
SCALE2 0.000000 0.003654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009989 0.00000
TER 5907 PRO A 761
TER 7516 LEU B 588
TER 13423 PRO C 761
TER 15032 LEU D 588
TER 20939 PRO E 761
TER 22548 LEU F 588
TER 28455 PRO G 761
TER 30064 LEU H 588
MASTER 640 0 49 101 238 0 0 630730 8 774 304
END |