HEADER TRANSFERASE 06-DEC-18 6IWQ
TITLE CRYSTAL STRUCTURE OF GALNAC-T7 WITH MN2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYLGALACTOSAMINYLTRANSFERASE 7;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: POLYPEPTIDE GALNAC TRANSFERASE 7,PP-GANTASE 7,PROTEIN-UDP
COMPND 5 ACETYLGALACTOSAMINYLTRANSFERASE 7,UDP-GALNAC:POLYPEPTIDE N-
COMPND 6 ACETYLGALACTOSAMINYLTRANSFERASE 7;
COMPND 7 EC: 2.4.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GALNT7;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS POLYPEPTIDE N ACETYLGALACTOSAMINYLTRANSFERASE ACTIVITY, TRANSFERRING
KEYWDS 2 GLYCOSYL GROUPS, MANGANESE ION BINDING, CARBOHYDRATE BINDING, METAL
KEYWDS 3 ION BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.YU,Y.X.YIN
REVDAT 2 20-FEB-19 6IWQ 1 JRNL
REVDAT 1 06-FEB-19 6IWQ 0
JRNL AUTH C.YU,L.LIANG,Y.YIN
JRNL TITL STRUCTURAL BASIS OF CARBOHYDRATE TRANSFER ACTIVITY OF
JRNL TITL 2 UDP-GALNAC: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 7.
JRNL REF BIOCHEM. BIOPHYS. RES. V. 510 266 2019
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 30685086
JRNL DOI 10.1016/J.BBRC.2019.01.084
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2400: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 103299
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5175
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 49.2750 - 9.1475 0.99 3892 213 0.2058 0.1963
REMARK 3 2 9.1475 - 7.2681 1.00 3773 207 0.1890 0.1983
REMARK 3 3 7.2681 - 6.3516 1.00 3745 201 0.2155 0.2501
REMARK 3 4 6.3516 - 5.7718 1.00 3767 171 0.2253 0.2422
REMARK 3 5 5.7718 - 5.3586 1.00 3708 197 0.2125 0.2209
REMARK 3 6 5.3586 - 5.0430 1.00 3700 190 0.1949 0.2019
REMARK 3 7 5.0430 - 4.7907 1.00 3701 195 0.1830 0.1808
REMARK 3 8 4.7907 - 4.5823 1.00 3655 227 0.1785 0.1881
REMARK 3 9 4.5823 - 4.4060 1.00 3717 152 0.1771 0.1955
REMARK 3 10 4.4060 - 4.2541 1.00 3685 201 0.1827 0.2119
REMARK 3 11 4.2541 - 4.1211 1.00 3677 201 0.2016 0.1860
REMARK 3 12 4.1211 - 4.0034 1.00 3638 220 0.2044 0.2133
REMARK 3 13 4.0034 - 3.8980 1.00 3663 187 0.2112 0.2324
REMARK 3 14 3.8980 - 3.8030 1.00 3662 201 0.2328 0.2387
REMARK 3 15 3.8030 - 3.7165 1.00 3605 215 0.2266 0.2464
REMARK 3 16 3.7165 - 3.6375 0.99 3616 194 0.2481 0.2859
REMARK 3 17 3.6375 - 3.5647 0.98 3616 161 0.2545 0.2931
REMARK 3 18 3.5647 - 3.4975 0.94 3414 198 0.2637 0.2874
REMARK 3 19 3.4975 - 3.4350 0.89 3256 163 0.2915 0.2960
REMARK 3 20 3.4350 - 3.3768 0.86 3106 184 0.2896 0.2758
REMARK 3 21 3.3768 - 3.3224 0.82 3026 156 0.2800 0.3253
REMARK 3 22 3.3224 - 3.2713 0.80 2913 151 0.2793 0.3478
REMARK 3 23 3.2713 - 3.2232 0.77 2797 154 0.2931 0.3428
REMARK 3 24 3.2232 - 3.1778 0.75 2758 120 0.2965 0.3279
REMARK 3 25 3.1778 - 3.1348 0.73 2645 137 0.3032 0.3245
REMARK 3 26 3.1348 - 3.0941 0.70 2578 128 0.3119 0.3528
REMARK 3 27 3.0941 - 3.0555 0.68 2470 126 0.3183 0.3273
REMARK 3 28 3.0555 - 3.0186 0.66 2407 116 0.3167 0.3057
REMARK 3 29 3.0186 - 2.9836 0.62 2247 120 0.3326 0.3343
REMARK 3 30 2.9836 - 2.9500 0.46 1687 89 0.3425 0.4284
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.023 27444
REMARK 3 ANGLE : 2.002 37212
REMARK 3 CHIRALITY : 0.104 3822
REMARK 3 PLANARITY : 0.010 4800
REMARK 3 DIHEDRAL : 26.867 10254
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6IWQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1300009913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103346
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 49.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
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 <I/SIGMA(I)> 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M LITHIUM SULFATE MONOHYDRATE,
REMARK 280 12%(W/V) POLYETHYLENE GLYCOL 4,000, 0.1M SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE PH 5.6, 5MM UDP, 5MM MNCL2, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 68.84750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 125.93500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.11650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 125.93500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.84750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 79.11650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 137.69500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 79.11650
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -125.93500
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 PRO A 61
REMARK 465 GLY A 62
REMARK 465 GLU A 63
REMARK 465 ASP A 64
REMARK 465 ARG A 65
REMARK 465 PHE A 66
REMARK 465 LYS A 67
REMARK 465 PRO A 68
REMARK 465 VAL A 69
REMARK 465 VAL A 70
REMARK 465 PRO A 71
REMARK 465 TRP A 72
REMARK 465 PRO A 73
REMARK 465 HIS A 74
REMARK 465 VAL A 75
REMARK 465 GLU A 76
REMARK 465 GLY A 77
REMARK 465 VAL A 78
REMARK 465 GLU A 79
REMARK 465 VAL A 80
REMARK 465 ASP A 81
REMARK 465 LEU A 82
REMARK 465 GLU A 83
REMARK 465 SER A 84
REMARK 465 ILE A 85
REMARK 465 ARG A 86
REMARK 465 ARG A 87
REMARK 465 ILE A 88
REMARK 465 ASN A 89
REMARK 465 LYS A 90
REMARK 465 ALA A 91
REMARK 465 LYS A 92
REMARK 465 ASN A 93
REMARK 465 GLU A 94
REMARK 465 GLN A 95
REMARK 465 GLU A 96
REMARK 465 HIS A 97
REMARK 465 HIS A 98
REMARK 465 ALA A 99
REMARK 465 GLY A 100
REMARK 465 GLY A 101
REMARK 465 ASP A 102
REMARK 465 SER A 103
REMARK 465 GLN A 104
REMARK 465 LYS A 105
REMARK 465 ASP A 106
REMARK 465 ILE A 107
REMARK 465 MET A 108
REMARK 465 GLN A 109
REMARK 465 ARG A 110
REMARK 465 GLN A 111
REMARK 465 PRO B 61
REMARK 465 GLY B 62
REMARK 465 GLU B 63
REMARK 465 ASP B 64
REMARK 465 ARG B 65
REMARK 465 PHE B 66
REMARK 465 LYS B 67
REMARK 465 PRO B 68
REMARK 465 VAL B 69
REMARK 465 VAL B 70
REMARK 465 PRO B 71
REMARK 465 TRP B 72
REMARK 465 PRO B 73
REMARK 465 HIS B 74
REMARK 465 VAL B 75
REMARK 465 GLU B 76
REMARK 465 GLY B 77
REMARK 465 VAL B 78
REMARK 465 GLU B 79
REMARK 465 VAL B 80
REMARK 465 ASP B 81
REMARK 465 LEU B 82
REMARK 465 GLU B 83
REMARK 465 SER B 84
REMARK 465 ILE B 85
REMARK 465 ARG B 86
REMARK 465 ARG B 87
REMARK 465 ILE B 88
REMARK 465 ASN B 89
REMARK 465 LYS B 90
REMARK 465 ALA B 91
REMARK 465 LYS B 92
REMARK 465 ASN B 93
REMARK 465 GLU B 94
REMARK 465 GLN B 95
REMARK 465 GLU B 96
REMARK 465 HIS B 97
REMARK 465 HIS B 98
REMARK 465 ALA B 99
REMARK 465 GLY B 100
REMARK 465 GLY B 101
REMARK 465 ASP B 102
REMARK 465 SER B 103
REMARK 465 GLN B 104
REMARK 465 LYS B 105
REMARK 465 ASP B 106
REMARK 465 ILE B 107
REMARK 465 MET B 108
REMARK 465 GLN B 109
REMARK 465 ARG B 110
REMARK 465 GLN B 111
REMARK 465 PRO C 61
REMARK 465 GLY C 62
REMARK 465 GLU C 63
REMARK 465 ASP C 64
REMARK 465 ARG C 65
REMARK 465 PHE C 66
REMARK 465 LYS C 67
REMARK 465 PRO C 68
REMARK 465 VAL C 69
REMARK 465 VAL C 70
REMARK 465 PRO C 71
REMARK 465 TRP C 72
REMARK 465 PRO C 73
REMARK 465 HIS C 74
REMARK 465 VAL C 75
REMARK 465 GLU C 76
REMARK 465 GLY C 77
REMARK 465 VAL C 78
REMARK 465 GLU C 79
REMARK 465 VAL C 80
REMARK 465 ASP C 81
REMARK 465 LEU C 82
REMARK 465 GLU C 83
REMARK 465 SER C 84
REMARK 465 ILE C 85
REMARK 465 ARG C 86
REMARK 465 ARG C 87
REMARK 465 ILE C 88
REMARK 465 ASN C 89
REMARK 465 LYS C 90
REMARK 465 ALA C 91
REMARK 465 LYS C 92
REMARK 465 ASN C 93
REMARK 465 GLU C 94
REMARK 465 GLN C 95
REMARK 465 GLU C 96
REMARK 465 HIS C 97
REMARK 465 HIS C 98
REMARK 465 ALA C 99
REMARK 465 GLY C 100
REMARK 465 GLY C 101
REMARK 465 ASP C 102
REMARK 465 SER C 103
REMARK 465 GLN C 104
REMARK 465 LYS C 105
REMARK 465 ASP C 106
REMARK 465 ILE C 107
REMARK 465 MET C 108
REMARK 465 GLN C 109
REMARK 465 ARG C 110
REMARK 465 GLN C 111
REMARK 465 PRO D 61
REMARK 465 GLY D 62
REMARK 465 GLU D 63
REMARK 465 ASP D 64
REMARK 465 ARG D 65
REMARK 465 PHE D 66
REMARK 465 LYS D 67
REMARK 465 PRO D 68
REMARK 465 VAL D 69
REMARK 465 VAL D 70
REMARK 465 PRO D 71
REMARK 465 TRP D 72
REMARK 465 PRO D 73
REMARK 465 HIS D 74
REMARK 465 VAL D 75
REMARK 465 GLU D 76
REMARK 465 GLY D 77
REMARK 465 VAL D 78
REMARK 465 GLU D 79
REMARK 465 VAL D 80
REMARK 465 ASP D 81
REMARK 465 LEU D 82
REMARK 465 GLU D 83
REMARK 465 SER D 84
REMARK 465 ILE D 85
REMARK 465 ARG D 86
REMARK 465 ARG D 87
REMARK 465 ILE D 88
REMARK 465 ASN D 89
REMARK 465 LYS D 90
REMARK 465 ALA D 91
REMARK 465 LYS D 92
REMARK 465 ASN D 93
REMARK 465 GLU D 94
REMARK 465 GLN D 95
REMARK 465 GLU D 96
REMARK 465 HIS D 97
REMARK 465 HIS D 98
REMARK 465 ALA D 99
REMARK 465 GLY D 100
REMARK 465 GLY D 101
REMARK 465 ASP D 102
REMARK 465 SER D 103
REMARK 465 GLN D 104
REMARK 465 LYS D 105
REMARK 465 ASP D 106
REMARK 465 ILE D 107
REMARK 465 MET D 108
REMARK 465 GLN D 109
REMARK 465 ARG D 110
REMARK 465 GLN D 111
REMARK 465 PRO E 61
REMARK 465 GLY E 62
REMARK 465 GLU E 63
REMARK 465 ASP E 64
REMARK 465 ARG E 65
REMARK 465 PHE E 66
REMARK 465 LYS E 67
REMARK 465 PRO E 68
REMARK 465 VAL E 69
REMARK 465 VAL E 70
REMARK 465 PRO E 71
REMARK 465 TRP E 72
REMARK 465 PRO E 73
REMARK 465 HIS E 74
REMARK 465 VAL E 75
REMARK 465 GLU E 76
REMARK 465 GLY E 77
REMARK 465 VAL E 78
REMARK 465 GLU E 79
REMARK 465 VAL E 80
REMARK 465 ASP E 81
REMARK 465 LEU E 82
REMARK 465 GLU E 83
REMARK 465 SER E 84
REMARK 465 ILE E 85
REMARK 465 ARG E 86
REMARK 465 ARG E 87
REMARK 465 ILE E 88
REMARK 465 ASN E 89
REMARK 465 LYS E 90
REMARK 465 ALA E 91
REMARK 465 LYS E 92
REMARK 465 ASN E 93
REMARK 465 GLU E 94
REMARK 465 GLN E 95
REMARK 465 GLU E 96
REMARK 465 HIS E 97
REMARK 465 HIS E 98
REMARK 465 ALA E 99
REMARK 465 GLY E 100
REMARK 465 GLY E 101
REMARK 465 ASP E 102
REMARK 465 SER E 103
REMARK 465 GLN E 104
REMARK 465 LYS E 105
REMARK 465 ASP E 106
REMARK 465 ILE E 107
REMARK 465 MET E 108
REMARK 465 GLN E 109
REMARK 465 ARG E 110
REMARK 465 GLN E 111
REMARK 465 PRO F 61
REMARK 465 GLY F 62
REMARK 465 GLU F 63
REMARK 465 ASP F 64
REMARK 465 ARG F 65
REMARK 465 PHE F 66
REMARK 465 LYS F 67
REMARK 465 PRO F 68
REMARK 465 VAL F 69
REMARK 465 VAL F 70
REMARK 465 PRO F 71
REMARK 465 TRP F 72
REMARK 465 PRO F 73
REMARK 465 HIS F 74
REMARK 465 VAL F 75
REMARK 465 GLU F 76
REMARK 465 GLY F 77
REMARK 465 VAL F 78
REMARK 465 GLU F 79
REMARK 465 VAL F 80
REMARK 465 ASP F 81
REMARK 465 LEU F 82
REMARK 465 GLU F 83
REMARK 465 SER F 84
REMARK 465 ILE F 85
REMARK 465 ARG F 86
REMARK 465 ARG F 87
REMARK 465 ILE F 88
REMARK 465 ASN F 89
REMARK 465 LYS F 90
REMARK 465 ALA F 91
REMARK 465 LYS F 92
REMARK 465 ASN F 93
REMARK 465 GLU F 94
REMARK 465 GLN F 95
REMARK 465 GLU F 96
REMARK 465 HIS F 97
REMARK 465 HIS F 98
REMARK 465 ALA F 99
REMARK 465 GLY F 100
REMARK 465 GLY F 101
REMARK 465 ASP F 102
REMARK 465 SER F 103
REMARK 465 GLN F 104
REMARK 465 LYS F 105
REMARK 465 ASP F 106
REMARK 465 ILE F 107
REMARK 465 MET F 108
REMARK 465 GLN F 109
REMARK 465 ARG F 110
REMARK 465 GLN F 111
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 SG CYS D 545 SG CYS D 562 1.09
REMARK 500 SG CYS D 625 SG CYS D 640 1.11
REMARK 500 SG CYS F 585 SG CYS F 600 1.14
REMARK 500 SG CYS F 197 SG CYS F 435 1.21
REMARK 500 SG CYS F 545 SG CYS F 562 1.44
REMARK 500 SG CYS A 197 SG CYS A 435 1.50
REMARK 500 SG CYS E 426 SG CYS E 507 1.66
REMARK 500 SG CYS A 426 SG CYS A 507 1.69
REMARK 500 SG CYS E 197 SG CYS E 435 1.74
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 137 CD PRO A 137 N 0.132
REMARK 500 VAL A 212 CB VAL A 212 CG2 -0.155
REMARK 500 VAL B 212 CB VAL B 212 CG2 -0.154
REMARK 500 VAL C 212 CB VAL C 212 CG2 -0.154
REMARK 500 PRO E 137 CD PRO E 137 N 0.116
REMARK 500 VAL E 212 CB VAL E 212 CG2 -0.155
REMARK 500 VAL F 212 CB VAL F 212 CG2 -0.155
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 137 CA - N - CD ANGL. DEV. = -8.7 DEGREES
REMARK 500 PRO A 149 C - N - CD ANGL. DEV. = 18.8 DEGREES
REMARK 500 PRO A 453 C - N - CD ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO A 485 C - N - CD ANGL. DEV. = 13.2 DEGREES
REMARK 500 MET A 514 CG - SD - CE ANGL. DEV. = -9.8 DEGREES
REMARK 500 PRO A 528 C - N - CD ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO A 529 C - N - CD ANGL. DEV. = 12.6 DEGREES
REMARK 500 PRO B 149 C - N - CD ANGL. DEV. = 17.6 DEGREES
REMARK 500 PRO B 452 C - N - CD ANGL. DEV. = 13.2 DEGREES
REMARK 500 PRO B 453 C - N - CD ANGL. DEV. = 12.8 DEGREES
REMARK 500 PRO B 460 C - N - CD ANGL. DEV. = 17.3 DEGREES
REMARK 500 PRO B 485 C - N - CD ANGL. DEV. = 13.2 DEGREES
REMARK 500 PRO B 491 C - N - CD ANGL. DEV. = -16.2 DEGREES
REMARK 500 MET B 514 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 PRO B 528 C - N - CD ANGL. DEV. = 12.7 DEGREES
REMARK 500 GLY B 554 N - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 GLY C 133 N - CA - C ANGL. DEV. = -21.9 DEGREES
REMARK 500 PRO C 460 C - N - CD ANGL. DEV. = 13.4 DEGREES
REMARK 500 PRO C 485 C - N - CD ANGL. DEV. = 13.2 DEGREES
REMARK 500 MET C 514 CG - SD - CE ANGL. DEV. = -9.8 DEGREES
REMARK 500 PRO C 528 C - N - CD ANGL. DEV. = 12.7 DEGREES
REMARK 500 LEU C 586 CA - CB - CG ANGL. DEV. = 17.7 DEGREES
REMARK 500 PRO D 117 C - N - CD ANGL. DEV. = -13.2 DEGREES
REMARK 500 PRO D 160 C - N - CD ANGL. DEV. = 18.7 DEGREES
REMARK 500 PRO D 452 C - N - CD ANGL. DEV. = 13.2 DEGREES
REMARK 500 MET D 514 CG - SD - CE ANGL. DEV. = -9.8 DEGREES
REMARK 500 PRO D 528 C - N - CD ANGL. DEV. = 12.7 DEGREES
REMARK 500 CYS D 600 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 PRO E 137 CA - N - CD ANGL. DEV. = -8.5 DEGREES
REMARK 500 PRO E 526 C - N - CD ANGL. DEV. = 13.2 DEGREES
REMARK 500 PRO E 529 C - N - CD ANGL. DEV. = 12.8 DEGREES
REMARK 500 LEU E 586 CA - CB - CG ANGL. DEV. = 17.7 DEGREES
REMARK 500 PRO F 451 C - N - CD ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO F 485 C - N - CD ANGL. DEV. = 13.2 DEGREES
REMARK 500 MET F 514 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 LEU F 586 CA - CB - CG ANGL. DEV. = 17.6 DEGREES
REMARK 500 CYS F 600 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 158 -161.91 -107.28
REMARK 500 ASN A 176 84.37 -67.33
REMARK 500 GLU A 204 2.97 84.96
REMARK 500 GLU A 256 -58.71 73.39
REMARK 500 ALA A 355 -154.69 -137.03
REMARK 500 TRP A 356 146.13 -177.36
REMARK 500 LEU A 404 -132.53 57.66
REMARK 500 ASP A 406 115.13 -34.76
REMARK 500 GLU A 415 -58.60 75.87
REMARK 500 GLN A 448 75.07 -157.16
REMARK 500 ASP A 474 -134.39 60.81
REMARK 500 PRO A 491 83.41 -65.32
REMARK 500 TYR A 582 -122.36 49.00
REMARK 500 GLN A 647 0.65 83.90
REMARK 500 LEU B 158 -161.92 -110.49
REMARK 500 GLU B 204 -2.51 83.48
REMARK 500 ILE B 231 -55.75 75.46
REMARK 500 GLU B 256 -59.02 73.56
REMARK 500 TRP B 265 3.98 82.72
REMARK 500 ALA B 355 -154.69 -137.05
REMARK 500 TRP B 356 146.12 -177.40
REMARK 500 PRO B 381 150.53 -43.74
REMARK 500 LEU B 404 -135.20 61.67
REMARK 500 ASP B 406 115.15 -34.67
REMARK 500 ASP B 474 -131.18 60.88
REMARK 500 MET B 549 15.66 57.12
REMARK 500 TYR B 582 -129.03 55.91
REMARK 500 GLU B 604 -129.28 59.35
REMARK 500 LEU C 158 -164.46 -121.28
REMARK 500 GLU C 204 2.89 86.96
REMARK 500 GLU C 256 -58.76 73.38
REMARK 500 TRP C 265 0.36 86.56
REMARK 500 ALA C 355 -154.74 -137.07
REMARK 500 TRP C 356 146.14 -177.38
REMARK 500 LEU C 404 -132.47 57.60
REMARK 500 ASP C 406 115.14 -34.77
REMARK 500 ASP C 474 -131.52 61.48
REMARK 500 PRO C 491 83.39 -65.29
REMARK 500 TYR C 582 -122.30 48.94
REMARK 500 GLN C 647 15.27 80.49
REMARK 500 GLU D 204 -9.74 -57.43
REMARK 500 GLU D 256 -56.24 73.58
REMARK 500 TRP D 265 -0.21 85.57
REMARK 500 ARG D 277 74.54 60.74
REMARK 500 ASP D 347 -126.51 53.00
REMARK 500 ALA D 355 -154.74 -137.01
REMARK 500 TRP D 356 146.13 -177.36
REMARK 500 LEU D 404 -132.51 57.57
REMARK 500 ASP D 406 115.17 -34.74
REMARK 500 ASP D 474 -128.45 62.00
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN B 553 GLY B 554 -34.11
REMARK 500 THR B 645 THR B 646 -43.67
REMARK 500 GLY C 346 ASP C 347 -141.21
REMARK 500 GLU C 348 ASP C 349 44.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E 701 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 301 OD2
REMARK 620 2 HIS E 303 NE2 71.1
REMARK 620 3 HIS E 440 NE2 59.1 71.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN F 701 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 301 OD2
REMARK 620 2 HIS F 303 NE2 64.3
REMARK 620 3 HIS F 440 NE2 54.2 69.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN E 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN F 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6IWR RELATED DB: PDB
REMARK 900 6IWR CONTAINS THE SAME PROTEIN COMPLEXED WITH UDP-GALNAC
DBREF 6IWQ A 61 657 UNP Q86SF2 GALT7_HUMAN 61 657
DBREF 6IWQ B 61 657 UNP Q86SF2 GALT7_HUMAN 61 657
DBREF 6IWQ C 61 657 UNP Q86SF2 GALT7_HUMAN 61 657
DBREF 6IWQ D 61 657 UNP Q86SF2 GALT7_HUMAN 61 657
DBREF 6IWQ E 61 657 UNP Q86SF2 GALT7_HUMAN 61 657
DBREF 6IWQ F 61 657 UNP Q86SF2 GALT7_HUMAN 61 657
SEQRES 1 A 597 PRO GLY GLU ASP ARG PHE LYS PRO VAL VAL PRO TRP PRO
SEQRES 2 A 597 HIS VAL GLU GLY VAL GLU VAL ASP LEU GLU SER ILE ARG
SEQRES 3 A 597 ARG ILE ASN LYS ALA LYS ASN GLU GLN GLU HIS HIS ALA
SEQRES 4 A 597 GLY GLY ASP SER GLN LYS ASP ILE MET GLN ARG GLN TYR
SEQRES 5 A 597 LEU THR PHE LYS PRO GLN THR PHE THR TYR HIS ASP PRO
SEQRES 6 A 597 VAL LEU ARG PRO GLY ILE LEU GLY ASN PHE GLU PRO LYS
SEQRES 7 A 597 GLU PRO GLU PRO PRO GLY VAL VAL GLY GLY PRO GLY GLU
SEQRES 8 A 597 LYS ALA LYS PRO LEU VAL LEU GLY PRO GLU PHE LYS GLN
SEQRES 9 A 597 ALA ILE GLN ALA SER ILE LYS GLU PHE GLY PHE ASN MET
SEQRES 10 A 597 VAL ALA SER ASP MET ILE SER LEU ASP ARG SER VAL ASN
SEQRES 11 A 597 ASP LEU ARG GLN GLU GLU CYS LYS TYR TRP HIS TYR ASP
SEQRES 12 A 597 GLU ASN LEU LEU THR SER SER VAL VAL ILE VAL PHE HIS
SEQRES 13 A 597 ASN GLU GLY TRP SER THR LEU MET ARG THR VAL HIS SER
SEQRES 14 A 597 VAL ILE LYS ARG THR PRO ARG LYS TYR LEU ALA GLU ILE
SEQRES 15 A 597 VAL LEU ILE ASP ASP PHE SER ASN LYS GLU HIS LEU LYS
SEQRES 16 A 597 GLU LYS LEU ASP GLU TYR ILE LYS LEU TRP ASN GLY LEU
SEQRES 17 A 597 VAL LYS VAL PHE ARG ASN GLU ARG ARG GLU GLY LEU ILE
SEQRES 18 A 597 GLN ALA ARG SER ILE GLY ALA GLN LYS ALA LYS LEU GLY
SEQRES 19 A 597 GLN VAL LEU ILE TYR LEU ASP ALA HIS CYS GLU VAL ALA
SEQRES 20 A 597 VAL ASN TRP TYR ALA PRO LEU VAL ALA PRO ILE SER LYS
SEQRES 21 A 597 ASP ARG THR ILE CYS THR VAL PRO LEU ILE ASP VAL ILE
SEQRES 22 A 597 ASN GLY ASN THR TYR GLU ILE ILE PRO GLN GLY GLY GLY
SEQRES 23 A 597 ASP GLU ASP GLY TYR ALA ARG GLY ALA TRP ASP TRP SER
SEQRES 24 A 597 MET LEU TRP LYS ARG VAL PRO LEU THR PRO GLN GLU LYS
SEQRES 25 A 597 ARG LEU ARG LYS THR LYS THR GLU PRO TYR ARG SER PRO
SEQRES 26 A 597 ALA MET ALA GLY GLY LEU PHE ALA ILE GLU ARG GLU PHE
SEQRES 27 A 597 PHE PHE GLU LEU GLY LEU TYR ASP PRO GLY LEU GLN ILE
SEQRES 28 A 597 TRP GLY GLY GLU ASN PHE GLU ILE SER TYR LYS ILE TRP
SEQRES 29 A 597 GLN CYS GLY GLY LYS LEU LEU PHE VAL PRO CYS SER ARG
SEQRES 30 A 597 VAL GLY HIS ILE TYR ARG LEU GLU GLY TRP GLN GLY ASN
SEQRES 31 A 597 PRO PRO PRO ILE TYR VAL GLY SER SER PRO THR LEU LYS
SEQRES 32 A 597 ASN TYR VAL ARG VAL VAL GLU VAL TRP TRP ASP GLU TYR
SEQRES 33 A 597 LYS ASP TYR PHE TYR ALA SER ARG PRO GLU SER GLN ALA
SEQRES 34 A 597 LEU PRO TYR GLY ASP ILE SER GLU LEU LYS LYS PHE ARG
SEQRES 35 A 597 GLU ASP HIS ASN CYS LYS SER PHE LYS TRP PHE MET GLU
SEQRES 36 A 597 GLU ILE ALA TYR ASP ILE THR SER HIS TYR PRO LEU PRO
SEQRES 37 A 597 PRO LYS ASN VAL ASP TRP GLY GLU ILE ARG GLY PHE GLU
SEQRES 38 A 597 THR ALA TYR CYS ILE ASP SER MET GLY LYS THR ASN GLY
SEQRES 39 A 597 GLY PHE VAL GLU LEU GLY PRO CYS HIS ARG MET GLY GLY
SEQRES 40 A 597 ASN GLN LEU PHE ARG ILE ASN GLU ALA ASN GLN LEU MET
SEQRES 41 A 597 GLN TYR ASP GLN CYS LEU THR LYS GLY ALA ASP GLY SER
SEQRES 42 A 597 LYS VAL MET ILE THR HIS CYS ASN LEU ASN GLU PHE LYS
SEQRES 43 A 597 GLU TRP GLN TYR PHE LYS ASN LEU HIS ARG PHE THR HIS
SEQRES 44 A 597 ILE PRO SER GLY LYS CYS LEU ASP ARG SER GLU VAL LEU
SEQRES 45 A 597 HIS GLN VAL PHE ILE SER ASN CYS ASP SER SER LYS THR
SEQRES 46 A 597 THR GLN LYS TRP GLU MET ASN ASN ILE HIS SER VAL
SEQRES 1 B 597 PRO GLY GLU ASP ARG PHE LYS PRO VAL VAL PRO TRP PRO
SEQRES 2 B 597 HIS VAL GLU GLY VAL GLU VAL ASP LEU GLU SER ILE ARG
SEQRES 3 B 597 ARG ILE ASN LYS ALA LYS ASN GLU GLN GLU HIS HIS ALA
SEQRES 4 B 597 GLY GLY ASP SER GLN LYS ASP ILE MET GLN ARG GLN TYR
SEQRES 5 B 597 LEU THR PHE LYS PRO GLN THR PHE THR TYR HIS ASP PRO
SEQRES 6 B 597 VAL LEU ARG PRO GLY ILE LEU GLY ASN PHE GLU PRO LYS
SEQRES 7 B 597 GLU PRO GLU PRO PRO GLY VAL VAL GLY GLY PRO GLY GLU
SEQRES 8 B 597 LYS ALA LYS PRO LEU VAL LEU GLY PRO GLU PHE LYS GLN
SEQRES 9 B 597 ALA ILE GLN ALA SER ILE LYS GLU PHE GLY PHE ASN MET
SEQRES 10 B 597 VAL ALA SER ASP MET ILE SER LEU ASP ARG SER VAL ASN
SEQRES 11 B 597 ASP LEU ARG GLN GLU GLU CYS LYS TYR TRP HIS TYR ASP
SEQRES 12 B 597 GLU ASN LEU LEU THR SER SER VAL VAL ILE VAL PHE HIS
SEQRES 13 B 597 ASN GLU GLY TRP SER THR LEU MET ARG THR VAL HIS SER
SEQRES 14 B 597 VAL ILE LYS ARG THR PRO ARG LYS TYR LEU ALA GLU ILE
SEQRES 15 B 597 VAL LEU ILE ASP ASP PHE SER ASN LYS GLU HIS LEU LYS
SEQRES 16 B 597 GLU LYS LEU ASP GLU TYR ILE LYS LEU TRP ASN GLY LEU
SEQRES 17 B 597 VAL LYS VAL PHE ARG ASN GLU ARG ARG GLU GLY LEU ILE
SEQRES 18 B 597 GLN ALA ARG SER ILE GLY ALA GLN LYS ALA LYS LEU GLY
SEQRES 19 B 597 GLN VAL LEU ILE TYR LEU ASP ALA HIS CYS GLU VAL ALA
SEQRES 20 B 597 VAL ASN TRP TYR ALA PRO LEU VAL ALA PRO ILE SER LYS
SEQRES 21 B 597 ASP ARG THR ILE CYS THR VAL PRO LEU ILE ASP VAL ILE
SEQRES 22 B 597 ASN GLY ASN THR TYR GLU ILE ILE PRO GLN GLY GLY GLY
SEQRES 23 B 597 ASP GLU ASP GLY TYR ALA ARG GLY ALA TRP ASP TRP SER
SEQRES 24 B 597 MET LEU TRP LYS ARG VAL PRO LEU THR PRO GLN GLU LYS
SEQRES 25 B 597 ARG LEU ARG LYS THR LYS THR GLU PRO TYR ARG SER PRO
SEQRES 26 B 597 ALA MET ALA GLY GLY LEU PHE ALA ILE GLU ARG GLU PHE
SEQRES 27 B 597 PHE PHE GLU LEU GLY LEU TYR ASP PRO GLY LEU GLN ILE
SEQRES 28 B 597 TRP GLY GLY GLU ASN PHE GLU ILE SER TYR LYS ILE TRP
SEQRES 29 B 597 GLN CYS GLY GLY LYS LEU LEU PHE VAL PRO CYS SER ARG
SEQRES 30 B 597 VAL GLY HIS ILE TYR ARG LEU GLU GLY TRP GLN GLY ASN
SEQRES 31 B 597 PRO PRO PRO ILE TYR VAL GLY SER SER PRO THR LEU LYS
SEQRES 32 B 597 ASN TYR VAL ARG VAL VAL GLU VAL TRP TRP ASP GLU TYR
SEQRES 33 B 597 LYS ASP TYR PHE TYR ALA SER ARG PRO GLU SER GLN ALA
SEQRES 34 B 597 LEU PRO TYR GLY ASP ILE SER GLU LEU LYS LYS PHE ARG
SEQRES 35 B 597 GLU ASP HIS ASN CYS LYS SER PHE LYS TRP PHE MET GLU
SEQRES 36 B 597 GLU ILE ALA TYR ASP ILE THR SER HIS TYR PRO LEU PRO
SEQRES 37 B 597 PRO LYS ASN VAL ASP TRP GLY GLU ILE ARG GLY PHE GLU
SEQRES 38 B 597 THR ALA TYR CYS ILE ASP SER MET GLY LYS THR ASN GLY
SEQRES 39 B 597 GLY PHE VAL GLU LEU GLY PRO CYS HIS ARG MET GLY GLY
SEQRES 40 B 597 ASN GLN LEU PHE ARG ILE ASN GLU ALA ASN GLN LEU MET
SEQRES 41 B 597 GLN TYR ASP GLN CYS LEU THR LYS GLY ALA ASP GLY SER
SEQRES 42 B 597 LYS VAL MET ILE THR HIS CYS ASN LEU ASN GLU PHE LYS
SEQRES 43 B 597 GLU TRP GLN TYR PHE LYS ASN LEU HIS ARG PHE THR HIS
SEQRES 44 B 597 ILE PRO SER GLY LYS CYS LEU ASP ARG SER GLU VAL LEU
SEQRES 45 B 597 HIS GLN VAL PHE ILE SER ASN CYS ASP SER SER LYS THR
SEQRES 46 B 597 THR GLN LYS TRP GLU MET ASN ASN ILE HIS SER VAL
SEQRES 1 C 597 PRO GLY GLU ASP ARG PHE LYS PRO VAL VAL PRO TRP PRO
SEQRES 2 C 597 HIS VAL GLU GLY VAL GLU VAL ASP LEU GLU SER ILE ARG
SEQRES 3 C 597 ARG ILE ASN LYS ALA LYS ASN GLU GLN GLU HIS HIS ALA
SEQRES 4 C 597 GLY GLY ASP SER GLN LYS ASP ILE MET GLN ARG GLN TYR
SEQRES 5 C 597 LEU THR PHE LYS PRO GLN THR PHE THR TYR HIS ASP PRO
SEQRES 6 C 597 VAL LEU ARG PRO GLY ILE LEU GLY ASN PHE GLU PRO LYS
SEQRES 7 C 597 GLU PRO GLU PRO PRO GLY VAL VAL GLY GLY PRO GLY GLU
SEQRES 8 C 597 LYS ALA LYS PRO LEU VAL LEU GLY PRO GLU PHE LYS GLN
SEQRES 9 C 597 ALA ILE GLN ALA SER ILE LYS GLU PHE GLY PHE ASN MET
SEQRES 10 C 597 VAL ALA SER ASP MET ILE SER LEU ASP ARG SER VAL ASN
SEQRES 11 C 597 ASP LEU ARG GLN GLU GLU CYS LYS TYR TRP HIS TYR ASP
SEQRES 12 C 597 GLU ASN LEU LEU THR SER SER VAL VAL ILE VAL PHE HIS
SEQRES 13 C 597 ASN GLU GLY TRP SER THR LEU MET ARG THR VAL HIS SER
SEQRES 14 C 597 VAL ILE LYS ARG THR PRO ARG LYS TYR LEU ALA GLU ILE
SEQRES 15 C 597 VAL LEU ILE ASP ASP PHE SER ASN LYS GLU HIS LEU LYS
SEQRES 16 C 597 GLU LYS LEU ASP GLU TYR ILE LYS LEU TRP ASN GLY LEU
SEQRES 17 C 597 VAL LYS VAL PHE ARG ASN GLU ARG ARG GLU GLY LEU ILE
SEQRES 18 C 597 GLN ALA ARG SER ILE GLY ALA GLN LYS ALA LYS LEU GLY
SEQRES 19 C 597 GLN VAL LEU ILE TYR LEU ASP ALA HIS CYS GLU VAL ALA
SEQRES 20 C 597 VAL ASN TRP TYR ALA PRO LEU VAL ALA PRO ILE SER LYS
SEQRES 21 C 597 ASP ARG THR ILE CYS THR VAL PRO LEU ILE ASP VAL ILE
SEQRES 22 C 597 ASN GLY ASN THR TYR GLU ILE ILE PRO GLN GLY GLY GLY
SEQRES 23 C 597 ASP GLU ASP GLY TYR ALA ARG GLY ALA TRP ASP TRP SER
SEQRES 24 C 597 MET LEU TRP LYS ARG VAL PRO LEU THR PRO GLN GLU LYS
SEQRES 25 C 597 ARG LEU ARG LYS THR LYS THR GLU PRO TYR ARG SER PRO
SEQRES 26 C 597 ALA MET ALA GLY GLY LEU PHE ALA ILE GLU ARG GLU PHE
SEQRES 27 C 597 PHE PHE GLU LEU GLY LEU TYR ASP PRO GLY LEU GLN ILE
SEQRES 28 C 597 TRP GLY GLY GLU ASN PHE GLU ILE SER TYR LYS ILE TRP
SEQRES 29 C 597 GLN CYS GLY GLY LYS LEU LEU PHE VAL PRO CYS SER ARG
SEQRES 30 C 597 VAL GLY HIS ILE TYR ARG LEU GLU GLY TRP GLN GLY ASN
SEQRES 31 C 597 PRO PRO PRO ILE TYR VAL GLY SER SER PRO THR LEU LYS
SEQRES 32 C 597 ASN TYR VAL ARG VAL VAL GLU VAL TRP TRP ASP GLU TYR
SEQRES 33 C 597 LYS ASP TYR PHE TYR ALA SER ARG PRO GLU SER GLN ALA
SEQRES 34 C 597 LEU PRO TYR GLY ASP ILE SER GLU LEU LYS LYS PHE ARG
SEQRES 35 C 597 GLU ASP HIS ASN CYS LYS SER PHE LYS TRP PHE MET GLU
SEQRES 36 C 597 GLU ILE ALA TYR ASP ILE THR SER HIS TYR PRO LEU PRO
SEQRES 37 C 597 PRO LYS ASN VAL ASP TRP GLY GLU ILE ARG GLY PHE GLU
SEQRES 38 C 597 THR ALA TYR CYS ILE ASP SER MET GLY LYS THR ASN GLY
SEQRES 39 C 597 GLY PHE VAL GLU LEU GLY PRO CYS HIS ARG MET GLY GLY
SEQRES 40 C 597 ASN GLN LEU PHE ARG ILE ASN GLU ALA ASN GLN LEU MET
SEQRES 41 C 597 GLN TYR ASP GLN CYS LEU THR LYS GLY ALA ASP GLY SER
SEQRES 42 C 597 LYS VAL MET ILE THR HIS CYS ASN LEU ASN GLU PHE LYS
SEQRES 43 C 597 GLU TRP GLN TYR PHE LYS ASN LEU HIS ARG PHE THR HIS
SEQRES 44 C 597 ILE PRO SER GLY LYS CYS LEU ASP ARG SER GLU VAL LEU
SEQRES 45 C 597 HIS GLN VAL PHE ILE SER ASN CYS ASP SER SER LYS THR
SEQRES 46 C 597 THR GLN LYS TRP GLU MET ASN ASN ILE HIS SER VAL
SEQRES 1 D 597 PRO GLY GLU ASP ARG PHE LYS PRO VAL VAL PRO TRP PRO
SEQRES 2 D 597 HIS VAL GLU GLY VAL GLU VAL ASP LEU GLU SER ILE ARG
SEQRES 3 D 597 ARG ILE ASN LYS ALA LYS ASN GLU GLN GLU HIS HIS ALA
SEQRES 4 D 597 GLY GLY ASP SER GLN LYS ASP ILE MET GLN ARG GLN TYR
SEQRES 5 D 597 LEU THR PHE LYS PRO GLN THR PHE THR TYR HIS ASP PRO
SEQRES 6 D 597 VAL LEU ARG PRO GLY ILE LEU GLY ASN PHE GLU PRO LYS
SEQRES 7 D 597 GLU PRO GLU PRO PRO GLY VAL VAL GLY GLY PRO GLY GLU
SEQRES 8 D 597 LYS ALA LYS PRO LEU VAL LEU GLY PRO GLU PHE LYS GLN
SEQRES 9 D 597 ALA ILE GLN ALA SER ILE LYS GLU PHE GLY PHE ASN MET
SEQRES 10 D 597 VAL ALA SER ASP MET ILE SER LEU ASP ARG SER VAL ASN
SEQRES 11 D 597 ASP LEU ARG GLN GLU GLU CYS LYS TYR TRP HIS TYR ASP
SEQRES 12 D 597 GLU ASN LEU LEU THR SER SER VAL VAL ILE VAL PHE HIS
SEQRES 13 D 597 ASN GLU GLY TRP SER THR LEU MET ARG THR VAL HIS SER
SEQRES 14 D 597 VAL ILE LYS ARG THR PRO ARG LYS TYR LEU ALA GLU ILE
SEQRES 15 D 597 VAL LEU ILE ASP ASP PHE SER ASN LYS GLU HIS LEU LYS
SEQRES 16 D 597 GLU LYS LEU ASP GLU TYR ILE LYS LEU TRP ASN GLY LEU
SEQRES 17 D 597 VAL LYS VAL PHE ARG ASN GLU ARG ARG GLU GLY LEU ILE
SEQRES 18 D 597 GLN ALA ARG SER ILE GLY ALA GLN LYS ALA LYS LEU GLY
SEQRES 19 D 597 GLN VAL LEU ILE TYR LEU ASP ALA HIS CYS GLU VAL ALA
SEQRES 20 D 597 VAL ASN TRP TYR ALA PRO LEU VAL ALA PRO ILE SER LYS
SEQRES 21 D 597 ASP ARG THR ILE CYS THR VAL PRO LEU ILE ASP VAL ILE
SEQRES 22 D 597 ASN GLY ASN THR TYR GLU ILE ILE PRO GLN GLY GLY GLY
SEQRES 23 D 597 ASP GLU ASP GLY TYR ALA ARG GLY ALA TRP ASP TRP SER
SEQRES 24 D 597 MET LEU TRP LYS ARG VAL PRO LEU THR PRO GLN GLU LYS
SEQRES 25 D 597 ARG LEU ARG LYS THR LYS THR GLU PRO TYR ARG SER PRO
SEQRES 26 D 597 ALA MET ALA GLY GLY LEU PHE ALA ILE GLU ARG GLU PHE
SEQRES 27 D 597 PHE PHE GLU LEU GLY LEU TYR ASP PRO GLY LEU GLN ILE
SEQRES 28 D 597 TRP GLY GLY GLU ASN PHE GLU ILE SER TYR LYS ILE TRP
SEQRES 29 D 597 GLN CYS GLY GLY LYS LEU LEU PHE VAL PRO CYS SER ARG
SEQRES 30 D 597 VAL GLY HIS ILE TYR ARG LEU GLU GLY TRP GLN GLY ASN
SEQRES 31 D 597 PRO PRO PRO ILE TYR VAL GLY SER SER PRO THR LEU LYS
SEQRES 32 D 597 ASN TYR VAL ARG VAL VAL GLU VAL TRP TRP ASP GLU TYR
SEQRES 33 D 597 LYS ASP TYR PHE TYR ALA SER ARG PRO GLU SER GLN ALA
SEQRES 34 D 597 LEU PRO TYR GLY ASP ILE SER GLU LEU LYS LYS PHE ARG
SEQRES 35 D 597 GLU ASP HIS ASN CYS LYS SER PHE LYS TRP PHE MET GLU
SEQRES 36 D 597 GLU ILE ALA TYR ASP ILE THR SER HIS TYR PRO LEU PRO
SEQRES 37 D 597 PRO LYS ASN VAL ASP TRP GLY GLU ILE ARG GLY PHE GLU
SEQRES 38 D 597 THR ALA TYR CYS ILE ASP SER MET GLY LYS THR ASN GLY
SEQRES 39 D 597 GLY PHE VAL GLU LEU GLY PRO CYS HIS ARG MET GLY GLY
SEQRES 40 D 597 ASN GLN LEU PHE ARG ILE ASN GLU ALA ASN GLN LEU MET
SEQRES 41 D 597 GLN TYR ASP GLN CYS LEU THR LYS GLY ALA ASP GLY SER
SEQRES 42 D 597 LYS VAL MET ILE THR HIS CYS ASN LEU ASN GLU PHE LYS
SEQRES 43 D 597 GLU TRP GLN TYR PHE LYS ASN LEU HIS ARG PHE THR HIS
SEQRES 44 D 597 ILE PRO SER GLY LYS CYS LEU ASP ARG SER GLU VAL LEU
SEQRES 45 D 597 HIS GLN VAL PHE ILE SER ASN CYS ASP SER SER LYS THR
SEQRES 46 D 597 THR GLN LYS TRP GLU MET ASN ASN ILE HIS SER VAL
SEQRES 1 E 597 PRO GLY GLU ASP ARG PHE LYS PRO VAL VAL PRO TRP PRO
SEQRES 2 E 597 HIS VAL GLU GLY VAL GLU VAL ASP LEU GLU SER ILE ARG
SEQRES 3 E 597 ARG ILE ASN LYS ALA LYS ASN GLU GLN GLU HIS HIS ALA
SEQRES 4 E 597 GLY GLY ASP SER GLN LYS ASP ILE MET GLN ARG GLN TYR
SEQRES 5 E 597 LEU THR PHE LYS PRO GLN THR PHE THR TYR HIS ASP PRO
SEQRES 6 E 597 VAL LEU ARG PRO GLY ILE LEU GLY ASN PHE GLU PRO LYS
SEQRES 7 E 597 GLU PRO GLU PRO PRO GLY VAL VAL GLY GLY PRO GLY GLU
SEQRES 8 E 597 LYS ALA LYS PRO LEU VAL LEU GLY PRO GLU PHE LYS GLN
SEQRES 9 E 597 ALA ILE GLN ALA SER ILE LYS GLU PHE GLY PHE ASN MET
SEQRES 10 E 597 VAL ALA SER ASP MET ILE SER LEU ASP ARG SER VAL ASN
SEQRES 11 E 597 ASP LEU ARG GLN GLU GLU CYS LYS TYR TRP HIS TYR ASP
SEQRES 12 E 597 GLU ASN LEU LEU THR SER SER VAL VAL ILE VAL PHE HIS
SEQRES 13 E 597 ASN GLU GLY TRP SER THR LEU MET ARG THR VAL HIS SER
SEQRES 14 E 597 VAL ILE LYS ARG THR PRO ARG LYS TYR LEU ALA GLU ILE
SEQRES 15 E 597 VAL LEU ILE ASP ASP PHE SER ASN LYS GLU HIS LEU LYS
SEQRES 16 E 597 GLU LYS LEU ASP GLU TYR ILE LYS LEU TRP ASN GLY LEU
SEQRES 17 E 597 VAL LYS VAL PHE ARG ASN GLU ARG ARG GLU GLY LEU ILE
SEQRES 18 E 597 GLN ALA ARG SER ILE GLY ALA GLN LYS ALA LYS LEU GLY
SEQRES 19 E 597 GLN VAL LEU ILE TYR LEU ASP ALA HIS CYS GLU VAL ALA
SEQRES 20 E 597 VAL ASN TRP TYR ALA PRO LEU VAL ALA PRO ILE SER LYS
SEQRES 21 E 597 ASP ARG THR ILE CYS THR VAL PRO LEU ILE ASP VAL ILE
SEQRES 22 E 597 ASN GLY ASN THR TYR GLU ILE ILE PRO GLN GLY GLY GLY
SEQRES 23 E 597 ASP GLU ASP GLY TYR ALA ARG GLY ALA TRP ASP TRP SER
SEQRES 24 E 597 MET LEU TRP LYS ARG VAL PRO LEU THR PRO GLN GLU LYS
SEQRES 25 E 597 ARG LEU ARG LYS THR LYS THR GLU PRO TYR ARG SER PRO
SEQRES 26 E 597 ALA MET ALA GLY GLY LEU PHE ALA ILE GLU ARG GLU PHE
SEQRES 27 E 597 PHE PHE GLU LEU GLY LEU TYR ASP PRO GLY LEU GLN ILE
SEQRES 28 E 597 TRP GLY GLY GLU ASN PHE GLU ILE SER TYR LYS ILE TRP
SEQRES 29 E 597 GLN CYS GLY GLY LYS LEU LEU PHE VAL PRO CYS SER ARG
SEQRES 30 E 597 VAL GLY HIS ILE TYR ARG LEU GLU GLY TRP GLN GLY ASN
SEQRES 31 E 597 PRO PRO PRO ILE TYR VAL GLY SER SER PRO THR LEU LYS
SEQRES 32 E 597 ASN TYR VAL ARG VAL VAL GLU VAL TRP TRP ASP GLU TYR
SEQRES 33 E 597 LYS ASP TYR PHE TYR ALA SER ARG PRO GLU SER GLN ALA
SEQRES 34 E 597 LEU PRO TYR GLY ASP ILE SER GLU LEU LYS LYS PHE ARG
SEQRES 35 E 597 GLU ASP HIS ASN CYS LYS SER PHE LYS TRP PHE MET GLU
SEQRES 36 E 597 GLU ILE ALA TYR ASP ILE THR SER HIS TYR PRO LEU PRO
SEQRES 37 E 597 PRO LYS ASN VAL ASP TRP GLY GLU ILE ARG GLY PHE GLU
SEQRES 38 E 597 THR ALA TYR CYS ILE ASP SER MET GLY LYS THR ASN GLY
SEQRES 39 E 597 GLY PHE VAL GLU LEU GLY PRO CYS HIS ARG MET GLY GLY
SEQRES 40 E 597 ASN GLN LEU PHE ARG ILE ASN GLU ALA ASN GLN LEU MET
SEQRES 41 E 597 GLN TYR ASP GLN CYS LEU THR LYS GLY ALA ASP GLY SER
SEQRES 42 E 597 LYS VAL MET ILE THR HIS CYS ASN LEU ASN GLU PHE LYS
SEQRES 43 E 597 GLU TRP GLN TYR PHE LYS ASN LEU HIS ARG PHE THR HIS
SEQRES 44 E 597 ILE PRO SER GLY LYS CYS LEU ASP ARG SER GLU VAL LEU
SEQRES 45 E 597 HIS GLN VAL PHE ILE SER ASN CYS ASP SER SER LYS THR
SEQRES 46 E 597 THR GLN LYS TRP GLU MET ASN ASN ILE HIS SER VAL
SEQRES 1 F 597 PRO GLY GLU ASP ARG PHE LYS PRO VAL VAL PRO TRP PRO
SEQRES 2 F 597 HIS VAL GLU GLY VAL GLU VAL ASP LEU GLU SER ILE ARG
SEQRES 3 F 597 ARG ILE ASN LYS ALA LYS ASN GLU GLN GLU HIS HIS ALA
SEQRES 4 F 597 GLY GLY ASP SER GLN LYS ASP ILE MET GLN ARG GLN TYR
SEQRES 5 F 597 LEU THR PHE LYS PRO GLN THR PHE THR TYR HIS ASP PRO
SEQRES 6 F 597 VAL LEU ARG PRO GLY ILE LEU GLY ASN PHE GLU PRO LYS
SEQRES 7 F 597 GLU PRO GLU PRO PRO GLY VAL VAL GLY GLY PRO GLY GLU
SEQRES 8 F 597 LYS ALA LYS PRO LEU VAL LEU GLY PRO GLU PHE LYS GLN
SEQRES 9 F 597 ALA ILE GLN ALA SER ILE LYS GLU PHE GLY PHE ASN MET
SEQRES 10 F 597 VAL ALA SER ASP MET ILE SER LEU ASP ARG SER VAL ASN
SEQRES 11 F 597 ASP LEU ARG GLN GLU GLU CYS LYS TYR TRP HIS TYR ASP
SEQRES 12 F 597 GLU ASN LEU LEU THR SER SER VAL VAL ILE VAL PHE HIS
SEQRES 13 F 597 ASN GLU GLY TRP SER THR LEU MET ARG THR VAL HIS SER
SEQRES 14 F 597 VAL ILE LYS ARG THR PRO ARG LYS TYR LEU ALA GLU ILE
SEQRES 15 F 597 VAL LEU ILE ASP ASP PHE SER ASN LYS GLU HIS LEU LYS
SEQRES 16 F 597 GLU LYS LEU ASP GLU TYR ILE LYS LEU TRP ASN GLY LEU
SEQRES 17 F 597 VAL LYS VAL PHE ARG ASN GLU ARG ARG GLU GLY LEU ILE
SEQRES 18 F 597 GLN ALA ARG SER ILE GLY ALA GLN LYS ALA LYS LEU GLY
SEQRES 19 F 597 GLN VAL LEU ILE TYR LEU ASP ALA HIS CYS GLU VAL ALA
SEQRES 20 F 597 VAL ASN TRP TYR ALA PRO LEU VAL ALA PRO ILE SER LYS
SEQRES 21 F 597 ASP ARG THR ILE CYS THR VAL PRO LEU ILE ASP VAL ILE
SEQRES 22 F 597 ASN GLY ASN THR TYR GLU ILE ILE PRO GLN GLY GLY GLY
SEQRES 23 F 597 ASP GLU ASP GLY TYR ALA ARG GLY ALA TRP ASP TRP SER
SEQRES 24 F 597 MET LEU TRP LYS ARG VAL PRO LEU THR PRO GLN GLU LYS
SEQRES 25 F 597 ARG LEU ARG LYS THR LYS THR GLU PRO TYR ARG SER PRO
SEQRES 26 F 597 ALA MET ALA GLY GLY LEU PHE ALA ILE GLU ARG GLU PHE
SEQRES 27 F 597 PHE PHE GLU LEU GLY LEU TYR ASP PRO GLY LEU GLN ILE
SEQRES 28 F 597 TRP GLY GLY GLU ASN PHE GLU ILE SER TYR LYS ILE TRP
SEQRES 29 F 597 GLN CYS GLY GLY LYS LEU LEU PHE VAL PRO CYS SER ARG
SEQRES 30 F 597 VAL GLY HIS ILE TYR ARG LEU GLU GLY TRP GLN GLY ASN
SEQRES 31 F 597 PRO PRO PRO ILE TYR VAL GLY SER SER PRO THR LEU LYS
SEQRES 32 F 597 ASN TYR VAL ARG VAL VAL GLU VAL TRP TRP ASP GLU TYR
SEQRES 33 F 597 LYS ASP TYR PHE TYR ALA SER ARG PRO GLU SER GLN ALA
SEQRES 34 F 597 LEU PRO TYR GLY ASP ILE SER GLU LEU LYS LYS PHE ARG
SEQRES 35 F 597 GLU ASP HIS ASN CYS LYS SER PHE LYS TRP PHE MET GLU
SEQRES 36 F 597 GLU ILE ALA TYR ASP ILE THR SER HIS TYR PRO LEU PRO
SEQRES 37 F 597 PRO LYS ASN VAL ASP TRP GLY GLU ILE ARG GLY PHE GLU
SEQRES 38 F 597 THR ALA TYR CYS ILE ASP SER MET GLY LYS THR ASN GLY
SEQRES 39 F 597 GLY PHE VAL GLU LEU GLY PRO CYS HIS ARG MET GLY GLY
SEQRES 40 F 597 ASN GLN LEU PHE ARG ILE ASN GLU ALA ASN GLN LEU MET
SEQRES 41 F 597 GLN TYR ASP GLN CYS LEU THR LYS GLY ALA ASP GLY SER
SEQRES 42 F 597 LYS VAL MET ILE THR HIS CYS ASN LEU ASN GLU PHE LYS
SEQRES 43 F 597 GLU TRP GLN TYR PHE LYS ASN LEU HIS ARG PHE THR HIS
SEQRES 44 F 597 ILE PRO SER GLY LYS CYS LEU ASP ARG SER GLU VAL LEU
SEQRES 45 F 597 HIS GLN VAL PHE ILE SER ASN CYS ASP SER SER LYS THR
SEQRES 46 F 597 THR GLN LYS TRP GLU MET ASN ASN ILE HIS SER VAL
HET MN A 701 1
HET MN B 701 1
HET MN C 701 1
HET MN D 701 1
HET MN E 701 1
HET MN F 701 1
HETNAM MN MANGANESE (II) ION
FORMUL 7 MN 6(MN 2+)
FORMUL 13 HOH *188(H2 O)
HELIX 1 AA1 PHE A 162 GLY A 174 1 13
HELIX 2 AA2 ASN A 176 MET A 182 1 7
HELIX 3 AA3 GLN A 194 LYS A 198 5 5
HELIX 4 AA4 GLY A 219 THR A 234 1 16
HELIX 5 AA5 PRO A 235 LYS A 237 5 3
HELIX 6 AA6 LYS A 251 LYS A 255 5 5
HELIX 7 AA7 GLU A 256 ILE A 262 1 7
HELIX 8 AA8 LYS A 263 ASN A 266 5 4
HELIX 9 AA9 GLY A 279 ALA A 291 1 13
HELIX 10 AB1 TRP A 310 ASP A 321 1 12
HELIX 11 AB2 THR A 368 ARG A 375 1 8
HELIX 12 AB3 ARG A 396 LEU A 402 1 7
HELIX 13 AB4 GLU A 415 CYS A 426 1 12
HELIX 14 AB5 SER A 459 TRP A 473 1 15
HELIX 15 AB6 TYR A 476 ARG A 484 1 9
HELIX 16 AB7 ILE A 495 HIS A 505 1 11
HELIX 17 AB8 SER A 509 ILE A 517 1 9
HELIX 18 AB9 ASP A 520 TYR A 525 1 6
HELIX 19 AC1 GLY A 566 LEU A 570 5 5
HELIX 20 AC2 PHE B 162 GLY B 174 1 13
HELIX 21 AC3 ASN B 176 MET B 182 1 7
HELIX 22 AC4 GLN B 194 LYS B 198 5 5
HELIX 23 AC5 GLY B 219 ARG B 233 1 15
HELIX 24 AC6 LYS B 251 LYS B 255 5 5
HELIX 25 AC7 GLU B 256 ILE B 262 1 7
HELIX 26 AC8 GLY B 279 LYS B 290 1 12
HELIX 27 AC9 TRP B 310 ASP B 321 1 12
HELIX 28 AD1 THR B 368 ARG B 375 1 8
HELIX 29 AD2 ARG B 396 LEU B 402 1 7
HELIX 30 AD3 GLY B 414 CYS B 426 1 13
HELIX 31 AD4 THR B 461 TRP B 473 1 13
HELIX 32 AD5 TYR B 476 ARG B 484 1 9
HELIX 33 AD6 ILE B 495 HIS B 505 1 11
HELIX 34 AD7 SER B 509 ILE B 517 1 9
HELIX 35 AD8 ASP B 520 TYR B 525 1 6
HELIX 36 AD9 GLY B 566 LEU B 570 5 5
HELIX 37 AE1 PHE C 162 GLY C 174 1 13
HELIX 38 AE2 ASN C 176 ILE C 183 1 8
HELIX 39 AE3 GLN C 194 LYS C 198 5 5
HELIX 40 AE4 GLY C 219 THR C 234 1 16
HELIX 41 AE5 PRO C 235 LYS C 237 5 3
HELIX 42 AE6 LYS C 251 LYS C 255 5 5
HELIX 43 AE7 GLU C 256 ILE C 262 1 7
HELIX 44 AE8 GLY C 279 ALA C 291 1 13
HELIX 45 AE9 TRP C 310 ASP C 321 1 12
HELIX 46 AF1 THR C 368 ARG C 375 1 8
HELIX 47 AF2 ARG C 396 LEU C 402 1 7
HELIX 48 AF3 GLY C 414 CYS C 426 1 13
HELIX 49 AF4 SER C 458 TRP C 473 1 16
HELIX 50 AF5 TYR C 476 ARG C 484 1 9
HELIX 51 AF6 ILE C 495 HIS C 505 1 11
HELIX 52 AF7 SER C 509 ILE C 517 1 9
HELIX 53 AF8 ASP C 520 TYR C 525 1 6
HELIX 54 AF9 GLY C 566 LEU C 570 5 5
HELIX 55 AG1 GLU D 161 GLY D 174 1 14
HELIX 56 AG2 ASN D 176 MET D 182 1 7
HELIX 57 AG3 GLN D 194 LYS D 198 5 5
HELIX 58 AG4 GLY D 219 THR D 234 1 16
HELIX 59 AG5 PRO D 235 LYS D 237 5 3
HELIX 60 AG6 LYS D 251 LYS D 255 5 5
HELIX 61 AG7 GLU D 256 ILE D 262 1 7
HELIX 62 AG8 GLY D 279 ALA D 291 1 13
HELIX 63 AG9 TRP D 310 ASP D 321 1 12
HELIX 64 AH1 THR D 368 ARG D 375 1 8
HELIX 65 AH2 ARG D 396 LEU D 402 1 7
HELIX 66 AH3 GLY D 414 CYS D 426 1 13
HELIX 67 AH4 PRO D 460 TRP D 473 1 14
HELIX 68 AH5 TYR D 476 ARG D 484 1 9
HELIX 69 AH6 PRO D 485 GLN D 488 5 4
HELIX 70 AH7 ILE D 495 HIS D 505 1 11
HELIX 71 AH8 SER D 509 ILE D 517 1 9
HELIX 72 AH9 ASP D 520 TYR D 525 1 6
HELIX 73 AI1 GLY D 566 LEU D 570 5 5
HELIX 74 AI2 LYS D 644 GLN D 647 5 4
HELIX 75 AI3 PHE E 162 GLY E 174 1 13
HELIX 76 AI4 ASN E 176 MET E 182 1 7
HELIX 77 AI5 GLN E 194 LYS E 198 5 5
HELIX 78 AI6 GLY E 219 THR E 234 1 16
HELIX 79 AI7 LYS E 251 LYS E 255 5 5
HELIX 80 AI8 GLU E 256 ILE E 262 1 7
HELIX 81 AI9 GLY E 279 LYS E 290 1 12
HELIX 82 AJ1 TRP E 310 ASP E 321 1 12
HELIX 83 AJ2 THR E 368 ARG E 375 1 8
HELIX 84 AJ3 ARG E 396 LEU E 402 1 7
HELIX 85 AJ4 GLY E 414 CYS E 426 1 13
HELIX 86 AJ5 SER E 458 TRP E 473 1 16
HELIX 87 AJ6 TYR E 476 ARG E 484 1 9
HELIX 88 AJ7 PRO E 485 GLN E 488 5 4
HELIX 89 AJ8 ILE E 495 HIS E 505 1 11
HELIX 90 AJ9 SER E 509 ILE E 517 1 9
HELIX 91 AK1 ASP E 520 TYR E 525 1 6
HELIX 92 AK2 PHE F 162 GLY F 174 1 13
HELIX 93 AK3 ASN F 176 MET F 182 1 7
HELIX 94 AK4 GLN F 194 LYS F 198 5 5
HELIX 95 AK5 GLY F 219 THR F 234 1 16
HELIX 96 AK6 PRO F 235 LYS F 237 5 3
HELIX 97 AK7 LYS F 251 LYS F 255 5 5
HELIX 98 AK8 LYS F 257 ILE F 262 1 6
HELIX 99 AK9 LYS F 263 ASN F 266 5 4
HELIX 100 AL1 GLY F 279 ALA F 291 1 13
HELIX 101 AL2 TRP F 310 ASP F 321 1 12
HELIX 102 AL3 THR F 368 ARG F 375 1 8
HELIX 103 AL4 ARG F 396 LEU F 402 1 7
HELIX 104 AL5 GLY F 414 CYS F 426 1 13
HELIX 105 AL6 SER F 459 TRP F 473 1 15
HELIX 106 AL7 TYR F 476 ARG F 484 1 9
HELIX 107 AL8 ILE F 495 HIS F 505 1 11
HELIX 108 AL9 SER F 509 ILE F 517 1 9
HELIX 109 AM1 ASP F 520 TYR F 525 1 6
HELIX 110 AM2 GLY F 566 LEU F 570 5 5
HELIX 111 AM3 LYS F 644 GLN F 647 5 4
SHEET 1 AA1 2 VAL A 126 LEU A 127 0
SHEET 2 AA1 2 TRP A 200 HIS A 201 -1 O HIS A 201 N VAL A 126
SHEET 1 AA2 5 VAL A 269 ARG A 273 0
SHEET 2 AA2 5 LEU A 239 ASP A 246 1 N LEU A 244 O LYS A 270
SHEET 3 AA2 5 SER A 209 PHE A 215 1 N SER A 209 O ALA A 240
SHEET 4 AA2 5 VAL A 296 TYR A 299 1 O ILE A 298 N SER A 210
SHEET 5 AA2 5 PHE A 392 GLU A 395 -1 O ILE A 394 N LEU A 297
SHEET 1 AA3 4 CYS A 304 VAL A 306 0
SHEET 2 AA3 4 LYS A 429 TYR A 442 -1 O GLY A 439 N GLU A 305
SHEET 3 AA3 4 ILE A 324 ASN A 334 1 N ASP A 331 O VAL A 438
SHEET 4 AA3 4 ILE A 340 ILE A 341 -1 O ILE A 341 N VAL A 332
SHEET 1 AA4 3 CYS A 304 VAL A 306 0
SHEET 2 AA4 3 LYS A 429 TYR A 442 -1 O GLY A 439 N GLU A 305
SHEET 3 AA4 3 TYR A 382 ARG A 383 -1 N TYR A 382 O PHE A 432
SHEET 1 AA5 2 ALA A 352 TRP A 356 0
SHEET 2 AA5 2 TRP A 362 PRO A 366 -1 O LYS A 363 N ALA A 355
SHEET 1 AA6 6 LYS A 594 HIS A 599 0
SHEET 2 AA6 6 GLN A 584 GLY A 589 -1 N CYS A 585 O THR A 598
SHEET 3 AA6 6 LEU A 579 GLN A 581 -1 N GLN A 581 O GLN A 584
SHEET 4 AA6 6 PHE A 571 ASN A 574 -1 N ARG A 572 O MET A 580
SHEET 5 AA6 6 ASN A 531 GLY A 539 -1 N ASP A 533 O ILE A 573
SHEET 6 AA6 6 TRP A 649 ASN A 652 -1 O ASN A 652 N GLU A 536
SHEET 1 AA7 2 TYR A 544 ASP A 547 0
SHEET 2 AA7 2 GLU A 558 PRO A 561 -1 O GLY A 560 N CYS A 545
SHEET 1 AA8 2 TRP A 608 PHE A 611 0
SHEET 2 AA8 2 ARG A 616 HIS A 619 -1 O ARG A 616 N PHE A 611
SHEET 1 AA9 2 CYS A 625 SER A 629 0
SHEET 2 AA9 2 GLN A 634 SER A 638 -1 O PHE A 636 N ASP A 627
SHEET 1 AB1 2 VAL B 126 LEU B 127 0
SHEET 2 AB1 2 TRP B 200 HIS B 201 -1 O HIS B 201 N VAL B 126
SHEET 1 AB2 5 VAL B 269 ARG B 273 0
SHEET 2 AB2 5 LEU B 239 ASP B 246 1 N LEU B 244 O LYS B 270
SHEET 3 AB2 5 SER B 209 PHE B 215 1 N SER B 209 O ALA B 240
SHEET 4 AB2 5 VAL B 296 ASP B 301 1 O ILE B 298 N SER B 210
SHEET 5 AB2 5 PHE B 392 GLU B 395 -1 O ILE B 394 N LEU B 297
SHEET 1 AB3 4 CYS B 304 VAL B 306 0
SHEET 2 AB3 4 LYS B 429 TYR B 442 -1 O GLY B 439 N GLU B 305
SHEET 3 AB3 4 ILE B 324 ASN B 334 1 N ILE B 333 O HIS B 440
SHEET 4 AB3 4 ILE B 340 ILE B 341 -1 O ILE B 341 N VAL B 332
SHEET 1 AB4 3 CYS B 304 VAL B 306 0
SHEET 2 AB4 3 LYS B 429 TYR B 442 -1 O GLY B 439 N GLU B 305
SHEET 3 AB4 3 TYR B 382 ARG B 383 -1 N TYR B 382 O PHE B 432
SHEET 1 AB5 2 ALA B 352 TRP B 356 0
SHEET 2 AB5 2 TRP B 362 PRO B 366 -1 O LYS B 363 N ALA B 355
SHEET 1 AB6 6 VAL B 595 HIS B 599 0
SHEET 2 AB6 6 GLN B 584 LYS B 588 -1 N CYS B 585 O THR B 598
SHEET 3 AB6 6 LEU B 579 GLN B 581 -1 N GLN B 581 O GLN B 584
SHEET 4 AB6 6 PHE B 571 ASN B 574 -1 N ARG B 572 O MET B 580
SHEET 5 AB6 6 ASN B 531 GLY B 539 -1 N ASP B 533 O ILE B 573
SHEET 6 AB6 6 TRP B 649 ASN B 652 -1 O GLU B 650 N ARG B 538
SHEET 1 AB7 2 TYR B 544 ASP B 547 0
SHEET 2 AB7 2 GLU B 558 PRO B 561 -1 O GLY B 560 N CYS B 545
SHEET 1 AB8 4 TRP B 608 PHE B 611 0
SHEET 2 AB8 4 ARG B 616 HIS B 619 -1 O ARG B 616 N PHE B 611
SHEET 3 AB8 4 LYS B 624 SER B 629 -1 O LYS B 624 N HIS B 619
SHEET 4 AB8 4 GLN B 634 SER B 638 -1 O PHE B 636 N ASP B 627
SHEET 1 AB9 2 VAL C 126 LEU C 127 0
SHEET 2 AB9 2 TRP C 200 HIS C 201 -1 O HIS C 201 N VAL C 126
SHEET 1 AC1 5 VAL C 269 ARG C 273 0
SHEET 2 AC1 5 LEU C 239 ASP C 246 1 N LEU C 244 O LYS C 270
SHEET 3 AC1 5 SER C 209 PHE C 215 1 N SER C 209 O ALA C 240
SHEET 4 AC1 5 VAL C 296 TYR C 299 1 O ILE C 298 N SER C 210
SHEET 5 AC1 5 PHE C 392 GLU C 395 -1 O ILE C 394 N LEU C 297
SHEET 1 AC2 4 CYS C 304 VAL C 306 0
SHEET 2 AC2 4 LYS C 429 TYR C 442 -1 O GLY C 439 N GLU C 305
SHEET 3 AC2 4 ILE C 324 ASN C 334 1 N ASP C 331 O VAL C 438
SHEET 4 AC2 4 ILE C 340 ILE C 341 -1 O ILE C 341 N VAL C 332
SHEET 1 AC3 3 CYS C 304 VAL C 306 0
SHEET 2 AC3 3 LYS C 429 TYR C 442 -1 O GLY C 439 N GLU C 305
SHEET 3 AC3 3 TYR C 382 ARG C 383 -1 N TYR C 382 O PHE C 432
SHEET 1 AC4 2 ALA C 352 GLY C 354 0
SHEET 2 AC4 2 ARG C 364 PRO C 366 -1 O VAL C 365 N ARG C 353
SHEET 1 AC5 7 GLY C 555 PHE C 556 0
SHEET 2 AC5 7 VAL C 595 HIS C 599 -1 O ILE C 597 N GLY C 555
SHEET 3 AC5 7 GLN C 584 LYS C 588 -1 N CYS C 585 O THR C 598
SHEET 4 AC5 7 LEU C 579 GLN C 581 -1 N GLN C 581 O GLN C 584
SHEET 5 AC5 7 PHE C 571 ASN C 574 -1 N ARG C 572 O MET C 580
SHEET 6 AC5 7 ASN C 531 GLY C 539 -1 N VAL C 532 O ILE C 573
SHEET 7 AC5 7 TRP C 649 ASN C 652 -1 O GLU C 650 N ARG C 538
SHEET 1 AC6 2 TYR C 544 ASP C 547 0
SHEET 2 AC6 2 GLU C 558 PRO C 561 -1 O GLU C 558 N ASP C 547
SHEET 1 AC7 2 TRP C 608 PHE C 611 0
SHEET 2 AC7 2 ARG C 616 HIS C 619 -1 O ARG C 616 N PHE C 611
SHEET 1 AC8 2 CYS C 625 SER C 629 0
SHEET 2 AC8 2 GLN C 634 SER C 638 -1 O PHE C 636 N ASP C 627
SHEET 1 AC9 2 VAL D 126 LEU D 127 0
SHEET 2 AC9 2 TRP D 200 HIS D 201 -1 O HIS D 201 N VAL D 126
SHEET 1 AD1 5 VAL D 269 ARG D 273 0
SHEET 2 AD1 5 LEU D 239 ASP D 246 1 N LEU D 244 O LYS D 270
SHEET 3 AD1 5 SER D 209 PHE D 215 1 N ILE D 213 O ILE D 245
SHEET 4 AD1 5 VAL D 296 TYR D 299 1 O ILE D 298 N VAL D 212
SHEET 5 AD1 5 PHE D 392 GLU D 395 -1 O ILE D 394 N LEU D 297
SHEET 1 AD2 4 CYS D 304 VAL D 306 0
SHEET 2 AD2 4 LYS D 429 ILE D 441 -1 O GLY D 439 N GLU D 305
SHEET 3 AD2 4 ILE D 324 ILE D 333 1 N ASP D 331 O VAL D 438
SHEET 4 AD2 4 ILE D 340 ILE D 341 -1 O ILE D 341 N VAL D 332
SHEET 1 AD3 3 CYS D 304 VAL D 306 0
SHEET 2 AD3 3 LYS D 429 ILE D 441 -1 O GLY D 439 N GLU D 305
SHEET 3 AD3 3 TYR D 382 ARG D 383 -1 N TYR D 382 O PHE D 432
SHEET 1 AD4 2 ALA D 352 TRP D 356 0
SHEET 2 AD4 2 TRP D 362 PRO D 366 -1 O LYS D 363 N ALA D 355
SHEET 1 AD5 7 GLY D 555 PHE D 556 0
SHEET 2 AD5 7 VAL D 595 HIS D 599 -1 O ILE D 597 N GLY D 555
SHEET 3 AD5 7 GLN D 584 LYS D 588 -1 N CYS D 585 O THR D 598
SHEET 4 AD5 7 LEU D 579 GLN D 581 -1 N LEU D 579 O LEU D 586
SHEET 5 AD5 7 PHE D 571 ASN D 574 -1 N ARG D 572 O MET D 580
SHEET 6 AD5 7 ASN D 531 GLY D 539 -1 N ASP D 533 O ILE D 573
SHEET 7 AD5 7 TRP D 649 ASN D 652 -1 O ASN D 652 N GLU D 536
SHEET 1 AD6 2 TYR D 544 ASP D 547 0
SHEET 2 AD6 2 GLU D 558 PRO D 561 -1 O GLY D 560 N CYS D 545
SHEET 1 AD7 2 TRP D 608 PHE D 611 0
SHEET 2 AD7 2 ARG D 616 HIS D 619 -1 O ARG D 616 N PHE D 611
SHEET 1 AD8 2 CYS D 625 SER D 629 0
SHEET 2 AD8 2 GLN D 634 SER D 638 -1 O PHE D 636 N ASP D 627
SHEET 1 AD9 2 VAL E 126 LEU E 127 0
SHEET 2 AD9 2 TRP E 200 HIS E 201 -1 O HIS E 201 N VAL E 126
SHEET 1 AE1 5 VAL E 269 ARG E 273 0
SHEET 2 AE1 5 LEU E 239 ASP E 246 1 N LEU E 244 O LYS E 270
SHEET 3 AE1 5 SER E 209 PHE E 215 1 N SER E 209 O ALA E 240
SHEET 4 AE1 5 VAL E 296 LEU E 300 1 O ILE E 298 N SER E 210
SHEET 5 AE1 5 PHE E 392 GLU E 395 -1 O ILE E 394 N LEU E 297
SHEET 1 AE2 4 CYS E 304 VAL E 306 0
SHEET 2 AE2 4 LYS E 429 ILE E 441 -1 O GLY E 439 N GLU E 305
SHEET 3 AE2 4 ILE E 324 ILE E 333 1 N ASP E 331 O VAL E 438
SHEET 4 AE2 4 ILE E 340 ILE E 341 -1 O ILE E 341 N VAL E 332
SHEET 1 AE3 3 CYS E 304 VAL E 306 0
SHEET 2 AE3 3 LYS E 429 ILE E 441 -1 O GLY E 439 N GLU E 305
SHEET 3 AE3 3 TYR E 382 ARG E 383 -1 N TYR E 382 O PHE E 432
SHEET 1 AE4 2 ALA E 352 TRP E 356 0
SHEET 2 AE4 2 TRP E 362 PRO E 366 -1 O LYS E 363 N ALA E 355
SHEET 1 AE5 7 GLY E 555 PHE E 556 0
SHEET 2 AE5 7 VAL E 595 HIS E 599 -1 O ILE E 597 N GLY E 555
SHEET 3 AE5 7 GLN E 584 LYS E 588 -1 N CYS E 585 O THR E 598
SHEET 4 AE5 7 LEU E 579 GLN E 581 -1 N LEU E 579 O LEU E 586
SHEET 5 AE5 7 LEU E 570 ASN E 574 -1 N ARG E 572 O MET E 580
SHEET 6 AE5 7 ASN E 531 GLY E 539 -1 N ASP E 533 O ILE E 573
SHEET 7 AE5 7 TRP E 649 ASN E 652 -1 O ASN E 652 N GLU E 536
SHEET 1 AE6 2 TYR E 544 ASP E 547 0
SHEET 2 AE6 2 GLU E 558 PRO E 561 -1 O GLY E 560 N CYS E 545
SHEET 1 AE7 2 TRP E 608 PHE E 611 0
SHEET 2 AE7 2 ARG E 616 HIS E 619 -1 O ARG E 616 N PHE E 611
SHEET 1 AE8 2 CYS E 625 SER E 629 0
SHEET 2 AE8 2 GLN E 634 SER E 638 -1 O PHE E 636 N ASP E 627
SHEET 1 AE9 2 VAL F 126 LEU F 127 0
SHEET 2 AE9 2 TRP F 200 HIS F 201 -1 O HIS F 201 N VAL F 126
SHEET 1 AF1 5 VAL F 269 PHE F 272 0
SHEET 2 AF1 5 LEU F 239 ASP F 246 1 N LEU F 244 O LYS F 270
SHEET 3 AF1 5 SER F 209 PHE F 215 1 N PHE F 215 O ILE F 245
SHEET 4 AF1 5 VAL F 296 TYR F 299 1 O ILE F 298 N SER F 210
SHEET 5 AF1 5 PHE F 392 GLU F 395 -1 O ILE F 394 N LEU F 297
SHEET 1 AF2 4 CYS F 304 VAL F 306 0
SHEET 2 AF2 4 LYS F 429 ILE F 441 -1 O GLY F 439 N GLU F 305
SHEET 3 AF2 4 ILE F 324 ILE F 333 1 N ILE F 333 O HIS F 440
SHEET 4 AF2 4 ILE F 340 ILE F 341 -1 O ILE F 341 N VAL F 332
SHEET 1 AF3 3 CYS F 304 VAL F 306 0
SHEET 2 AF3 3 LYS F 429 ILE F 441 -1 O GLY F 439 N GLU F 305
SHEET 3 AF3 3 TYR F 382 ARG F 383 -1 N TYR F 382 O PHE F 432
SHEET 1 AF4 2 ALA F 352 TRP F 356 0
SHEET 2 AF4 2 TRP F 362 PRO F 366 -1 O LYS F 363 N ALA F 355
SHEET 1 AF5 7 GLY F 555 PHE F 556 0
SHEET 2 AF5 7 VAL F 595 HIS F 599 -1 O ILE F 597 N GLY F 555
SHEET 3 AF5 7 GLN F 584 LYS F 588 -1 N CYS F 585 O THR F 598
SHEET 4 AF5 7 LEU F 579 GLN F 581 -1 N GLN F 581 O GLN F 584
SHEET 5 AF5 7 PHE F 571 ASN F 574 -1 N ARG F 572 O MET F 580
SHEET 6 AF5 7 ASN F 531 GLY F 539 -1 N ASP F 533 O ILE F 573
SHEET 7 AF5 7 TRP F 649 ASN F 652 -1 O ASN F 652 N GLU F 536
SHEET 1 AF6 2 TYR F 544 ASP F 547 0
SHEET 2 AF6 2 GLU F 558 PRO F 561 -1 O GLY F 560 N CYS F 545
SHEET 1 AF7 2 TRP F 608 PHE F 611 0
SHEET 2 AF7 2 ARG F 616 HIS F 619 -1 O THR F 618 N GLN F 609
SHEET 1 AF8 2 CYS F 625 SER F 629 0
SHEET 2 AF8 2 GLN F 634 SER F 638 -1 O PHE F 636 N ASP F 627
SSBOND 1 CYS A 545 CYS A 562 1555 1555 2.05
SSBOND 2 CYS A 585 CYS A 600 1555 1555 2.98
SSBOND 3 CYS A 625 CYS A 640 1555 1555 2.12
SSBOND 4 CYS B 197 CYS B 435 1555 1555 2.02
SSBOND 5 CYS B 426 CYS B 507 1555 1555 2.09
SSBOND 6 CYS B 545 CYS B 562 1555 1555 2.05
SSBOND 7 CYS B 585 CYS B 600 1555 1555 2.57
SSBOND 8 CYS B 625 CYS B 640 1555 1555 2.66
SSBOND 9 CYS C 197 CYS C 435 1555 1555 1.91
SSBOND 10 CYS C 426 CYS C 507 1555 1555 2.09
SSBOND 11 CYS C 545 CYS C 562 1555 1555 2.05
SSBOND 12 CYS C 585 CYS C 600 1555 1555 2.14
SSBOND 13 CYS C 625 CYS C 640 1555 1555 2.86
SSBOND 14 CYS D 197 CYS D 435 1555 1555 2.06
SSBOND 15 CYS D 426 CYS D 507 1555 1555 2.09
SSBOND 16 CYS D 585 CYS D 600 1555 1555 2.97
SSBOND 17 CYS E 545 CYS E 562 1555 1555 2.75
SSBOND 18 CYS E 585 CYS E 600 1555 1555 2.07
SSBOND 19 CYS E 625 CYS E 640 1555 1555 2.34
SSBOND 20 CYS F 426 CYS F 507 1555 1555 2.09
SSBOND 21 CYS F 625 CYS F 640 1555 1555 2.05
LINK OD2 ASP B 301 MN MN B 701 1555 1555 2.37
LINK OD2 ASP C 301 MN MN C 701 1555 1555 2.76
LINK OD2 ASP E 301 MN MN E 701 1555 1555 2.32
LINK NE2 HIS E 303 MN MN E 701 1555 1555 2.73
LINK NE2 HIS E 440 MN MN E 701 1555 1555 2.43
LINK OD2 ASP F 301 MN MN F 701 1555 1555 2.41
LINK NE2 HIS F 303 MN MN F 701 1555 1555 2.69
LINK NE2 HIS F 440 MN MN F 701 1555 1555 2.57
CISPEP 1 GLY A 133 ASN A 134 0 -3.48
CISPEP 2 GLY A 148 PRO A 149 0 -6.51
CISPEP 3 GLU A 151 LYS A 152 0 -5.56
CISPEP 4 GLY A 159 PRO A 160 0 -4.37
CISPEP 5 GLY A 414 GLU A 415 0 11.88
CISPEP 6 GLN A 448 GLY A 449 0 10.56
CISPEP 7 TYR A 455 VAL A 456 0 -11.55
CISPEP 8 GLY A 457 SER A 458 0 -20.85
CISPEP 9 SER A 458 SER A 459 0 -4.32
CISPEP 10 ALA A 590 ASP A 591 0 -8.52
CISPEP 11 VAL A 631 LEU A 632 0 -3.78
CISPEP 12 GLY B 133 ASN B 134 0 -16.74
CISPEP 13 VAL B 146 GLY B 147 0 -13.54
CISPEP 14 GLY B 148 PRO B 149 0 -5.95
CISPEP 15 GLU B 151 LYS B 152 0 -18.51
CISPEP 16 GLY B 159 PRO B 160 0 4.00
CISPEP 17 GLU B 348 ASP B 349 0 28.39
CISPEP 18 SER B 458 SER B 459 0 -10.67
CISPEP 19 SER B 459 PRO B 460 0 15.88
CISPEP 20 GLY B 554 GLY B 555 0 8.45
CISPEP 21 ALA B 590 ASP B 591 0 -12.42
CISPEP 22 LEU B 602 ASN B 603 0 -12.73
CISPEP 23 VAL B 631 LEU B 632 0 -3.59
CISPEP 24 LYS B 644 THR B 645 0 22.26
CISPEP 25 HIS B 655 SER B 656 0 1.13
CISPEP 26 GLY C 133 ASN C 134 0 -2.60
CISPEP 27 VAL C 146 GLY C 147 0 -5.33
CISPEP 28 GLY C 148 PRO C 149 0 7.72
CISPEP 29 GLU C 151 LYS C 152 0 -7.23
CISPEP 30 GLY C 159 PRO C 160 0 -4.43
CISPEP 31 GLY C 413 GLY C 414 0 5.40
CISPEP 32 GLY C 457 SER C 458 0 1.02
CISPEP 33 ALA C 590 ASP C 591 0 -2.94
CISPEP 34 VAL C 631 LEU C 632 0 -2.79
CISPEP 35 LYS C 644 THR C 645 0 4.10
CISPEP 36 GLY D 133 ASN D 134 0 -7.47
CISPEP 37 VAL D 146 GLY D 147 0 -11.47
CISPEP 38 GLY D 148 PRO D 149 0 7.72
CISPEP 39 GLU D 151 LYS D 152 0 -1.53
CISPEP 40 GLY D 159 PRO D 160 0 -3.69
CISPEP 41 ASP D 347 GLU D 348 0 3.86
CISPEP 42 GLU D 348 ASP D 349 0 19.15
CISPEP 43 SER D 459 PRO D 460 0 -5.28
CISPEP 44 ALA D 590 ASP D 591 0 7.92
CISPEP 45 VAL D 631 LEU D 632 0 1.75
CISPEP 46 SER D 642 SER D 643 0 -6.73
CISPEP 47 SER D 643 LYS D 644 0 8.11
CISPEP 48 GLY E 133 ASN E 134 0 -9.78
CISPEP 49 VAL E 146 GLY E 147 0 -11.45
CISPEP 50 GLY E 148 PRO E 149 0 -12.23
CISPEP 51 GLU E 151 LYS E 152 0 -15.14
CISPEP 52 GLY E 159 PRO E 160 0 -4.36
CISPEP 53 GLY E 457 SER E 458 0 9.91
CISPEP 54 ALA E 590 ASP E 591 0 -6.67
CISPEP 55 VAL E 631 LEU E 632 0 -0.09
CISPEP 56 GLY F 133 ASN F 134 0 -3.54
CISPEP 57 VAL F 146 GLY F 147 0 -8.40
CISPEP 58 GLY F 148 PRO F 149 0 -2.25
CISPEP 59 GLU F 151 LYS F 152 0 -7.11
CISPEP 60 GLY F 159 PRO F 160 0 6.62
CISPEP 61 GLU F 348 ASP F 349 0 13.00
CISPEP 62 ILE F 454 TYR F 455 0 -13.56
CISPEP 63 GLY F 457 SER F 458 0 -18.57
CISPEP 64 ALA F 590 ASP F 591 0 2.67
CISPEP 65 VAL F 631 LEU F 632 0 -4.36
SITE 1 AC1 3 ASP A 301 HIS A 303 HIS A 440
SITE 1 AC2 3 ASP B 301 HIS B 303 HIS B 440
SITE 1 AC3 3 ASP C 301 HIS C 303 HIS C 440
SITE 1 AC4 2 ASP D 301 HIS D 440
SITE 1 AC5 3 ASP E 301 HIS E 303 HIS E 440
SITE 1 AC6 3 ASP F 301 HIS F 303 HIS F 440
CRYST1 137.695 158.233 251.870 90.00 90.00 90.00 P 21 21 21 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007262 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006320 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003970 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
