HEADER IMMUNE SYSTEM/RECEPTOR 23-DEC-11 4ADF
TITLE CRYSTAL STRUCTURE OF THE HUMAN COLONY-STIMULATING FACTOR 1 (HCSF-1)
TITLE 2 CYTOKINE IN COMPLEX WITH THE VIRAL RECEPTOR BARF1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SECRETED PROTEIN BARF1;
COMPND 3 CHAIN: A, B, C, D, E, F, M, N, O, P, Q, R;
COMPND 4 SYNONYM: BARF1,33 KDA EARLY PROTEIN, P33;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MACROPHAGE COLONY-STIMULATING FACTOR 1;
COMPND 9 CHAIN: G, H, I, J, K, L, S, T, U, V, W, X;
COMPND 10 FRAGMENT: UNP RESIDUES 33-181;
COMPND 11 SYNONYM: HCSF-1, CSF-1, M-CSF, MCSF, LANIMOSTIM, PROCESSED MACROPHAGE
COMPND 12 COLONY-STIMULATING FACTOR 1;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4;
SOURCE 3 ORGANISM_TAXID: 10376;
SOURCE 4 STRAIN: B95-8;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PHLSEC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VARIANT: CODONPLUS RIL;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS IMMUNE SYSTEM-RECEPTOR COMPLEX, RTKIII, EXTRACELLULAR, CYTOKINE
KEYWDS 2 RECEPTOR-CYTOKINE COMPLEX, FOUR-HELIX BUNDLE, GLYCOPROTEIN,
KEYWDS 3 IMMUNOGLOBULIN DOMAIN, ONCOGENE, CYTOKINE/SIGNALING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ELEGHEERT,N.BRACKE,S.N.SAVVIDES
REVDAT 4 20-DEC-23 4ADF 1 HETSYN
REVDAT 3 29-JUL-20 4ADF 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 26-SEP-12 4ADF 1 JRNL
REVDAT 1 22-AUG-12 4ADF 0
JRNL AUTH J.ELEGHEERT,N.BRACKE,P.POULIOT,I.GUTSCHE,A.V.SHKUMATOV,
JRNL AUTH 2 N.TARBOURIECH,K.VERSTRAETE,A.BEKAERT,W.P.BURMEISTER,
JRNL AUTH 3 D.I.SVERGUN,B.N.LAMBRECHT,B.VERGAUWEN,S.N.SAVVIDES
JRNL TITL ALLOSTERIC COMPETITIVE INACTIVATION OF HEMATOPOIETIC CSF-1
JRNL TITL 2 SIGNALING BY THE VIRAL DECOY RECEPTOR BARF1.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 938 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 22902366
JRNL DOI 10.1038/NSMB.2367
REMARK 2
REMARK 2 RESOLUTION. 4.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 58094
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2872
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 75.8580 - 12.1236 0.97 2786 113 0.2939 0.2882
REMARK 3 2 12.1236 - 9.6290 0.98 2676 141 0.1934 0.2242
REMARK 3 3 9.6290 - 8.4137 0.99 2663 140 0.1973 0.2268
REMARK 3 4 8.4137 - 7.6452 0.99 2649 140 0.2101 0.2506
REMARK 3 5 7.6452 - 7.0976 1.00 2648 139 0.1939 0.2606
REMARK 3 6 7.0976 - 6.6794 0.99 2654 138 0.2103 0.2731
REMARK 3 7 6.6794 - 6.3451 0.99 2648 138 0.2195 0.2555
REMARK 3 8 6.3451 - 6.0690 0.99 2610 137 0.2233 0.2878
REMARK 3 9 6.0690 - 5.8355 1.00 2638 139 0.2207 0.2694
REMARK 3 10 5.8355 - 5.6342 0.99 2637 138 0.2288 0.3082
REMARK 3 11 5.6342 - 5.4581 0.99 2594 136 0.2341 0.3028
REMARK 3 12 5.4581 - 5.3021 0.99 2618 139 0.2249 0.3184
REMARK 3 13 5.3021 - 5.1625 0.99 2605 136 0.2282 0.2806
REMARK 3 14 5.1625 - 5.0366 1.00 2628 139 0.2356 0.2904
REMARK 3 15 5.0366 - 4.9221 0.99 2627 138 0.2493 0.3138
REMARK 3 16 4.9221 - 4.8174 1.00 2614 138 0.2693 0.3190
REMARK 3 17 4.8174 - 4.7210 0.99 2563 137 0.2814 0.2884
REMARK 3 18 4.7210 - 4.6320 0.99 2631 139 0.2830 0.2995
REMARK 3 19 4.6320 - 4.5493 0.99 2564 136 0.3078 0.3401
REMARK 3 20 4.5493 - 4.4722 0.99 2604 137 0.3222 0.3562
REMARK 3 21 4.4722 - 4.4000 0.97 2565 134 0.3456 0.4054
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 187.2
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 165.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 216.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 19.42460
REMARK 3 B22 (A**2) : 19.42460
REMARK 3 B33 (A**2) : -38.84930
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 33275
REMARK 3 ANGLE : 1.292 45139
REMARK 3 CHIRALITY : 0.070 5276
REMARK 3 PLANARITY : 0.005 5606
REMARK 3 DIHEDRAL : 21.617 12385
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 4ADF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1290050791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9714
REMARK 200 MONOCHROMATOR : BARTELS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58151
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.400
REMARK 200 RESOLUTION RANGE LOW (A) : 75.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.81000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: PDB ENTRIES 2CH8, 3UF2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL, PH 8.50, 1.0 M
REMARK 280 AMMONIUM PHOSPHATE MONOBASIC
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.39000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 220.78000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 220.78000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 110.39000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 35730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 93500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, Y, Z, a, b, c, d
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 36350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 94650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R, S, T, U, V,
REMARK 350 AND CHAINS: W, X, e, f, g, h, i, j
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN M, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN N, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN O, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN P, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN Q, THR 169 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN R, THR 169 TO SER
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 161
REMARK 465 GLU A 162
REMARK 465 GLY A 163
REMARK 465 VAL A 164
REMARK 465 GLU A 165
REMARK 465 PRO A 166
REMARK 465 ALA A 167
REMARK 465 PRO A 168
REMARK 465 SER A 169
REMARK 465 ALA A 170
REMARK 465 ALA A 171
REMARK 465 SER A 220
REMARK 465 GLN A 221
REMARK 465 LYS A 222
REMARK 465 HIS A 223
REMARK 465 HIS A 224
REMARK 465 HIS A 225
REMARK 465 HIS A 226
REMARK 465 HIS A 227
REMARK 465 HIS A 228
REMARK 465 GLU B 162
REMARK 465 GLY B 163
REMARK 465 VAL B 164
REMARK 465 GLU B 165
REMARK 465 PRO B 166
REMARK 465 ALA B 167
REMARK 465 PRO B 168
REMARK 465 SER B 169
REMARK 465 ALA B 170
REMARK 465 ALA B 171
REMARK 465 ASN B 172
REMARK 465 GLN B 221
REMARK 465 LYS B 222
REMARK 465 HIS B 223
REMARK 465 HIS B 224
REMARK 465 HIS B 225
REMARK 465 HIS B 226
REMARK 465 HIS B 227
REMARK 465 HIS B 228
REMARK 465 PRO C 161
REMARK 465 GLU C 162
REMARK 465 GLY C 163
REMARK 465 VAL C 164
REMARK 465 GLU C 165
REMARK 465 PRO C 166
REMARK 465 ALA C 167
REMARK 465 PRO C 168
REMARK 465 SER C 169
REMARK 465 ALA C 170
REMARK 465 ALA C 171
REMARK 465 ASN C 172
REMARK 465 LEU C 219
REMARK 465 SER C 220
REMARK 465 GLN C 221
REMARK 465 LYS C 222
REMARK 465 HIS C 223
REMARK 465 HIS C 224
REMARK 465 HIS C 225
REMARK 465 HIS C 226
REMARK 465 HIS C 227
REMARK 465 HIS C 228
REMARK 465 PRO D 161
REMARK 465 GLU D 162
REMARK 465 GLY D 163
REMARK 465 VAL D 164
REMARK 465 GLU D 165
REMARK 465 PRO D 166
REMARK 465 ALA D 167
REMARK 465 PRO D 168
REMARK 465 SER D 169
REMARK 465 ALA D 170
REMARK 465 ALA D 171
REMARK 465 ASN D 172
REMARK 465 GLY D 173
REMARK 465 GLN D 221
REMARK 465 LYS D 222
REMARK 465 HIS D 223
REMARK 465 HIS D 224
REMARK 465 HIS D 225
REMARK 465 HIS D 226
REMARK 465 HIS D 227
REMARK 465 HIS D 228
REMARK 465 PRO E 161
REMARK 465 GLU E 162
REMARK 465 GLY E 163
REMARK 465 VAL E 164
REMARK 465 GLU E 165
REMARK 465 PRO E 166
REMARK 465 ALA E 167
REMARK 465 PRO E 168
REMARK 465 SER E 169
REMARK 465 ALA E 170
REMARK 465 ALA E 171
REMARK 465 ASN E 172
REMARK 465 SER E 220
REMARK 465 GLN E 221
REMARK 465 LYS E 222
REMARK 465 HIS E 223
REMARK 465 HIS E 224
REMARK 465 HIS E 225
REMARK 465 HIS E 226
REMARK 465 HIS E 227
REMARK 465 HIS E 228
REMARK 465 PRO F 161
REMARK 465 GLU F 162
REMARK 465 GLY F 163
REMARK 465 VAL F 164
REMARK 465 GLU F 165
REMARK 465 PRO F 166
REMARK 465 ALA F 167
REMARK 465 PRO F 168
REMARK 465 SER F 169
REMARK 465 ALA F 170
REMARK 465 SER F 220
REMARK 465 GLN F 221
REMARK 465 LYS F 222
REMARK 465 HIS F 223
REMARK 465 HIS F 224
REMARK 465 HIS F 225
REMARK 465 HIS F 226
REMARK 465 HIS F 227
REMARK 465 HIS F 228
REMARK 465 GLY G -3
REMARK 465 SER G -2
REMARK 465 HIS G -1
REMARK 465 MET G 0
REMARK 465 GLU G 1
REMARK 465 GLU G 2
REMARK 465 SER G 148
REMARK 465 GLN G 149
REMARK 465 GLY H -3
REMARK 465 SER H -2
REMARK 465 HIS H -1
REMARK 465 MET H 0
REMARK 465 GLU H 1
REMARK 465 GLU H 2
REMARK 465 VAL H 3
REMARK 465 SER H 4
REMARK 465 GLU H 5
REMARK 465 SER H 148
REMARK 465 GLN H 149
REMARK 465 GLY I -3
REMARK 465 SER I -2
REMARK 465 HIS I -1
REMARK 465 MET I 0
REMARK 465 GLU I 1
REMARK 465 GLU I 2
REMARK 465 VAL I 3
REMARK 465 SER I 4
REMARK 465 GLU I 5
REMARK 465 TYR I 6
REMARK 465 TYR I 95
REMARK 465 GLU I 96
REMARK 465 GLU I 97
REMARK 465 HIS I 98
REMARK 465 SER I 148
REMARK 465 GLN I 149
REMARK 465 GLY J -3
REMARK 465 SER J -2
REMARK 465 HIS J -1
REMARK 465 MET J 0
REMARK 465 GLU J 1
REMARK 465 GLU J 2
REMARK 465 VAL J 3
REMARK 465 SER J 4
REMARK 465 GLU J 5
REMARK 465 SER J 148
REMARK 465 GLN J 149
REMARK 465 GLY K -3
REMARK 465 SER K -2
REMARK 465 HIS K -1
REMARK 465 MET K 0
REMARK 465 GLU K 1
REMARK 465 GLU K 2
REMARK 465 VAL K 3
REMARK 465 SER K 147
REMARK 465 SER K 148
REMARK 465 GLN K 149
REMARK 465 GLY L -3
REMARK 465 SER L -2
REMARK 465 HIS L -1
REMARK 465 MET L 0
REMARK 465 GLU L 1
REMARK 465 GLU L 2
REMARK 465 VAL L 3
REMARK 465 SER L 4
REMARK 465 GLU L 5
REMARK 465 TYR L 6
REMARK 465 THR L 92
REMARK 465 LYS L 93
REMARK 465 ASP L 94
REMARK 465 TYR L 95
REMARK 465 GLU L 96
REMARK 465 SER L 147
REMARK 465 SER L 148
REMARK 465 GLN L 149
REMARK 465 GLU M 162
REMARK 465 GLY M 163
REMARK 465 VAL M 164
REMARK 465 GLU M 165
REMARK 465 PRO M 166
REMARK 465 ALA M 167
REMARK 465 PRO M 168
REMARK 465 SER M 169
REMARK 465 SER M 220
REMARK 465 GLN M 221
REMARK 465 LYS M 222
REMARK 465 HIS M 223
REMARK 465 HIS M 224
REMARK 465 HIS M 225
REMARK 465 HIS M 226
REMARK 465 HIS M 227
REMARK 465 HIS M 228
REMARK 465 VAL N 164
REMARK 465 GLU N 165
REMARK 465 PRO N 166
REMARK 465 ALA N 167
REMARK 465 PRO N 168
REMARK 465 SER N 169
REMARK 465 ALA N 170
REMARK 465 ALA N 171
REMARK 465 SER N 220
REMARK 465 GLN N 221
REMARK 465 LYS N 222
REMARK 465 HIS N 223
REMARK 465 HIS N 224
REMARK 465 HIS N 225
REMARK 465 HIS N 226
REMARK 465 HIS N 227
REMARK 465 HIS N 228
REMARK 465 GLU O 162
REMARK 465 GLY O 163
REMARK 465 VAL O 164
REMARK 465 GLU O 165
REMARK 465 PRO O 166
REMARK 465 ALA O 167
REMARK 465 PRO O 168
REMARK 465 SER O 169
REMARK 465 ALA O 170
REMARK 465 ALA O 171
REMARK 465 ASN O 172
REMARK 465 GLY O 173
REMARK 465 GLY O 174
REMARK 465 SER O 220
REMARK 465 GLN O 221
REMARK 465 LYS O 222
REMARK 465 HIS O 223
REMARK 465 HIS O 224
REMARK 465 HIS O 225
REMARK 465 HIS O 226
REMARK 465 HIS O 227
REMARK 465 HIS O 228
REMARK 465 GLU P 162
REMARK 465 GLY P 163
REMARK 465 VAL P 164
REMARK 465 GLU P 165
REMARK 465 PRO P 166
REMARK 465 ALA P 167
REMARK 465 PRO P 168
REMARK 465 SER P 169
REMARK 465 ALA P 170
REMARK 465 ALA P 171
REMARK 465 ASN P 172
REMARK 465 GLN P 221
REMARK 465 LYS P 222
REMARK 465 HIS P 223
REMARK 465 HIS P 224
REMARK 465 HIS P 225
REMARK 465 HIS P 226
REMARK 465 HIS P 227
REMARK 465 HIS P 228
REMARK 465 PRO Q 161
REMARK 465 GLU Q 162
REMARK 465 GLY Q 163
REMARK 465 VAL Q 164
REMARK 465 GLU Q 165
REMARK 465 PRO Q 166
REMARK 465 ALA Q 167
REMARK 465 PRO Q 168
REMARK 465 SER Q 169
REMARK 465 ALA Q 170
REMARK 465 ALA Q 171
REMARK 465 ASN Q 172
REMARK 465 GLY Q 173
REMARK 465 GLY Q 174
REMARK 465 SER Q 220
REMARK 465 GLN Q 221
REMARK 465 LYS Q 222
REMARK 465 HIS Q 223
REMARK 465 HIS Q 224
REMARK 465 HIS Q 225
REMARK 465 HIS Q 226
REMARK 465 HIS Q 227
REMARK 465 HIS Q 228
REMARK 465 PRO R 161
REMARK 465 GLU R 162
REMARK 465 GLY R 163
REMARK 465 VAL R 164
REMARK 465 GLU R 165
REMARK 465 PRO R 166
REMARK 465 ALA R 167
REMARK 465 PRO R 168
REMARK 465 SER R 169
REMARK 465 ALA R 170
REMARK 465 ALA R 171
REMARK 465 ASN R 172
REMARK 465 GLY R 173
REMARK 465 GLY R 174
REMARK 465 GLN R 221
REMARK 465 LYS R 222
REMARK 465 HIS R 223
REMARK 465 HIS R 224
REMARK 465 HIS R 225
REMARK 465 HIS R 226
REMARK 465 HIS R 227
REMARK 465 HIS R 228
REMARK 465 GLY S -3
REMARK 465 SER S -2
REMARK 465 HIS S -1
REMARK 465 MET S 0
REMARK 465 GLU S 1
REMARK 465 GLU S 2
REMARK 465 VAL S 3
REMARK 465 SER S 148
REMARK 465 GLN S 149
REMARK 465 GLY T -3
REMARK 465 SER T -2
REMARK 465 HIS T -1
REMARK 465 MET T 0
REMARK 465 GLU T 1
REMARK 465 GLU T 2
REMARK 465 VAL T 3
REMARK 465 SER T 4
REMARK 465 GLU T 5
REMARK 465 SER T 148
REMARK 465 GLN T 149
REMARK 465 GLY U -3
REMARK 465 SER U -2
REMARK 465 HIS U -1
REMARK 465 MET U 0
REMARK 465 GLU U 1
REMARK 465 GLU U 2
REMARK 465 VAL U 3
REMARK 465 SER U 148
REMARK 465 GLN U 149
REMARK 465 GLY V -3
REMARK 465 SER V -2
REMARK 465 HIS V -1
REMARK 465 MET V 0
REMARK 465 GLU V 1
REMARK 465 GLU V 2
REMARK 465 VAL V 3
REMARK 465 SER V 4
REMARK 465 TYR V 95
REMARK 465 GLU V 96
REMARK 465 SER V 148
REMARK 465 GLN V 149
REMARK 465 GLY W -3
REMARK 465 SER W -2
REMARK 465 HIS W -1
REMARK 465 MET W 0
REMARK 465 GLU W 1
REMARK 465 GLU W 2
REMARK 465 ASP W 94
REMARK 465 TYR W 95
REMARK 465 GLU W 96
REMARK 465 SER W 148
REMARK 465 GLN W 149
REMARK 465 GLY X -3
REMARK 465 SER X -2
REMARK 465 HIS X -1
REMARK 465 MET X 0
REMARK 465 GLU X 1
REMARK 465 GLU X 2
REMARK 465 VAL X 3
REMARK 465 ASP X 94
REMARK 465 TYR X 95
REMARK 465 GLU X 96
REMARK 465 GLU X 97
REMARK 465 HIS X 98
REMARK 465 SER X 148
REMARK 465 GLN X 149
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 ASN A 172 CG OD1 ND2
REMARK 470 LYS B 179 CG CD CE NZ
REMARK 470 LYS D 179 CG CD CE NZ
REMARK 470 LYS E 179 CG CD CE NZ
REMARK 470 ASN F 172 CG OD1 ND2
REMARK 470 LYS F 193 CG CD CE NZ
REMARK 470 GLU G 5 CG CD OE1 OE2
REMARK 470 TYR G 95 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS G 98 CG ND1 CD2 CE1 NE2
REMARK 470 LYS G 100 CG CD CE NZ
REMARK 470 LYS G 130 CG CD CE NZ
REMARK 470 GLN H 42 CG CD OE1 NE2
REMARK 470 TYR H 95 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN H 140 CG OD1 ND2
REMARK 470 GLU H 145 CG CD OE1 OE2
REMARK 470 LYS I 44 CG CD CE NZ
REMARK 470 ARG I 68 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 130 CG CD CE NZ
REMARK 470 TYR J 95 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS J 130 CG CD CE NZ
REMARK 470 ASN J 140 CG OD1 ND2
REMARK 470 LYS K 93 CG CD CE NZ
REMARK 470 TYR K 95 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS K 130 CG CD CE NZ
REMARK 470 LYS L 130 CG CD CE NZ
REMARK 470 LYS L 137 CG CD CE NZ
REMARK 470 ASN L 140 CG OD1 ND2
REMARK 470 ASN M 172 CG OD1 ND2
REMARK 470 LYS M 207 CG CD CE NZ
REMARK 470 LYS O 179 CG CD CE NZ
REMARK 470 LYS O 193 CG CD CE NZ
REMARK 470 LYS O 207 CG CD CE NZ
REMARK 470 LYS R 179 CG CD CE NZ
REMARK 470 LYS S 93 CG CD CE NZ
REMARK 470 HIS S 98 CG ND1 CD2 CE1 NE2
REMARK 470 LYS S 100 CG CD CE NZ
REMARK 470 LYS S 130 CG CD CE NZ
REMARK 470 LYS S 137 CG CD CE NZ
REMARK 470 TYR T 95 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS T 98 CG ND1 CD2 CE1 NE2
REMARK 470 ASN T 140 CG OD1 ND2
REMARK 470 LYS U 51 CG CD CE NZ
REMARK 470 TYR U 95 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU U 97 CG CD OE1 OE2
REMARK 470 LYS U 130 CG CD CE NZ
REMARK 470 GLU V 5 CG CD OE1 OE2
REMARK 470 ASN V 140 CG OD1 ND2
REMARK 470 GLU V 145 CG CD OE1 OE2
REMARK 470 LYS W 44 CG CD CE NZ
REMARK 470 LYS W 51 CG CD CE NZ
REMARK 470 GLU W 97 CG CD OE1 OE2
REMARK 470 HIS W 98 CG ND1 CD2 CE1 NE2
REMARK 470 ASP W 99 CG OD1 OD2
REMARK 470 LYS W 100 CG CD CE NZ
REMARK 470 LYS W 130 CG CD CE NZ
REMARK 470 ARG X 86 CG CD NE CZ NH1 NH2
REMARK 470 LYS X 100 CG CD CE NZ
REMARK 470 LYS X 130 CG CD CE NZ
REMARK 470 ASN X 140 CG OD1 ND2
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 MET A 160 CA - CB - CG ANGL. DEV. = 15.0 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 ALA A 84 -136.33 55.73
REMARK 500 GLU A 117 118.22 -161.96
REMARK 500 ASP A 206 -124.96 59.71
REMARK 500 ALA B 84 -136.48 55.67
REMARK 500 GLU B 117 118.70 -162.43
REMARK 500 ASP B 206 -125.11 59.50
REMARK 500 ALA C 84 -136.26 55.78
REMARK 500 GLU C 117 118.53 -162.77
REMARK 500 ASP C 206 -125.53 59.62
REMARK 500 ALA D 84 -136.26 55.77
REMARK 500 GLU D 117 119.14 -162.41
REMARK 500 ASP D 206 -125.25 59.81
REMARK 500 ALA E 84 -136.17 56.02
REMARK 500 GLU E 117 118.64 -162.73
REMARK 500 ASP E 206 -125.19 59.56
REMARK 500 ALA F 84 -136.37 55.81
REMARK 500 GLU F 117 118.75 -162.45
REMARK 500 ASP F 206 -124.93 59.50
REMARK 500 TYR G 6 17.12 83.03
REMARK 500 THR G 64 -70.82 -107.94
REMARK 500 CYS G 146 -85.80 -85.15
REMARK 500 THR H 64 -71.09 -107.95
REMARK 500 THR I 64 -70.85 -108.08
REMARK 500 CYS I 146 -82.98 -82.20
REMARK 500 THR J 64 -70.87 -108.00
REMARK 500 THR K 64 -70.66 -107.45
REMARK 500 THR L 64 -70.78 -108.19
REMARK 500 ALA M 84 -136.20 55.61
REMARK 500 GLU M 117 118.53 -162.45
REMARK 500 ASN M 172 68.93 -109.97
REMARK 500 ASP M 206 -125.18 59.64
REMARK 500 ALA N 84 -136.72 55.96
REMARK 500 GLU N 117 118.50 -161.92
REMARK 500 MET N 160 169.00 100.63
REMARK 500 ASP N 206 -125.36 59.87
REMARK 500 ALA O 84 -136.11 55.93
REMARK 500 GLU O 117 118.87 -161.97
REMARK 500 ASP O 206 -125.29 59.72
REMARK 500 ALA P 84 -136.56 55.79
REMARK 500 GLU P 117 118.71 -162.69
REMARK 500 ASP P 206 -125.23 59.74
REMARK 500 ALA Q 84 -136.27 55.79
REMARK 500 GLU Q 117 118.28 -162.94
REMARK 500 ASP Q 206 -125.38 59.59
REMARK 500 ALA R 84 -136.47 55.90
REMARK 500 GLU R 117 118.48 -162.51
REMARK 500 ASP R 206 -125.28 59.67
REMARK 500 THR S 64 -70.89 -108.12
REMARK 500 THR T 64 -70.51 -108.00
REMARK 500 CYS T 146 -85.74 -85.40
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HMC RELATED DB: PDB
REMARK 900 HUMAN MACROPHAGE COLONY STIMULATING FACTOR (ALPHA FORM, SOLUBLE)
DBREF 4ADF A 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF B 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF C 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF D 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF E 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF F 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF G 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF H 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF I 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF J 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF K 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF L 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF M 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF N 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF O 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF P 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF Q 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF R 21 221 UNP P0CW72 BARF1_EBVG 21 221
DBREF 4ADF S 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF T 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF U 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF V 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF W 1 149 UNP P09603 CSF1_HUMAN 33 181
DBREF 4ADF X 1 149 UNP P09603 CSF1_HUMAN 33 181
SEQADV 4ADF LYS A 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS A 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS A 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS A 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS A 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS A 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS A 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER A 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS B 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS B 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS B 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS B 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS B 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS B 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS B 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER B 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS C 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS C 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS C 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS C 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS C 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS C 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS C 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER C 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS D 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS D 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS D 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS D 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS D 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS D 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS D 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER D 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS E 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS E 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS E 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS E 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS E 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS E 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS E 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER E 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS F 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS F 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS F 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS F 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS F 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS F 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS F 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER F 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF GLY G -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER G -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS G -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET G 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY H -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER H -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS H -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET H 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY I -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER I -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS I -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET I 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY J -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER J -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS J -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET J 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY K -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER K -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS K -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET K 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY L -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER L -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS L -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET L 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF LYS M 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS M 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS M 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS M 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS M 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS M 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS M 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER M 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS N 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS N 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS N 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS N 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS N 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS N 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS N 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER N 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS O 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS O 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS O 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS O 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS O 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS O 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS O 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER O 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS P 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS P 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS P 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS P 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS P 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS P 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS P 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER P 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS Q 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS Q 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS Q 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS Q 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS Q 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS Q 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS Q 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER Q 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF LYS R 222 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS R 223 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS R 224 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS R 225 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS R 226 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS R 227 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF HIS R 228 UNP P0CW72 EXPRESSION TAG
SEQADV 4ADF SER R 169 UNP P0CW72 THR 169 ENGINEERED MUTATION
SEQADV 4ADF GLY S -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER S -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS S -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET S 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY T -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER T -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS T -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET T 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY U -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER U -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS U -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET U 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY V -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER V -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS V -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET V 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY W -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER W -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS W -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET W 0 UNP P09603 EXPRESSION TAG
SEQADV 4ADF GLY X -3 UNP P09603 EXPRESSION TAG
SEQADV 4ADF SER X -2 UNP P09603 EXPRESSION TAG
SEQADV 4ADF HIS X -1 UNP P09603 EXPRESSION TAG
SEQADV 4ADF MET X 0 UNP P09603 EXPRESSION TAG
SEQRES 1 A 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 A 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 A 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 A 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 A 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 A 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 A 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 A 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 A 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 A 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 A 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 A 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 A 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 A 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 A 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 A 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 B 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 B 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 B 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 B 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 B 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 B 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 B 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 B 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 B 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 B 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 B 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 B 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 B 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 B 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 B 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 C 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 C 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 C 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 C 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 C 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 C 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 C 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 C 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 C 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 C 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 C 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 C 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 C 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 C 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 C 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 D 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 D 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 D 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 D 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 D 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 D 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 D 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 D 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 D 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 D 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 D 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 D 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 D 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 D 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 D 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 E 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 E 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 E 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 E 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 E 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 E 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 E 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 E 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 E 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 E 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 E 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 E 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 E 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 E 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 E 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 E 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 F 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 F 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 F 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 F 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 F 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 F 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 F 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 F 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 F 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 F 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 F 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 F 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 F 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 F 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 F 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 F 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 G 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 G 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 G 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 G 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 G 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 G 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 G 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 G 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 G 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 G 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 G 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 G 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 H 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 H 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 H 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 H 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 H 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 H 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 H 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 H 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 H 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 H 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 H 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 H 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 I 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 I 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 I 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 I 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 I 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 I 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 I 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 I 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 I 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 I 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 I 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 I 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 J 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 J 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 J 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 J 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 J 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 J 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 J 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 J 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 J 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 J 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 J 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 J 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 K 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 K 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 K 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 K 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 K 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 K 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 K 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 K 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 K 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 K 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 K 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 K 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 L 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 L 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 L 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 L 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 L 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 L 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 L 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 L 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 L 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 L 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 L 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 L 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 M 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 M 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 M 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 M 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 M 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 M 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 M 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 M 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 M 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 M 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 M 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 M 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 M 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 M 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 M 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 M 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 N 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 N 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 N 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 N 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 N 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 N 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 N 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 N 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 N 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 N 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 N 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 N 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 N 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 N 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 N 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 N 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 O 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 O 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 O 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 O 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 O 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 O 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 O 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 O 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 O 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 O 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 O 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 O 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 O 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 O 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 O 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 O 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 P 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 P 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 P 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 P 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 P 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 P 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 P 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 P 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 P 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 P 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 P 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 P 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 P 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 P 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 P 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 P 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 Q 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 Q 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 Q 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 Q 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 Q 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 Q 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 Q 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 Q 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 Q 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 Q 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 Q 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 Q 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 Q 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 Q 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 Q 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 Q 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 R 208 VAL THR ALA PHE LEU GLY GLU ARG VAL THR LEU THR SER
SEQRES 2 R 208 TYR TRP ARG ARG VAL SER LEU GLY PRO GLU ILE GLU VAL
SEQRES 3 R 208 SER TRP PHE LYS LEU GLY PRO GLY GLU GLU GLN VAL LEU
SEQRES 4 R 208 ILE GLY ARG MET HIS HIS ASP VAL ILE PHE ILE GLU TRP
SEQRES 5 R 208 PRO PHE ARG GLY PHE PHE ASP ILE HIS ARG SER ALA ASN
SEQRES 6 R 208 THR PHE PHE LEU VAL VAL THR ALA ALA ASN ILE SER HIS
SEQRES 7 R 208 ASP GLY ASN TYR LEU CYS ARG MET LYS LEU GLY GLU THR
SEQRES 8 R 208 GLU VAL THR LYS GLN GLU HIS LEU SER VAL VAL LYS PRO
SEQRES 9 R 208 LEU THR LEU SER VAL HIS SER GLU ARG SER GLN PHE PRO
SEQRES 10 R 208 ASP PHE SER VAL LEU THR VAL THR CYS THR VAL ASN ALA
SEQRES 11 R 208 PHE PRO HIS PRO HIS VAL GLN TRP LEU MET PRO GLU GLY
SEQRES 12 R 208 VAL GLU PRO ALA PRO SER ALA ALA ASN GLY GLY VAL MET
SEQRES 13 R 208 LYS GLU LYS ASP GLY SER LEU SER VAL ALA VAL ASP LEU
SEQRES 14 R 208 SER LEU PRO LYS PRO TRP HIS LEU PRO VAL THR CYS VAL
SEQRES 15 R 208 GLY LYS ASN ASP LYS GLU GLU ALA HIS GLY VAL TYR VAL
SEQRES 16 R 208 SER GLY TYR LEU SER GLN LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 S 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 S 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 S 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 S 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 S 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 S 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 S 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 S 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 S 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 S 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 S 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 S 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 T 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 T 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 T 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 T 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 T 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 T 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 T 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 T 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 T 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 T 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 T 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 T 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 U 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 U 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 U 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 U 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 U 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 U 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 U 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 U 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 U 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 U 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 U 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 U 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 V 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 V 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 V 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 V 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 V 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 V 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 V 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 V 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 V 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 V 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 V 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 V 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 W 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 W 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 W 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 W 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 W 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 W 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 W 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 W 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 W 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 W 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 W 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 W 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
SEQRES 1 X 153 GLY SER HIS MET GLU GLU VAL SER GLU TYR CYS SER HIS
SEQRES 2 X 153 MET ILE GLY SER GLY HIS LEU GLN SER LEU GLN ARG LEU
SEQRES 3 X 153 ILE ASP SER GLN MET GLU THR SER CYS GLN ILE THR PHE
SEQRES 4 X 153 GLU PHE VAL ASP GLN GLU GLN LEU LYS ASP PRO VAL CYS
SEQRES 5 X 153 TYR LEU LYS LYS ALA PHE LEU LEU VAL GLN ASP ILE MET
SEQRES 6 X 153 GLU ASP THR MET ARG PHE ARG ASP ASN THR PRO ASN ALA
SEQRES 7 X 153 ILE ALA ILE VAL GLN LEU GLN GLU LEU SER LEU ARG LEU
SEQRES 8 X 153 LYS SER CYS PHE THR LYS ASP TYR GLU GLU HIS ASP LYS
SEQRES 9 X 153 ALA CYS VAL ARG THR PHE TYR GLU THR PRO LEU GLN LEU
SEQRES 10 X 153 LEU GLU LYS VAL LYS ASN VAL PHE ASN GLU THR LYS ASN
SEQRES 11 X 153 LEU LEU ASP LYS ASP TRP ASN ILE PHE SER LYS ASN CYS
SEQRES 12 X 153 ASN ASN SER PHE ALA GLU CYS SER SER GLN
MODRES 4ADF ASN A 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN B 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN C 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN D 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN E 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN F 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN M 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN N 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN O 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN P 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN Q 95 ASN GLYCOSYLATION SITE
MODRES 4ADF ASN R 95 ASN GLYCOSYLATION SITE
HET NAG Y 1 14
HET NAG Y 2 14
HET BMA Y 3 11
HET MAN Y 4 11
HET MAN Y 5 11
HET MAN Y 6 11
HET NAG Z 1 14
HET NAG Z 2 14
HET BMA Z 3 11
HET MAN Z 4 11
HET MAN Z 5 11
HET MAN Z 6 11
HET MAN Z 7 11
HET NAG a 1 14
HET NAG a 2 14
HET BMA a 3 11
HET MAN a 4 11
HET MAN a 5 11
HET MAN a 6 11
HET MAN a 7 11
HET NAG b 1 14
HET NAG b 2 14
HET BMA b 3 11
HET MAN b 4 11
HET MAN b 5 11
HET NAG c 1 14
HET NAG c 2 14
HET BMA c 3 11
HET MAN c 4 11
HET MAN c 5 11
HET NAG d 1 14
HET NAG d 2 14
HET BMA d 3 11
HET MAN d 4 11
HET MAN d 5 11
HET NAG e 1 14
HET NAG e 2 14
HET BMA e 3 11
HET MAN e 4 11
HET MAN e 5 11
HET MAN e 6 11
HET NAG f 1 14
HET NAG f 2 14
HET BMA f 3 11
HET MAN f 4 11
HET MAN f 5 11
HET MAN f 6 11
HET NAG g 1 14
HET NAG g 2 14
HET BMA g 3 11
HET MAN g 4 11
HET MAN g 5 11
HET NAG h 1 14
HET NAG h 2 14
HET BMA h 3 11
HET MAN h 4 11
HET MAN h 5 11
HET MAN h 6 11
HET NAG i 1 14
HET NAG i 2 14
HET BMA i 3 11
HET MAN i 4 11
HET MAN i 5 11
HET MAN i 6 11
HET MAN i 7 11
HET NAG j 1 14
HET NAG j 2 14
HET BMA j 3 11
HET MAN j 4 11
HET MAN j 5 11
HET MAN j 6 11
HET MAN j 7 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 25 NAG 24(C8 H15 N O6)
FORMUL 25 BMA 12(C6 H12 O6)
FORMUL 25 MAN 36(C6 H12 O6)
HELIX 1 1 ASN A 95 ASP A 99 5 5
HELIX 2 2 ASN B 95 ASP B 99 5 5
HELIX 3 3 ASN C 95 ASP C 99 5 5
HELIX 4 4 ASN D 95 ASP D 99 5 5
HELIX 5 5 ASN E 95 ASP E 99 5 5
HELIX 6 6 ASN F 95 ASP F 99 5 5
HELIX 7 7 TYR G 6 MET G 10 5 5
HELIX 8 8 GLY G 12 GLN G 26 1 15
HELIX 9 9 ASP G 45 THR G 64 1 20
HELIX 10 10 THR G 71 LYS G 88 1 18
HELIX 11 11 SER G 89 PHE G 91 5 3
HELIX 12 12 TYR G 95 ASP G 99 5 5
HELIX 13 13 THR G 109 ASP G 131 1 23
HELIX 14 14 TRP G 132 LYS G 137 5 6
HELIX 15 15 CYS G 139 GLU G 145 1 7
HELIX 16 16 TYR H 6 MET H 10 5 5
HELIX 17 17 GLY H 12 GLN H 26 1 15
HELIX 18 18 ASP H 45 THR H 64 1 20
HELIX 19 19 THR H 71 LYS H 88 1 18
HELIX 20 20 SER H 89 PHE H 91 5 3
HELIX 21 21 TYR H 95 ASP H 99 5 5
HELIX 22 22 THR H 109 ASP H 131 1 23
HELIX 23 23 TRP H 132 LYS H 137 5 6
HELIX 24 24 CYS H 139 GLU H 145 1 7
HELIX 25 25 GLY I 12 GLN I 26 1 15
HELIX 26 26 ASP I 45 THR I 64 1 20
HELIX 27 27 THR I 71 LYS I 88 1 18
HELIX 28 28 SER I 89 PHE I 91 5 3
HELIX 29 29 THR I 109 ASP I 131 1 23
HELIX 30 30 TRP I 132 LYS I 137 5 6
HELIX 31 31 CYS I 139 GLU I 145 1 7
HELIX 32 32 TYR J 6 MET J 10 5 5
HELIX 33 33 GLY J 12 GLN J 26 1 15
HELIX 34 34 ASP J 45 THR J 64 1 20
HELIX 35 35 THR J 71 LYS J 88 1 18
HELIX 36 36 SER J 89 PHE J 91 5 3
HELIX 37 37 TYR J 95 ASP J 99 5 5
HELIX 38 38 THR J 109 ASP J 131 1 23
HELIX 39 39 TRP J 132 LYS J 137 5 6
HELIX 40 40 CYS J 139 GLU J 145 1 7
HELIX 41 41 TYR K 6 MET K 10 5 5
HELIX 42 42 GLY K 12 GLN K 26 1 15
HELIX 43 43 ASP K 45 THR K 64 1 20
HELIX 44 44 THR K 71 LYS K 88 1 18
HELIX 45 45 SER K 89 PHE K 91 5 3
HELIX 46 46 TYR K 95 ASP K 99 5 5
HELIX 47 47 THR K 109 ASP K 131 1 23
HELIX 48 48 TRP K 132 LYS K 137 5 6
HELIX 49 49 CYS K 139 GLU K 145 1 7
HELIX 50 50 GLY L 12 GLN L 26 1 15
HELIX 51 51 ASP L 45 THR L 64 1 20
HELIX 52 52 THR L 71 LYS L 88 1 18
HELIX 53 53 SER L 89 PHE L 91 5 3
HELIX 54 54 THR L 109 ASP L 131 1 23
HELIX 55 55 TRP L 132 LYS L 137 5 6
HELIX 56 56 CYS L 139 GLU L 145 1 7
HELIX 57 57 ASN M 95 ASP M 99 5 5
HELIX 58 58 ASN N 95 ASP N 99 5 5
HELIX 59 59 ASN O 95 ASP O 99 5 5
HELIX 60 60 ASN P 95 ASP P 99 5 5
HELIX 61 61 ASN Q 95 ASP Q 99 5 5
HELIX 62 62 ASN R 95 ASP R 99 5 5
HELIX 63 63 TYR S 6 MET S 10 5 5
HELIX 64 64 GLY S 12 GLN S 26 1 15
HELIX 65 65 ASP S 45 THR S 64 1 20
HELIX 66 66 THR S 71 LYS S 88 1 18
HELIX 67 67 SER S 89 PHE S 91 5 3
HELIX 68 68 TYR S 95 ASP S 99 5 5
HELIX 69 69 THR S 109 ASP S 131 1 23
HELIX 70 70 TRP S 132 LYS S 137 5 6
HELIX 71 71 CYS S 139 GLU S 145 1 7
HELIX 72 72 TYR T 6 MET T 10 5 5
HELIX 73 73 GLY T 12 GLN T 26 1 15
HELIX 74 74 ASP T 45 THR T 64 1 20
HELIX 75 75 THR T 71 LYS T 88 1 18
HELIX 76 76 SER T 89 PHE T 91 5 3
HELIX 77 77 TYR T 95 ASP T 99 5 5
HELIX 78 78 THR T 109 ASP T 131 1 23
HELIX 79 79 TRP T 132 LYS T 137 5 6
HELIX 80 80 CYS T 139 GLU T 145 1 7
HELIX 81 81 TYR U 6 MET U 10 5 5
HELIX 82 82 GLY U 12 GLN U 26 1 15
HELIX 83 83 ASP U 45 THR U 64 1 20
HELIX 84 84 THR U 71 LYS U 88 1 18
HELIX 85 85 SER U 89 PHE U 91 5 3
HELIX 86 86 TYR U 95 ASP U 99 5 5
HELIX 87 87 THR U 109 ASP U 131 1 23
HELIX 88 88 TRP U 132 LYS U 137 5 6
HELIX 89 89 CYS U 139 GLU U 145 1 7
HELIX 90 90 TYR V 6 MET V 10 5 5
HELIX 91 91 GLY V 12 GLN V 26 1 15
HELIX 92 92 ASP V 45 THR V 64 1 20
HELIX 93 93 THR V 71 LYS V 88 1 18
HELIX 94 94 SER V 89 PHE V 91 5 3
HELIX 95 95 THR V 109 ASP V 131 1 23
HELIX 96 96 TRP V 132 LYS V 137 5 6
HELIX 97 97 CYS V 139 GLU V 145 1 7
HELIX 98 98 GLY W 12 GLN W 26 1 15
HELIX 99 99 ASP W 45 THR W 64 1 20
HELIX 100 100 THR W 71 LYS W 88 1 18
HELIX 101 101 SER W 89 PHE W 91 5 3
HELIX 102 102 THR W 109 ASP W 131 1 23
HELIX 103 103 TRP W 132 LYS W 137 5 6
HELIX 104 104 CYS W 139 GLU W 145 1 7
HELIX 105 105 TYR X 6 MET X 10 5 5
HELIX 106 106 GLY X 12 GLN X 26 1 15
HELIX 107 107 ASP X 45 THR X 64 1 20
HELIX 108 108 THR X 71 LYS X 88 1 18
HELIX 109 109 SER X 89 PHE X 91 5 3
HELIX 110 110 THR X 109 ASP X 131 1 23
HELIX 111 111 TRP X 132 LYS X 137 5 6
HELIX 112 112 CYS X 139 GLU X 145 1 7
SHEET 1 AA 2 THR A 22 PHE A 24 0
SHEET 2 AA 2 THR A 111 ARG A 133 -1 O SER A 120 N ALA A 23
SHEET 1 AB 8 ILE A 68 ILE A 70 0
SHEET 2 AB 8 VAL A 58 MET A 63 1 O ARG A 62 N PHE A 69
SHEET 3 AB 8 GLU A 45 LYS A 50 -1 O VAL A 46 N MET A 63
SHEET 4 AB 8 GLY A 100 LEU A 108 1 O LEU A 103 N PHE A 49
SHEET 5 AB 8 THR A 111 ARG A 133 -1 O THR A 111 N LEU A 108
SHEET 6 AB 8 LEU A 142 PHE A 151 1 O THR A 143 N GLU A 132
SHEET 7 AB 8 LEU A 183 LEU A 191 1 O LEU A 183 N ALA A 150
SHEET 8 AB 8 GLY A 174 LYS A 177 1 N GLY A 174 O ALA A 186
SHEET 1 AC 9 ILE A 68 ILE A 70 0
SHEET 2 AC 9 VAL A 58 MET A 63 1 O ARG A 62 N PHE A 69
SHEET 3 AC 9 GLU A 45 LYS A 50 -1 O VAL A 46 N MET A 63
SHEET 4 AC 9 GLY A 100 LEU A 108 1 O LEU A 103 N PHE A 49
SHEET 5 AC 9 THR A 111 ARG A 133 -1 O THR A 111 N LEU A 108
SHEET 6 AC 9 THR N 111 ARG N 133 -1 O GLU N 112 N GLU A 112
SHEET 7 AC 9 LEU N 142 PHE N 151 -1 O THR N 143 N GLU N 132
SHEET 8 AC 9 LEU N 183 LEU N 191 -1 O LEU N 183 N ALA N 150
SHEET 9 AC 9 GLY N 173 LYS N 177 -1 N GLY N 174 O ALA N 186
SHEET 1 AD 6 ILE A 68 ILE A 70 0
SHEET 2 AD 6 VAL A 58 MET A 63 1 O ARG A 62 N PHE A 69
SHEET 3 AD 6 GLU A 45 LYS A 50 -1 O VAL A 46 N MET A 63
SHEET 4 AD 6 GLY A 100 LEU A 108 1 O LEU A 103 N PHE A 49
SHEET 5 AD 6 THR A 111 ARG A 133 -1 O THR A 111 N LEU A 108
SHEET 6 AD 6 THR A 22 PHE A 24 -1 O ALA A 23 N VAL A 122
SHEET 1 DA 2 THR D 22 PHE D 24 0
SHEET 2 DA 2 THR D 111 ARG D 133 -1 O SER D 120 N ALA D 23
SHEET 1 AE10 ILE A 68 ILE A 70 0
SHEET 2 AE10 VAL A 58 MET A 63 1 O ARG A 62 N PHE A 69
SHEET 3 AE10 GLU A 45 LYS A 50 -1 O VAL A 46 N MET A 63
SHEET 4 AE10 GLY A 100 LEU A 108 1 O LEU A 103 N PHE A 49
SHEET 5 AE10 THR A 111 ARG A 133 -1 O THR A 111 N LEU A 108
SHEET 6 AE10 THR N 111 ARG N 133 -1 O GLU N 112 N GLU A 112
SHEET 7 AE10 GLY N 100 LEU N 108 1 O GLY N 100 N LEU N 119
SHEET 8 AE10 GLU N 45 LYS N 50 1 O GLU N 45 N LYS N 107
SHEET 9 AE10 VAL N 58 MET N 63 1 O VAL N 58 N LYS N 50
SHEET 10 AE10 ILE N 68 ILE N 70 1 O PHE N 69 N ARG N 62
SHEET 1 AF 7 ILE A 68 ILE A 70 0
SHEET 2 AF 7 VAL A 58 MET A 63 1 O ARG A 62 N PHE A 69
SHEET 3 AF 7 GLU A 45 LYS A 50 -1 O VAL A 46 N MET A 63
SHEET 4 AF 7 GLY A 100 LEU A 108 1 O LEU A 103 N PHE A 49
SHEET 5 AF 7 THR A 111 ARG A 133 -1 O THR A 111 N LEU A 108
SHEET 6 AF 7 THR N 111 ARG N 133 -1 O GLU N 112 N GLU A 112
SHEET 7 AF 7 THR N 22 PHE N 24 1 O ALA N 23 N VAL N 122
SHEET 1 DB 8 ILE D 68 ILE D 70 0
SHEET 2 DB 8 VAL D 58 MET D 63 -1 O ARG D 62 N PHE D 69
SHEET 3 DB 8 GLU D 45 LYS D 50 -1 O VAL D 46 N MET D 63
SHEET 4 DB 8 GLY D 100 LEU D 108 -1 O LEU D 103 N PHE D 49
SHEET 5 DB 8 THR D 111 ARG D 133 -1 O THR D 111 N LEU D 108
SHEET 6 DB 8 LEU D 142 PHE D 151 1 O THR D 143 N GLU D 132
SHEET 7 DB 8 LEU D 183 LEU D 191 1 O LEU D 183 N ALA D 150
SHEET 8 DB 8 VAL D 175 LYS D 177 1 O MET D 176 N SER D 184
SHEET 1 DC 6 ILE D 68 ILE D 70 0
SHEET 2 DC 6 VAL D 58 MET D 63 -1 O ARG D 62 N PHE D 69
SHEET 3 DC 6 GLU D 45 LYS D 50 -1 O VAL D 46 N MET D 63
SHEET 4 DC 6 GLY D 100 LEU D 108 -1 O LEU D 103 N PHE D 49
SHEET 5 DC 6 THR D 111 ARG D 133 -1 O THR D 111 N LEU D 108
SHEET 6 DC 6 THR D 22 PHE D 24 -1 O ALA D 23 N VAL D 122
SHEET 1 RA 2 THR R 22 PHE R 24 0
SHEET 2 RA 2 THR R 111 ARG R 133 1 O SER R 120 N ALA R 23
SHEET 1 DD 9 ILE D 68 ILE D 70 0
SHEET 2 DD 9 VAL D 58 MET D 63 -1 O ARG D 62 N PHE D 69
SHEET 3 DD 9 GLU D 45 LYS D 50 -1 O VAL D 46 N MET D 63
SHEET 4 DD 9 GLY D 100 LEU D 108 -1 O LEU D 103 N PHE D 49
SHEET 5 DD 9 THR D 111 ARG D 133 -1 O THR D 111 N LEU D 108
SHEET 6 DD 9 THR A 111 ARG A 133 1 O LEU A 127 N VAL D 129
SHEET 7 DD 9 LEU A 142 PHE A 151 1 O THR A 143 N GLU A 132
SHEET 8 DD 9 LEU A 183 LEU A 191 1 O LEU A 183 N ALA A 150
SHEET 9 DD 9 GLY A 174 LYS A 177 1 N GLY A 174 O ALA A 186
SHEET 1 DE10 ILE D 68 ILE D 70 0
SHEET 2 DE10 VAL D 58 MET D 63 -1 O ARG D 62 N PHE D 69
SHEET 3 DE10 GLU D 45 LYS D 50 -1 O VAL D 46 N MET D 63
SHEET 4 DE10 GLY D 100 LEU D 108 -1 O LEU D 103 N PHE D 49
SHEET 5 DE10 THR D 111 ARG D 133 -1 O THR D 111 N LEU D 108
SHEET 6 DE10 THR A 111 ARG A 133 1 O LEU A 127 N VAL D 129
SHEET 7 DE10 THR N 111 ARG N 133 -1 O GLU N 112 N GLU A 112
SHEET 8 DE10 LEU N 142 PHE N 151 -1 O THR N 143 N GLU N 132
SHEET 9 DE10 LEU N 183 LEU N 191 -1 O LEU N 183 N ALA N 150
SHEET 10 DE10 GLY N 173 LYS N 177 -1 N GLY N 174 O ALA N 186
SHEET 1 DF10 ILE D 68 ILE D 70 0
SHEET 2 DF10 VAL D 58 MET D 63 -1 O ARG D 62 N PHE D 69
SHEET 3 DF10 GLU D 45 LYS D 50 -1 O VAL D 46 N MET D 63
SHEET 4 DF10 GLY D 100 LEU D 108 -1 O LEU D 103 N PHE D 49
SHEET 5 DF10 THR D 111 ARG D 133 -1 O THR D 111 N LEU D 108
SHEET 6 DF10 THR A 111 ARG A 133 1 O LEU A 127 N VAL D 129
SHEET 7 DF10 GLY A 100 LEU A 108 -1 O GLY A 100 N LEU A 119
SHEET 8 DF10 GLU A 45 LYS A 50 -1 O GLU A 45 N LYS A 107
SHEET 9 DF10 VAL A 58 MET A 63 1 O VAL A 58 N LYS A 50
SHEET 10 DF10 ILE A 68 ILE A 70 1 O PHE A 69 N ARG A 62
SHEET 1 DG11 ILE D 68 ILE D 70 0
SHEET 2 DG11 VAL D 58 MET D 63 -1 O ARG D 62 N PHE D 69
SHEET 3 DG11 GLU D 45 LYS D 50 -1 O VAL D 46 N MET D 63
SHEET 4 DG11 GLY D 100 LEU D 108 -1 O LEU D 103 N PHE D 49
SHEET 5 DG11 THR D 111 ARG D 133 -1 O THR D 111 N LEU D 108
SHEET 6 DG11 THR A 111 ARG A 133 1 O LEU A 127 N VAL D 129
SHEET 7 DG11 THR N 111 ARG N 133 -1 O GLU N 112 N GLU A 112
SHEET 8 DG11 GLY N 100 LEU N 108 1 O GLY N 100 N LEU N 119
SHEET 9 DG11 GLU N 45 LYS N 50 1 O GLU N 45 N LYS N 107
SHEET 10 DG11 VAL N 58 MET N 63 1 O VAL N 58 N LYS N 50
SHEET 11 DG11 ILE N 68 ILE N 70 1 O PHE N 69 N ARG N 62
SHEET 1 DH 8 ILE D 68 ILE D 70 0
SHEET 2 DH 8 VAL D 58 MET D 63 -1 O ARG D 62 N PHE D 69
SHEET 3 DH 8 GLU D 45 LYS D 50 -1 O VAL D 46 N MET D 63
SHEET 4 DH 8 GLY D 100 LEU D 108 -1 O LEU D 103 N PHE D 49
SHEET 5 DH 8 THR D 111 ARG D 133 -1 O THR D 111 N LEU D 108
SHEET 6 DH 8 THR A 111 ARG A 133 1 O LEU A 127 N VAL D 129
SHEET 7 DH 8 THR N 111 ARG N 133 -1 O GLU N 112 N GLU A 112
SHEET 8 DH 8 THR N 22 PHE N 24 1 O ALA N 23 N VAL N 122
SHEET 1 RB 8 ILE R 68 ILE R 70 0
SHEET 2 RB 8 VAL R 58 MET R 63 -1 O ARG R 62 N PHE R 69
SHEET 3 RB 8 GLU R 45 LYS R 50 -1 O VAL R 46 N MET R 63
SHEET 4 RB 8 GLY R 100 LEU R 108 -1 O LEU R 103 N PHE R 49
SHEET 5 RB 8 THR R 111 ARG R 133 1 O THR R 111 N LEU R 108
SHEET 6 RB 8 LEU R 142 PHE R 151 1 O THR R 143 N GLU R 132
SHEET 7 RB 8 LEU R 183 LEU R 191 -1 O LEU R 183 N ALA R 150
SHEET 8 RB 8 MET R 176 LYS R 177 -1 O MET R 176 N SER R 184
SHEET 1 RC 6 ILE R 68 ILE R 70 0
SHEET 2 RC 6 VAL R 58 MET R 63 -1 O ARG R 62 N PHE R 69
SHEET 3 RC 6 GLU R 45 LYS R 50 -1 O VAL R 46 N MET R 63
SHEET 4 RC 6 GLY R 100 LEU R 108 -1 O LEU R 103 N PHE R 49
SHEET 5 RC 6 THR R 111 ARG R 133 1 O THR R 111 N LEU R 108
SHEET 6 RC 6 THR R 22 PHE R 24 -1 O ALA R 23 N VAL R 122
SHEET 1 AG 3 VAL A 29 TYR A 34 0
SHEET 2 AG 3 THR A 86 VAL A 91 -1 O PHE A 87 N SER A 33
SHEET 3 AG 3 PHE A 78 SER A 83 -1 O ASP A 79 N VAL A 90
SHEET 1 AH 6 PRO A 154 TRP A 158 0
SHEET 2 AH 6 VAL A 199 ASN A 205 -1 O VAL A 202 N GLN A 157
SHEET 3 AH 6 GLU A 208 SER A 216 -1 O GLU A 208 N ASN A 205
SHEET 4 AH 6 GLU D 208 SER D 216 -1 O GLU D 209 N VAL A 215
SHEET 5 AH 6 VAL D 199 ASN D 205 -1 O VAL D 199 N TYR D 214
SHEET 6 AH 6 PRO D 154 TRP D 158 -1 O HIS D 155 N LYS D 204
SHEET 1 BA 2 THR B 22 PHE B 24 0
SHEET 2 BA 2 THR B 111 ARG B 133 1 O SER B 120 N ALA B 23
SHEET 1 BB 9 ILE B 68 ILE B 70 0
SHEET 2 BB 9 VAL B 58 MET B 63 -1 O ARG B 62 N PHE B 69
SHEET 3 BB 9 GLU B 45 LYS B 50 -1 O VAL B 46 N MET B 63
SHEET 4 BB 9 GLY B 100 LEU B 108 -1 O LEU B 103 N PHE B 49
SHEET 5 BB 9 THR B 111 ARG B 133 -1 O THR B 111 N LEU B 108
SHEET 6 BB 9 THR F 111 ARG F 133 -1 O LEU F 125 N SER B 131
SHEET 7 BB 9 LEU F 142 PHE F 151 -1 O THR F 143 N GLU F 132
SHEET 8 BB 9 LEU F 183 LEU F 191 -1 O LEU F 183 N ALA F 150
SHEET 9 BB 9 GLY F 173 LYS F 177 -1 N GLY F 174 O ALA F 186
SHEET 1 BC 8 ILE B 68 ILE B 70 0
SHEET 2 BC 8 VAL B 58 MET B 63 -1 O ARG B 62 N PHE B 69
SHEET 3 BC 8 GLU B 45 LYS B 50 -1 O VAL B 46 N MET B 63
SHEET 4 BC 8 GLY B 100 LEU B 108 -1 O LEU B 103 N PHE B 49
SHEET 5 BC 8 THR B 111 ARG B 133 -1 O THR B 111 N LEU B 108
SHEET 6 BC 8 LEU B 142 PHE B 151 1 O THR B 143 N GLU B 132
SHEET 7 BC 8 LEU B 183 LEU B 191 -1 O LEU B 183 N ALA B 150
SHEET 8 BC 8 GLY B 174 LYS B 177 -1 N GLY B 174 O ALA B 186
SHEET 1 BD 6 ILE B 68 ILE B 70 0
SHEET 2 BD 6 VAL B 58 MET B 63 -1 O ARG B 62 N PHE B 69
SHEET 3 BD 6 GLU B 45 LYS B 50 -1 O VAL B 46 N MET B 63
SHEET 4 BD 6 GLY B 100 LEU B 108 -1 O LEU B 103 N PHE B 49
SHEET 5 BD 6 THR B 111 ARG B 133 -1 O THR B 111 N LEU B 108
SHEET 6 BD 6 THR B 22 PHE B 24 1 O ALA B 23 N VAL B 122
SHEET 1 FA 2 THR F 22 PHE F 24 0
SHEET 2 FA 2 THR F 111 ARG F 133 -1 O SER F 120 N ALA F 23
SHEET 1 BE10 ILE B 68 ILE B 70 0
SHEET 2 BE10 VAL B 58 MET B 63 -1 O ARG B 62 N PHE B 69
SHEET 3 BE10 GLU B 45 LYS B 50 -1 O VAL B 46 N MET B 63
SHEET 4 BE10 GLY B 100 LEU B 108 -1 O LEU B 103 N PHE B 49
SHEET 5 BE10 THR B 111 ARG B 133 -1 O THR B 111 N LEU B 108
SHEET 6 BE10 THR F 111 ARG F 133 -1 O LEU F 125 N SER B 131
SHEET 7 BE10 GLY F 100 LEU F 108 -1 O GLY F 100 N LEU F 119
SHEET 8 BE10 GLU F 45 LYS F 50 -1 O GLU F 45 N LYS F 107
SHEET 9 BE10 VAL F 58 MET F 63 1 O VAL F 58 N LYS F 50
SHEET 10 BE10 ILE F 68 ILE F 70 1 O PHE F 69 N ARG F 62
SHEET 1 BF 7 ILE B 68 ILE B 70 0
SHEET 2 BF 7 VAL B 58 MET B 63 -1 O ARG B 62 N PHE B 69
SHEET 3 BF 7 GLU B 45 LYS B 50 -1 O VAL B 46 N MET B 63
SHEET 4 BF 7 GLY B 100 LEU B 108 -1 O LEU B 103 N PHE B 49
SHEET 5 BF 7 THR B 111 ARG B 133 -1 O THR B 111 N LEU B 108
SHEET 6 BF 7 THR F 111 ARG F 133 -1 O LEU F 125 N SER B 131
SHEET 7 BF 7 THR F 22 PHE F 24 -1 O ALA F 23 N VAL F 122
SHEET 1 BG 3 VAL B 29 TYR B 34 0
SHEET 2 BG 3 THR B 86 VAL B 91 -1 O PHE B 87 N SER B 33
SHEET 3 BG 3 PHE B 78 SER B 83 -1 O ASP B 79 N VAL B 90
SHEET 1 BH 6 PRO B 154 TRP B 158 0
SHEET 2 BH 6 VAL B 199 ASN B 205 -1 O VAL B 202 N GLN B 157
SHEET 3 BH 6 GLU B 208 SER B 216 -1 O GLU B 208 N ASN B 205
SHEET 4 BH 6 GLU F 208 SER F 216 -1 O GLU F 209 N VAL B 215
SHEET 5 BH 6 VAL F 199 ASN F 205 -1 O VAL F 199 N TYR F 214
SHEET 6 BH 6 PRO F 154 TRP F 158 -1 O HIS F 155 N LYS F 204
SHEET 1 CA 2 THR C 22 PHE C 24 0
SHEET 2 CA 2 THR C 111 ARG C 133 1 O SER C 120 N ALA C 23
SHEET 1 CB 9 ILE C 68 ILE C 70 0
SHEET 2 CB 9 VAL C 58 MET C 63 1 O ARG C 62 N PHE C 69
SHEET 3 CB 9 GLU C 45 LYS C 50 -1 O VAL C 46 N MET C 63
SHEET 4 CB 9 GLY C 100 LEU C 108 -1 O LEU C 103 N PHE C 49
SHEET 5 CB 9 THR C 111 ARG C 133 1 O THR C 111 N LEU C 108
SHEET 6 CB 9 THR E 111 ARG E 133 -1 O LEU E 127 N VAL C 129
SHEET 7 CB 9 LEU E 142 PHE E 151 1 O THR E 143 N GLU E 132
SHEET 8 CB 9 LEU E 183 LEU E 191 1 O LEU E 183 N ALA E 150
SHEET 9 CB 9 MET E 176 LYS E 177 -1 O MET E 176 N SER E 184
SHEET 1 CC 8 ILE C 68 ILE C 70 0
SHEET 2 CC 8 VAL C 58 MET C 63 1 O ARG C 62 N PHE C 69
SHEET 3 CC 8 GLU C 45 LYS C 50 -1 O VAL C 46 N MET C 63
SHEET 4 CC 8 GLY C 100 LEU C 108 -1 O LEU C 103 N PHE C 49
SHEET 5 CC 8 THR C 111 ARG C 133 1 O THR C 111 N LEU C 108
SHEET 6 CC 8 LEU C 142 PHE C 151 -1 O THR C 143 N GLU C 132
SHEET 7 CC 8 LEU C 183 LEU C 191 -1 O LEU C 183 N ALA C 150
SHEET 8 CC 8 GLY C 174 LYS C 177 -1 N GLY C 174 O ALA C 186
SHEET 1 CD 6 ILE C 68 ILE C 70 0
SHEET 2 CD 6 VAL C 58 MET C 63 1 O ARG C 62 N PHE C 69
SHEET 3 CD 6 GLU C 45 LYS C 50 -1 O VAL C 46 N MET C 63
SHEET 4 CD 6 GLY C 100 LEU C 108 -1 O LEU C 103 N PHE C 49
SHEET 5 CD 6 THR C 111 ARG C 133 1 O THR C 111 N LEU C 108
SHEET 6 CD 6 THR C 22 PHE C 24 1 O ALA C 23 N VAL C 122
SHEET 1 EA 2 THR E 22 PHE E 24 0
SHEET 2 EA 2 THR E 111 ARG E 133 -1 O SER E 120 N ALA E 23
SHEET 1 CE10 ILE C 68 ILE C 70 0
SHEET 2 CE10 VAL C 58 MET C 63 1 O ARG C 62 N PHE C 69
SHEET 3 CE10 GLU C 45 LYS C 50 -1 O VAL C 46 N MET C 63
SHEET 4 CE10 GLY C 100 LEU C 108 -1 O LEU C 103 N PHE C 49
SHEET 5 CE10 THR C 111 ARG C 133 1 O THR C 111 N LEU C 108
SHEET 6 CE10 THR E 111 ARG E 133 -1 O LEU E 127 N VAL C 129
SHEET 7 CE10 GLY E 100 LEU E 108 -1 O GLY E 100 N LEU E 119
SHEET 8 CE10 GLU E 45 LYS E 50 -1 O GLU E 45 N LYS E 107
SHEET 9 CE10 VAL E 58 MET E 63 -1 O VAL E 58 N LYS E 50
SHEET 10 CE10 ILE E 68 ILE E 70 -1 O PHE E 69 N ARG E 62
SHEET 1 CF 7 ILE C 68 ILE C 70 0
SHEET 2 CF 7 VAL C 58 MET C 63 1 O ARG C 62 N PHE C 69
SHEET 3 CF 7 GLU C 45 LYS C 50 -1 O VAL C 46 N MET C 63
SHEET 4 CF 7 GLY C 100 LEU C 108 -1 O LEU C 103 N PHE C 49
SHEET 5 CF 7 THR C 111 ARG C 133 1 O THR C 111 N LEU C 108
SHEET 6 CF 7 THR E 111 ARG E 133 -1 O LEU E 127 N VAL C 129
SHEET 7 CF 7 THR E 22 PHE E 24 -1 O ALA E 23 N VAL E 122
SHEET 1 CG 3 VAL C 29 TYR C 34 0
SHEET 2 CG 3 THR C 86 VAL C 91 -1 O PHE C 87 N SER C 33
SHEET 3 CG 3 PHE C 78 SER C 83 -1 O ASP C 79 N VAL C 90
SHEET 1 CH 6 PRO C 154 TRP C 158 0
SHEET 2 CH 6 VAL C 199 ASN C 205 -1 O VAL C 202 N GLN C 157
SHEET 3 CH 6 GLU C 208 SER C 216 -1 O GLU C 208 N ASN C 205
SHEET 4 CH 6 GLU E 208 SER E 216 -1 O GLU E 209 N VAL C 215
SHEET 5 CH 6 VAL E 199 ASN E 205 -1 O VAL E 199 N TYR E 214
SHEET 6 CH 6 PRO E 154 TRP E 158 -1 O HIS E 155 N LYS E 204
SHEET 1 DI 3 VAL D 29 TYR D 34 0
SHEET 2 DI 3 THR D 86 VAL D 91 -1 O PHE D 87 N SER D 33
SHEET 3 DI 3 PHE D 78 SER D 83 -1 O ASP D 79 N VAL D 90
SHEET 1 EB 3 VAL E 29 TYR E 34 0
SHEET 2 EB 3 THR E 86 VAL E 91 -1 O PHE E 87 N SER E 33
SHEET 3 EB 3 PHE E 78 SER E 83 -1 O ASP E 79 N VAL E 90
SHEET 1 FB 3 VAL F 29 TYR F 34 0
SHEET 2 FB 3 THR F 86 VAL F 91 -1 O PHE F 87 N SER F 33
SHEET 3 FB 3 PHE F 78 SER F 83 -1 O ASP F 79 N VAL F 90
SHEET 1 GA 2 ILE G 33 VAL G 38 0
SHEET 2 GA 2 VAL G 103 GLU G 108 -1 O ARG G 104 N PHE G 37
SHEET 1 HA 2 ILE H 33 VAL H 38 0
SHEET 2 HA 2 VAL H 103 GLU H 108 -1 O ARG H 104 N PHE H 37
SHEET 1 IA 2 ILE I 33 VAL I 38 0
SHEET 2 IA 2 VAL I 103 GLU I 108 -1 O ARG I 104 N PHE I 37
SHEET 1 JA 2 ILE J 33 VAL J 38 0
SHEET 2 JA 2 VAL J 103 GLU J 108 -1 O ARG J 104 N PHE J 37
SHEET 1 KA 2 ILE K 33 VAL K 38 0
SHEET 2 KA 2 VAL K 103 GLU K 108 -1 O ARG K 104 N PHE K 37
SHEET 1 LA 2 ILE L 33 VAL L 38 0
SHEET 2 LA 2 VAL L 103 GLU L 108 -1 O ARG L 104 N PHE L 37
SHEET 1 MA 2 THR M 22 PHE M 24 0
SHEET 2 MA 2 THR M 111 ARG M 133 1 O SER M 120 N ALA M 23
SHEET 1 MB 9 ILE M 68 ILE M 70 0
SHEET 2 MB 9 VAL M 58 MET M 63 1 O ARG M 62 N PHE M 69
SHEET 3 MB 9 GLU M 45 LYS M 50 -1 O VAL M 46 N MET M 63
SHEET 4 MB 9 GLY M 100 LEU M 108 -1 O LEU M 103 N PHE M 49
SHEET 5 MB 9 THR M 111 ARG M 133 1 O THR M 111 N LEU M 108
SHEET 6 MB 9 THR O 111 ARG O 133 -1 O LEU O 125 N SER M 131
SHEET 7 MB 9 LEU O 142 PHE O 151 1 O THR O 143 N GLU O 132
SHEET 8 MB 9 LEU O 183 LEU O 191 1 O LEU O 183 N ALA O 150
SHEET 9 MB 9 MET O 176 LYS O 177 1 O MET O 176 N SER O 184
SHEET 1 MC 8 ILE M 68 ILE M 70 0
SHEET 2 MC 8 VAL M 58 MET M 63 1 O ARG M 62 N PHE M 69
SHEET 3 MC 8 GLU M 45 LYS M 50 -1 O VAL M 46 N MET M 63
SHEET 4 MC 8 GLY M 100 LEU M 108 -1 O LEU M 103 N PHE M 49
SHEET 5 MC 8 THR M 111 ARG M 133 1 O THR M 111 N LEU M 108
SHEET 6 MC 8 LEU M 142 PHE M 151 1 O THR M 143 N GLU M 132
SHEET 7 MC 8 LEU M 183 LEU M 191 -1 O LEU M 183 N ALA M 150
SHEET 8 MC 8 VAL M 175 LYS M 177 -1 O MET M 176 N SER M 184
SHEET 1 MD 6 ILE M 68 ILE M 70 0
SHEET 2 MD 6 VAL M 58 MET M 63 1 O ARG M 62 N PHE M 69
SHEET 3 MD 6 GLU M 45 LYS M 50 -1 O VAL M 46 N MET M 63
SHEET 4 MD 6 GLY M 100 LEU M 108 -1 O LEU M 103 N PHE M 49
SHEET 5 MD 6 THR M 111 ARG M 133 1 O THR M 111 N LEU M 108
SHEET 6 MD 6 THR M 22 PHE M 24 1 O ALA M 23 N VAL M 122
SHEET 1 OA 2 THR O 22 PHE O 24 0
SHEET 2 OA 2 THR O 111 ARG O 133 -1 O SER O 120 N ALA O 23
SHEET 1 ME10 ILE M 68 ILE M 70 0
SHEET 2 ME10 VAL M 58 MET M 63 1 O ARG M 62 N PHE M 69
SHEET 3 ME10 GLU M 45 LYS M 50 -1 O VAL M 46 N MET M 63
SHEET 4 ME10 GLY M 100 LEU M 108 -1 O LEU M 103 N PHE M 49
SHEET 5 ME10 THR M 111 ARG M 133 1 O THR M 111 N LEU M 108
SHEET 6 ME10 THR O 111 ARG O 133 -1 O LEU O 125 N SER M 131
SHEET 7 ME10 GLY O 100 LEU O 108 -1 O GLY O 100 N LEU O 119
SHEET 8 ME10 GLU O 45 LYS O 50 -1 O GLU O 45 N LYS O 107
SHEET 9 ME10 VAL O 58 MET O 63 -1 O VAL O 58 N LYS O 50
SHEET 10 ME10 ILE O 68 ILE O 70 -1 O PHE O 69 N ARG O 62
SHEET 1 MF 7 ILE M 68 ILE M 70 0
SHEET 2 MF 7 VAL M 58 MET M 63 1 O ARG M 62 N PHE M 69
SHEET 3 MF 7 GLU M 45 LYS M 50 -1 O VAL M 46 N MET M 63
SHEET 4 MF 7 GLY M 100 LEU M 108 -1 O LEU M 103 N PHE M 49
SHEET 5 MF 7 THR M 111 ARG M 133 1 O THR M 111 N LEU M 108
SHEET 6 MF 7 THR O 111 ARG O 133 -1 O LEU O 125 N SER M 131
SHEET 7 MF 7 THR O 22 PHE O 24 1 O ALA O 23 N VAL O 122
SHEET 1 MG 3 VAL M 29 TYR M 34 0
SHEET 2 MG 3 THR M 86 VAL M 91 -1 O PHE M 87 N SER M 33
SHEET 3 MG 3 PHE M 78 SER M 83 -1 O ASP M 79 N VAL M 90
SHEET 1 MH 6 PRO M 154 TRP M 158 0
SHEET 2 MH 6 VAL M 199 ASN M 205 -1 O VAL M 202 N GLN M 157
SHEET 3 MH 6 GLU M 208 SER M 216 -1 O GLU M 208 N ASN M 205
SHEET 4 MH 6 GLU O 208 SER O 216 -1 O GLU O 209 N VAL M 215
SHEET 5 MH 6 VAL O 199 ASN O 205 -1 O VAL O 199 N TYR O 214
SHEET 6 MH 6 PRO O 154 LEU O 159 -1 O HIS O 155 N LYS O 204
SHEET 1 NA 3 VAL N 29 TYR N 34 0
SHEET 2 NA 3 THR N 86 VAL N 91 -1 O PHE N 87 N SER N 33
SHEET 3 NA 3 PHE N 78 SER N 83 -1 O ASP N 79 N VAL N 90
SHEET 1 NB 6 PRO N 154 TRP N 158 0
SHEET 2 NB 6 VAL N 199 ASN N 205 -1 O VAL N 202 N GLN N 157
SHEET 3 NB 6 GLU N 208 SER N 216 -1 O GLU N 208 N ASN N 205
SHEET 4 NB 6 GLU R 208 SER R 216 -1 O GLU R 209 N VAL N 215
SHEET 5 NB 6 VAL R 199 ASN R 205 -1 O VAL R 199 N TYR R 214
SHEET 6 NB 6 PRO R 154 TRP R 158 -1 O HIS R 155 N LYS R 204
SHEET 1 OB 3 VAL O 29 TYR O 34 0
SHEET 2 OB 3 THR O 86 VAL O 91 -1 O PHE O 87 N SER O 33
SHEET 3 OB 3 PHE O 78 SER O 83 -1 O ASP O 79 N VAL O 90
SHEET 1 PA 2 THR P 22 PHE P 24 0
SHEET 2 PA 2 THR P 111 ARG P 133 1 O SER P 120 N ALA P 23
SHEET 1 PB 9 ILE P 68 ILE P 70 0
SHEET 2 PB 9 VAL P 58 MET P 63 1 O ARG P 62 N PHE P 69
SHEET 3 PB 9 GLU P 45 LYS P 50 -1 O VAL P 46 N MET P 63
SHEET 4 PB 9 GLY P 100 LEU P 108 -1 O LEU P 103 N PHE P 49
SHEET 5 PB 9 THR P 111 ARG P 133 1 O THR P 111 N LEU P 108
SHEET 6 PB 9 THR Q 111 ARG Q 133 -1 O LEU Q 127 N VAL P 129
SHEET 7 PB 9 LEU Q 142 PHE Q 151 1 O THR Q 143 N GLU Q 132
SHEET 8 PB 9 LEU Q 183 LEU Q 191 1 O LEU Q 183 N ALA Q 150
SHEET 9 PB 9 MET Q 176 LYS Q 177 -1 O MET Q 176 N SER Q 184
SHEET 1 PC 8 ILE P 68 ILE P 70 0
SHEET 2 PC 8 VAL P 58 MET P 63 1 O ARG P 62 N PHE P 69
SHEET 3 PC 8 GLU P 45 LYS P 50 -1 O VAL P 46 N MET P 63
SHEET 4 PC 8 GLY P 100 LEU P 108 -1 O LEU P 103 N PHE P 49
SHEET 5 PC 8 THR P 111 ARG P 133 1 O THR P 111 N LEU P 108
SHEET 6 PC 8 LEU P 142 PHE P 151 -1 O THR P 143 N GLU P 132
SHEET 7 PC 8 LEU P 183 LEU P 191 -1 O LEU P 183 N ALA P 150
SHEET 8 PC 8 GLY P 174 LYS P 177 -1 O GLY P 174 N ALA P 186
SHEET 1 PD 6 ILE P 68 ILE P 70 0
SHEET 2 PD 6 VAL P 58 MET P 63 1 O ARG P 62 N PHE P 69
SHEET 3 PD 6 GLU P 45 LYS P 50 -1 O VAL P 46 N MET P 63
SHEET 4 PD 6 GLY P 100 LEU P 108 -1 O LEU P 103 N PHE P 49
SHEET 5 PD 6 THR P 111 ARG P 133 1 O THR P 111 N LEU P 108
SHEET 6 PD 6 THR P 22 PHE P 24 1 O ALA P 23 N VAL P 122
SHEET 1 QA 2 THR Q 22 PHE Q 24 0
SHEET 2 QA 2 THR Q 111 ARG Q 133 -1 O SER Q 120 N ALA Q 23
SHEET 1 PE10 ILE P 68 ILE P 70 0
SHEET 2 PE10 VAL P 58 MET P 63 1 O ARG P 62 N PHE P 69
SHEET 3 PE10 GLU P 45 LYS P 50 -1 O VAL P 46 N MET P 63
SHEET 4 PE10 GLY P 100 LEU P 108 -1 O LEU P 103 N PHE P 49
SHEET 5 PE10 THR P 111 ARG P 133 1 O THR P 111 N LEU P 108
SHEET 6 PE10 THR Q 111 ARG Q 133 -1 O LEU Q 127 N VAL P 129
SHEET 7 PE10 GLY Q 100 LEU Q 108 -1 O GLY Q 100 N LEU Q 119
SHEET 8 PE10 GLU Q 45 LYS Q 50 -1 O GLU Q 45 N LYS Q 107
SHEET 9 PE10 VAL Q 58 MET Q 63 -1 O VAL Q 58 N LYS Q 50
SHEET 10 PE10 ILE Q 68 ILE Q 70 -1 O PHE Q 69 N ARG Q 62
SHEET 1 PF 7 ILE P 68 ILE P 70 0
SHEET 2 PF 7 VAL P 58 MET P 63 1 O ARG P 62 N PHE P 69
SHEET 3 PF 7 GLU P 45 LYS P 50 -1 O VAL P 46 N MET P 63
SHEET 4 PF 7 GLY P 100 LEU P 108 -1 O LEU P 103 N PHE P 49
SHEET 5 PF 7 THR P 111 ARG P 133 1 O THR P 111 N LEU P 108
SHEET 6 PF 7 THR Q 111 ARG Q 133 -1 O LEU Q 127 N VAL P 129
SHEET 7 PF 7 THR Q 22 PHE Q 24 -1 O ALA Q 23 N VAL Q 122
SHEET 1 PG 3 VAL P 29 TYR P 34 0
SHEET 2 PG 3 THR P 86 VAL P 91 -1 O PHE P 87 N SER P 33
SHEET 3 PG 3 PHE P 78 SER P 83 -1 O ASP P 79 N VAL P 90
SHEET 1 PH 6 PRO P 154 TRP P 158 0
SHEET 2 PH 6 VAL P 199 ASN P 205 -1 O VAL P 202 N GLN P 157
SHEET 3 PH 6 GLU P 208 SER P 216 -1 O GLU P 208 N ASN P 205
SHEET 4 PH 6 GLU Q 208 SER Q 216 -1 O GLU Q 209 N VAL P 215
SHEET 5 PH 6 VAL Q 199 ASN Q 205 -1 O VAL Q 199 N TYR Q 214
SHEET 6 PH 6 PRO Q 154 TRP Q 158 -1 O HIS Q 155 N LYS Q 204
SHEET 1 QB 3 VAL Q 29 TYR Q 34 0
SHEET 2 QB 3 THR Q 86 VAL Q 91 -1 O PHE Q 87 N SER Q 33
SHEET 3 QB 3 PHE Q 78 SER Q 83 -1 O ASP Q 79 N VAL Q 90
SHEET 1 RD 3 VAL R 29 TYR R 34 0
SHEET 2 RD 3 THR R 86 VAL R 91 -1 O PHE R 87 N SER R 33
SHEET 3 RD 3 PHE R 78 SER R 83 -1 O ASP R 79 N VAL R 90
SHEET 1 SA 2 ILE S 33 VAL S 38 0
SHEET 2 SA 2 VAL S 103 GLU S 108 -1 O ARG S 104 N PHE S 37
SHEET 1 TA 2 ILE T 33 VAL T 38 0
SHEET 2 TA 2 VAL T 103 GLU T 108 -1 O ARG T 104 N PHE T 37
SHEET 1 UA 2 ILE U 33 VAL U 38 0
SHEET 2 UA 2 VAL U 103 GLU U 108 -1 O ARG U 104 N PHE U 37
SHEET 1 VA 2 ILE V 33 VAL V 38 0
SHEET 2 VA 2 VAL V 103 GLU V 108 -1 O ARG V 104 N PHE V 37
SHEET 1 WA 2 ILE W 33 VAL W 38 0
SHEET 2 WA 2 VAL W 103 GLU W 108 -1 O ARG W 104 N PHE W 37
SHEET 1 XA 2 ILE X 33 VAL X 38 0
SHEET 2 XA 2 VAL X 103 GLU X 108 -1 O ARG X 104 N PHE X 37
SSBOND 1 CYS A 146 CYS A 201 1555 1555 2.03
SSBOND 2 CYS B 146 CYS B 201 1555 1555 2.04
SSBOND 3 CYS C 146 CYS C 201 1555 1555 2.03
SSBOND 4 CYS D 146 CYS D 201 1555 1555 2.03
SSBOND 5 CYS E 146 CYS E 201 1555 1555 2.03
SSBOND 6 CYS F 146 CYS F 201 1555 1555 2.03
SSBOND 7 CYS G 7 CYS G 90 1555 1555 2.03
SSBOND 8 CYS G 31 CYS H 31 1555 1555 2.03
SSBOND 9 CYS G 48 CYS G 139 1555 1555 2.03
SSBOND 10 CYS G 102 CYS G 146 1555 1555 2.04
SSBOND 11 CYS H 7 CYS H 90 1555 1555 2.04
SSBOND 12 CYS H 48 CYS H 139 1555 1555 2.03
SSBOND 13 CYS H 102 CYS H 146 1555 1555 2.03
SSBOND 14 CYS I 7 CYS I 90 1555 1555 2.03
SSBOND 15 CYS I 31 CYS J 31 1555 1555 2.03
SSBOND 16 CYS I 48 CYS I 139 1555 1555 2.03
SSBOND 17 CYS I 102 CYS I 146 1555 1555 2.04
SSBOND 18 CYS J 7 CYS J 90 1555 1555 2.02
SSBOND 19 CYS J 48 CYS J 139 1555 1555 2.04
SSBOND 20 CYS J 102 CYS J 146 1555 1555 2.03
SSBOND 21 CYS K 7 CYS K 90 1555 1555 2.04
SSBOND 22 CYS K 31 CYS L 31 1555 1555 2.02
SSBOND 23 CYS K 48 CYS K 139 1555 1555 2.03
SSBOND 24 CYS K 102 CYS K 146 1555 1555 2.04
SSBOND 25 CYS L 7 CYS L 90 1555 1555 2.04
SSBOND 26 CYS L 48 CYS L 139 1555 1555 2.03
SSBOND 27 CYS L 102 CYS L 146 1555 1555 2.03
SSBOND 28 CYS M 146 CYS M 201 1555 1555 2.03
SSBOND 29 CYS N 146 CYS N 201 1555 1555 2.04
SSBOND 30 CYS O 146 CYS O 201 1555 1555 2.03
SSBOND 31 CYS P 146 CYS P 201 1555 1555 2.03
SSBOND 32 CYS Q 146 CYS Q 201 1555 1555 2.03
SSBOND 33 CYS R 146 CYS R 201 1555 1555 2.04
SSBOND 34 CYS S 7 CYS S 90 1555 1555 2.04
SSBOND 35 CYS S 31 CYS T 31 1555 1555 2.02
SSBOND 36 CYS S 48 CYS S 139 1555 1555 2.03
SSBOND 37 CYS S 102 CYS S 146 1555 1555 2.04
SSBOND 38 CYS T 7 CYS T 90 1555 1555 2.04
SSBOND 39 CYS T 48 CYS T 139 1555 1555 2.03
SSBOND 40 CYS T 102 CYS T 146 1555 1555 2.03
SSBOND 41 CYS U 7 CYS U 90 1555 1555 2.03
SSBOND 42 CYS U 31 CYS V 31 1555 1555 2.02
SSBOND 43 CYS U 48 CYS U 139 1555 1555 2.03
SSBOND 44 CYS U 102 CYS U 146 1555 1555 2.03
SSBOND 45 CYS V 7 CYS V 90 1555 1555 2.04
SSBOND 46 CYS V 48 CYS V 139 1555 1555 2.03
SSBOND 47 CYS V 102 CYS V 146 1555 1555 2.03
SSBOND 48 CYS W 7 CYS W 90 1555 1555 2.03
SSBOND 49 CYS W 31 CYS X 31 1555 1555 2.03
SSBOND 50 CYS W 48 CYS W 139 1555 1555 2.03
SSBOND 51 CYS W 102 CYS W 146 1555 1555 2.04
SSBOND 52 CYS X 7 CYS X 90 1555 1555 2.04
SSBOND 53 CYS X 48 CYS X 139 1555 1555 2.03
SSBOND 54 CYS X 102 CYS X 146 1555 1555 2.03
LINK ND2 ASN A 95 C1 NAG Y 1 1555 1555 1.45
LINK ND2 ASN B 95 C1 NAG Z 1 1555 1555 1.46
LINK ND2 ASN C 95 C1 NAG a 1 1555 1555 1.46
LINK ND2 ASN D 95 C1 NAG b 1 1555 1555 1.47
LINK ND2 ASN E 95 C1 NAG c 1 1555 1555 1.46
LINK ND2 ASN F 95 C1 NAG d 1 1555 1555 1.46
LINK ND2 ASN M 95 C1 NAG e 1 1555 1555 1.45
LINK ND2 ASN N 95 C1 NAG f 1 1555 1555 1.45
LINK ND2 ASN O 95 C1 NAG g 1 1555 1555 1.44
LINK ND2 ASN P 95 C1 NAG h 1 1555 1555 1.45
LINK ND2 ASN Q 95 C1 NAG i 1 1555 1555 1.45
LINK ND2 ASN R 95 C1 NAG j 1 1555 1555 1.46
LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45
LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.45
LINK O6 BMA Y 3 C1 MAN Y 4 1555 1555 1.45
LINK O3 BMA Y 3 C1 MAN Y 6 1555 1555 1.44
LINK O6 MAN Y 4 C1 MAN Y 5 1555 1555 1.44
LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.46
LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.46
LINK O6 BMA Z 3 C1 MAN Z 4 1555 1555 1.45
LINK O3 BMA Z 3 C1 MAN Z 7 1555 1555 1.46
LINK O3 MAN Z 4 C1 MAN Z 5 1555 1555 1.44
LINK O6 MAN Z 4 C1 MAN Z 6 1555 1555 1.44
LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45
LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.45
LINK O6 BMA a 3 C1 MAN a 4 1555 1555 1.45
LINK O3 BMA a 3 C1 MAN a 7 1555 1555 1.45
LINK O3 MAN a 4 C1 MAN a 5 1555 1555 1.44
LINK O6 MAN a 4 C1 MAN a 6 1555 1555 1.44
LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.46
LINK O4 NAG b 2 C1 BMA b 3 1555 1555 1.46
LINK O3 BMA b 3 C1 MAN b 4 1555 1555 1.44
LINK O6 BMA b 3 C1 MAN b 5 1555 1555 1.44
LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.46
LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.45
LINK O3 BMA c 3 C1 MAN c 4 1555 1555 1.45
LINK O6 BMA c 3 C1 MAN c 5 1555 1555 1.45
LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.45
LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.47
LINK O3 BMA d 3 C1 MAN d 4 1555 1555 1.45
LINK O6 BMA d 3 C1 MAN d 5 1555 1555 1.45
LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44
LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.44
LINK O6 BMA e 3 C1 MAN e 4 1555 1555 1.46
LINK O3 BMA e 3 C1 MAN e 6 1555 1555 1.45
LINK O6 MAN e 4 C1 MAN e 5 1555 1555 1.43
LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.45
LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.45
LINK O6 BMA f 3 C1 MAN f 4 1555 1555 1.45
LINK O3 BMA f 3 C1 MAN f 6 1555 1555 1.45
LINK O6 MAN f 4 C1 MAN f 5 1555 1555 1.45
LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44
LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.44
LINK O3 BMA g 3 C1 MAN g 4 1555 1555 1.44
LINK O6 BMA g 3 C1 MAN g 5 1555 1555 1.44
LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.45
LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.46
LINK O6 BMA h 3 C1 MAN h 4 1555 1555 1.44
LINK O3 BMA h 3 C1 MAN h 6 1555 1555 1.45
LINK O6 MAN h 4 C1 MAN h 5 1555 1555 1.44
LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44
LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.45
LINK O6 BMA i 3 C1 MAN i 4 1555 1555 1.45
LINK O3 BMA i 3 C1 MAN i 7 1555 1555 1.45
LINK O3 MAN i 4 C1 MAN i 5 1555 1555 1.45
LINK O6 MAN i 4 C1 MAN i 6 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 1.45
LINK O6 BMA j 3 C1 MAN j 4 1555 1555 1.44
LINK O3 BMA j 3 C1 MAN j 7 1555 1555 1.46
LINK O3 MAN j 4 C1 MAN j 5 1555 1555 1.44
LINK O6 MAN j 4 C1 MAN j 6 1555 1555 1.44
CISPEP 1 PHE A 136 PRO A 137 0 -5.55
CISPEP 2 PHE A 151 PRO A 152 0 8.26
CISPEP 3 LYS A 193 PRO A 194 0 -2.10
CISPEP 4 LEU A 197 PRO A 198 0 -7.91
CISPEP 5 PHE B 136 PRO B 137 0 -5.37
CISPEP 6 PHE B 151 PRO B 152 0 8.36
CISPEP 7 LYS B 193 PRO B 194 0 -1.83
CISPEP 8 LEU B 197 PRO B 198 0 -7.35
CISPEP 9 PHE C 136 PRO C 137 0 -5.47
CISPEP 10 PHE C 151 PRO C 152 0 8.57
CISPEP 11 LYS C 193 PRO C 194 0 -2.12
CISPEP 12 LEU C 197 PRO C 198 0 -7.97
CISPEP 13 PHE D 136 PRO D 137 0 -5.45
CISPEP 14 PHE D 151 PRO D 152 0 8.34
CISPEP 15 LYS D 193 PRO D 194 0 -0.41
CISPEP 16 LEU D 197 PRO D 198 0 -7.39
CISPEP 17 PHE E 136 PRO E 137 0 -5.57
CISPEP 18 PHE E 151 PRO E 152 0 8.57
CISPEP 19 LYS E 193 PRO E 194 0 -1.68
CISPEP 20 LEU E 197 PRO E 198 0 -7.89
CISPEP 21 PHE F 136 PRO F 137 0 -5.68
CISPEP 22 PHE F 151 PRO F 152 0 8.39
CISPEP 23 LYS F 193 PRO F 194 0 -1.75
CISPEP 24 LEU F 197 PRO F 198 0 -8.17
CISPEP 25 PHE M 136 PRO M 137 0 -5.60
CISPEP 26 PHE M 151 PRO M 152 0 8.32
CISPEP 27 LYS M 193 PRO M 194 0 -2.01
CISPEP 28 LEU M 197 PRO M 198 0 -7.59
CISPEP 29 PHE N 136 PRO N 137 0 -5.45
CISPEP 30 PHE N 151 PRO N 152 0 8.54
CISPEP 31 MET N 160 PRO N 161 0 -2.05
CISPEP 32 LYS N 193 PRO N 194 0 -1.78
CISPEP 33 LEU N 197 PRO N 198 0 -7.97
CISPEP 34 PHE O 136 PRO O 137 0 -5.54
CISPEP 35 PHE O 151 PRO O 152 0 8.31
CISPEP 36 MET O 160 PRO O 161 0 -0.81
CISPEP 37 LYS O 193 PRO O 194 0 -1.78
CISPEP 38 LEU O 197 PRO O 198 0 -8.65
CISPEP 39 PHE P 136 PRO P 137 0 -5.52
CISPEP 40 PHE P 151 PRO P 152 0 8.50
CISPEP 41 LYS P 193 PRO P 194 0 -1.76
CISPEP 42 LEU P 197 PRO P 198 0 -7.68
CISPEP 43 PHE Q 136 PRO Q 137 0 -5.59
CISPEP 44 PHE Q 151 PRO Q 152 0 8.40
CISPEP 45 LYS Q 193 PRO Q 194 0 -2.13
CISPEP 46 LEU Q 197 PRO Q 198 0 -7.98
CISPEP 47 PHE R 136 PRO R 137 0 -5.47
CISPEP 48 PHE R 151 PRO R 152 0 8.31
CISPEP 49 LYS R 193 PRO R 194 0 -1.87
CISPEP 50 LEU R 197 PRO R 198 0 -7.39
CRYST1 218.440 218.440 331.170 90.00 90.00 120.00 P 31 2 1 72
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 0.004578 0.002643 0.000000 0.00000
SCALE2 0.000000 0.005286 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003020 0.00000
MTRIX1 1 0.380200 0.878900 0.288200 -11.97540 1
MTRIX2 1 0.887600 -0.434200 0.153400 -26.44570 1
MTRIX3 1 0.260000 0.197500 -0.945200 146.57280 1
MTRIX1 2 -0.060000 -0.668200 -0.741600 -57.06790 1
MTRIX2 2 -0.711300 0.549800 -0.437900 -43.44340 1
MTRIX3 2 0.700300 0.501300 -0.508200 164.32330 1
MTRIX1 3 -0.428500 0.365200 -0.826500 -22.87230 1
MTRIX2 3 0.378700 -0.757900 -0.531200 -34.00660 1
MTRIX3 3 -0.820300 -0.540600 0.186500 -31.14340 1
MTRIX1 4 -0.815800 0.058300 0.575300 -150.46410 1
MTRIX2 4 0.162900 -0.931400 0.325400 -109.77840 1
MTRIX3 4 0.554900 0.359200 0.750400 69.77630 1
MTRIX1 5 -0.027300 -0.696400 0.717100 -146.31620 1
MTRIX2 5 -0.705200 0.521900 0.480000 -101.04060 1
MTRIX3 5 -0.708500 -0.492600 -0.505400 20.34150 1
MTRIX1 6 0.875200 0.015300 -0.483500 35.76670 1
MTRIX2 6 -0.200100 0.921400 -0.333000 -52.79920 1
MTRIX3 6 0.440400 0.388200 0.809500 90.50620 1
MTRIX1 7 0.279100 0.926200 -0.253500 -19.15160 1
MTRIX2 7 0.938500 -0.319000 -0.132100 41.89330 1
MTRIX3 7 -0.203200 -0.201000 -0.958300 62.37860 1
MTRIX1 8 -0.806600 0.023900 -0.590600 -131.09810 1
MTRIX2 8 0.228000 -0.909300 -0.348200 -31.61640 1
MTRIX3 8 -0.545300 -0.415500 0.728000 -16.84110 1
MTRIX1 9 -0.257400 -0.904600 -0.339700 -93.26440 1
MTRIX2 9 -0.902500 0.350700 -0.250200 -132.61270 1
MTRIX3 9 0.345400 0.242200 -0.906600 121.19700 1
MTRIX1 10 -0.498900 0.293800 0.815300 -131.15210 1
MTRIX2 10 0.436700 -0.727400 0.529300 -30.70660 1
MTRIX3 10 0.748600 0.620100 0.234600 138.31570 1
MTRIX1 11 0.396700 -0.356900 0.845700 -50.51250 1
MTRIX2 11 -0.496500 0.691500 0.524700 -106.28290 1
MTRIX3 11 -0.772100 -0.628000 0.097100 -26.33590 1
MTRIX1 12 -0.086200 0.775500 -0.625400 -86.66940 1
MTRIX2 12 0.776600 -0.340900 -0.529700 75.97970 1
MTRIX3 12 -0.624000 -0.531400 -0.572900 -32.30200 1
MTRIX1 13 0.169900 -0.719600 -0.673300 -78.35330 1
MTRIX2 13 -0.658800 0.425200 -0.620700 -59.01740 1
MTRIX3 13 0.732900 0.549000 -0.401800 110.78040 1
MTRIX1 14 -0.984500 0.051300 -0.167700 -195.24620 1
MTRIX2 14 -0.038200 -0.996000 -0.080200 -24.90150 1
MTRIX3 14 -0.171100 -0.072600 0.982600 -15.70650 1
MTRIX1 15 0.158200 -0.743400 0.649800 -112.17270 1
MTRIX2 15 -0.746100 0.341100 0.571800 -95.04280 1
MTRIX3 15 -0.646800 -0.575300 -0.500700 -34.90370 1
MTRIX1 16 -0.180500 0.720100 0.669900 -129.08690 1
MTRIX2 16 0.719500 -0.367700 0.589200 40.49840 1
MTRIX3 16 0.670600 0.588400 -0.451800 106.94870 1
MTRIX1 17 0.452000 0.875900 0.168900 1.50560 1
MTRIX2 17 0.877900 -0.470300 0.089600 -27.09730 1
MTRIX3 17 0.157900 0.107800 -0.981600 130.53470 1
MTRIX1 18 -0.086500 -0.630300 -0.771500 -53.43910 1
MTRIX2 18 -0.638900 0.629300 -0.442500 -36.68860 1
MTRIX3 18 0.764400 0.454600 -0.457100 160.49760 1
MTRIX1 19 -0.462100 0.314700 -0.829100 -26.22740 1
MTRIX2 19 0.330800 -0.806200 -0.490500 -43.22300 1
MTRIX3 19 -0.822800 -0.500900 0.268500 -38.24390 1
MTRIX1 20 -0.104200 -0.696300 0.710200 -149.26500 1
MTRIX2 20 -0.745600 0.527200 0.407500 -101.60870 1
MTRIX3 20 -0.658200 -0.487100 -0.574100 24.22020 1
MTRIX1 21 -0.812600 0.029500 0.582100 -151.41880 1
MTRIX2 21 0.210800 -0.916300 0.340500 -107.71350 1
MTRIX3 21 0.543500 0.399400 0.738300 71.38440 1
(ATOM LINES ARE NOT SHOWN.)
END