HEADER IMMUNE SYSTEM 11-AUG-14 4R2G
TITLE CRYSTAL STRUCTURE OF PGT124 FAB BOUND TO HIV-1 JRCSF GP120 CORE AND TO
TITLE 2 CD4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SURFACE PROTEIN GP160;
COMPND 3 CHAIN: E, O, A, K;
COMPND 4 SYNONYM: ENV POLYPROTEIN,ENV POLYPROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;
COMPND 8 CHAIN: F, B, H, L;
COMPND 9 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PGT124 LIGHT CHAIN;
COMPND 13 CHAIN: P, C, I, M;
COMPND 14 SYNONYM: IG LAMBDA CHAIN C REGION DOT,IG LAMBDA CHAIN C REGION NEWM,
COMPND 15 IG LAMBDA-3 CHAIN C REGIONS;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: PGT124 HEAVY CHAIN;
COMPND 19 CHAIN: Q, D, J, N;
COMPND 20 SYNONYM: IMMUNOGLOBULIN GAMMA-1 HEAVY CHAIN NIE;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 GROUP M
SOURCE 3 SUBTYPE B;
SOURCE 4 ORGANISM_COMMON: HIV-1;
SOURCE 5 ORGANISM_TAXID: 11688;
SOURCE 6 STRAIN: ISOLATE JRCSF;
SOURCE 7 GENE: ENV;
SOURCE 8 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: 293 FREESTYLE;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: CD4;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN, HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: IGL@, IGLC3;
SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: 293 FREESTYLE;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 30 ORGANISM_COMMON: HUMAN, HUMAN;
SOURCE 31 ORGANISM_TAXID: 9606;
SOURCE 32 GENE: IGH@;
SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 34 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 36 EXPRESSION_SYSTEM_CELL_LINE: 293 FREESTYLE
KEYWDS PROTEIN-PROTEIN COMPLEX, IGG, ANTI-HIV ANTIBODIES, GP120, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR F.GARCES,I.A.WILSON
REVDAT 4 29-JUL-20 4R2G 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 21-JUN-17 4R2G 1 DBREF
REVDAT 2 15-OCT-14 4R2G 1 REMARK
REVDAT 1 08-OCT-14 4R2G 0
JRNL AUTH F.GARCES,D.SOK,L.KONG,R.MCBRIDE,H.J.KIM,K.F.SAYE-FRANCISCO,
JRNL AUTH 2 J.P.JULIEN,Y.HUA,A.CUPO,J.P.MOORE,J.C.PAULSON,A.B.WARD,
JRNL AUTH 3 D.R.BURTON,I.A.WILSON
JRNL TITL STRUCTURAL EVOLUTION OF GLYCAN RECOGNITION BY A FAMILY OF
JRNL TITL 2 POTENT HIV ANTIBODIES.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 159 69 2014
JRNL REFN ISSN 0092-8674
JRNL PMID 25259921
JRNL DOI 10.1016/J.CELL.2014.09.009
REMARK 2
REMARK 2 RESOLUTION. 3.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 3.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 94587
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4720
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 39.6496 - 10.1457 0.95 3103 148 0.2446 0.2878
REMARK 3 2 10.1457 - 8.0753 0.97 3057 167 0.1800 0.2140
REMARK 3 3 8.0753 - 7.0610 0.97 3001 160 0.2032 0.2479
REMARK 3 4 7.0610 - 6.4184 0.99 3055 160 0.2076 0.2524
REMARK 3 5 6.4184 - 5.9600 0.99 3052 166 0.2083 0.2699
REMARK 3 6 5.9600 - 5.6096 1.00 3047 175 0.2065 0.2813
REMARK 3 7 5.6096 - 5.3294 0.94 2866 157 0.1934 0.2503
REMARK 3 8 5.3294 - 5.0979 0.99 3020 163 0.1730 0.2092
REMARK 3 9 5.0979 - 4.9020 0.99 3035 144 0.1669 0.2152
REMARK 3 10 4.9020 - 4.7331 1.00 3027 154 0.1650 0.2288
REMARK 3 11 4.7331 - 4.5854 1.00 3024 167 0.1596 0.2176
REMARK 3 12 4.5854 - 4.4545 0.99 3005 162 0.1620 0.2170
REMARK 3 13 4.4545 - 4.3374 1.00 2988 157 0.1679 0.2290
REMARK 3 14 4.3374 - 4.2317 1.00 3026 153 0.1693 0.2590
REMARK 3 15 4.2317 - 4.1356 0.98 2980 159 0.1838 0.2423
REMARK 3 16 4.1356 - 4.0476 0.95 2880 143 0.1988 0.2634
REMARK 3 17 4.0476 - 3.9667 1.00 3013 171 0.2115 0.2668
REMARK 3 18 3.9667 - 3.8920 0.99 2987 151 0.2427 0.3444
REMARK 3 19 3.8920 - 3.8225 0.99 2982 154 0.2388 0.2977
REMARK 3 20 3.8225 - 3.7578 1.00 3005 164 0.2211 0.2465
REMARK 3 21 3.7578 - 3.6972 1.00 3047 151 0.2261 0.2939
REMARK 3 22 3.6972 - 3.6403 0.99 2973 150 0.2624 0.3073
REMARK 3 23 3.6403 - 3.5868 1.00 2971 160 0.2482 0.3135
REMARK 3 24 3.5868 - 3.5364 1.00 3027 141 0.2422 0.3001
REMARK 3 25 3.5364 - 3.4886 1.00 3006 152 0.2521 0.2974
REMARK 3 26 3.4886 - 3.4433 1.00 2980 155 0.2877 0.3595
REMARK 3 27 3.4433 - 3.4003 0.99 3029 166 0.3104 0.3740
REMARK 3 28 3.4003 - 3.3593 0.99 2979 145 0.2826 0.3653
REMARK 3 29 3.3593 - 3.3203 0.93 2781 152 0.2794 0.3524
REMARK 3 30 3.3203 - 3.2830 0.98 2921 173 0.2883 0.3267
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 29813
REMARK 3 ANGLE : 1.373 40397
REMARK 3 CHIRALITY : 0.078 4717
REMARK 3 PLANARITY : 0.005 5058
REMARK 3 DIHEDRAL : 16.066 11109
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 4R2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000086814.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94587
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.283
REMARK 200 RESOLUTION RANGE LOW (A) : 39.647
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.87000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M AMMONIUM SULPHATE, 0.1M TRIS, 13%
REMARK 280 GLYCEROL, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 82.20300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.85600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 82.71900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.85600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 82.20300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 82.71900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, P, Q, G
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, O, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, J, K, V
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M, N, A, S, T, U
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR E 317
REMARK 465 ARG E 318
REMARK 465 PRO E 319
REMARK 465 GLY E 320
REMARK 465 GLU E 321
REMARK 465 GLU E 492
REMARK 465 MET F 0
REMARK 465 VAL F 176
REMARK 465 LEU F 177
REMARK 465 ALA F 178
REMARK 465 PHE F 179
REMARK 465 GLN F 180
REMARK 465 LYS F 181
REMARK 465 ALA F 182
REMARK 465 SER F 183
REMARK 465 SER P 4
REMARK 465 GLU P 211
REMARK 465 CYS P 212
REMARK 465 SER P 213
REMARK 465 GLN Q 1
REMARK 465 LYS Q 147
REMARK 465 SER Q 148
REMARK 465 THR Q 149
REMARK 465 LYS Q 232
REMARK 465 SER Q 233
REMARK 465 CYS Q 234
REMARK 465 ASP Q 235
REMARK 465 MET B 0
REMARK 465 VAL B 176
REMARK 465 LEU B 177
REMARK 465 ALA B 178
REMARK 465 PHE B 179
REMARK 465 GLN B 180
REMARK 465 LYS B 181
REMARK 465 ALA B 182
REMARK 465 SER B 183
REMARK 465 SER C 4
REMARK 465 GLU C 211
REMARK 465 CYS C 212
REMARK 465 SER C 213
REMARK 465 GLN D 1
REMARK 465 SER D 146
REMARK 465 LYS D 147
REMARK 465 SER D 148
REMARK 465 THR D 149
REMARK 465 SER D 150
REMARK 465 GLY D 151
REMARK 465 LYS D 232
REMARK 465 SER D 233
REMARK 465 CYS D 234
REMARK 465 ASP D 235
REMARK 465 MET H 0
REMARK 465 LEU H 177
REMARK 465 ALA H 178
REMARK 465 PHE H 179
REMARK 465 GLN H 180
REMARK 465 LYS H 181
REMARK 465 ALA H 182
REMARK 465 SER H 183
REMARK 465 SER I 4
REMARK 465 GLU I 211
REMARK 465 CYS I 212
REMARK 465 SER I 213
REMARK 465 GLN J 1
REMARK 465 SER J 146
REMARK 465 LYS J 147
REMARK 465 SER J 148
REMARK 465 THR J 149
REMARK 465 SER J 150
REMARK 465 LYS J 232
REMARK 465 SER J 233
REMARK 465 CYS J 234
REMARK 465 ASP J 235
REMARK 465 MET L 0
REMARK 465 LYS L 1
REMARK 465 LYS L 2
REMARK 465 VAL L 176
REMARK 465 LEU L 177
REMARK 465 ALA L 178
REMARK 465 PHE L 179
REMARK 465 GLN L 180
REMARK 465 LYS L 181
REMARK 465 ALA L 182
REMARK 465 SER L 183
REMARK 465 SER M 4
REMARK 465 GLU M 211
REMARK 465 CYS M 212
REMARK 465 SER M 213
REMARK 465 LYS N 147
REMARK 465 SER N 148
REMARK 465 THR N 149
REMARK 465 SER N 150
REMARK 465 LYS N 232
REMARK 465 SER N 233
REMARK 465 CYS N 234
REMARK 465 ASP N 235
REMARK 465 THR O 317
REMARK 465 ARG O 318
REMARK 465 PRO O 319
REMARK 465 GLY O 320
REMARK 465 GLU O 321
REMARK 465 GLU O 492
REMARK 465 THR A 317
REMARK 465 ARG A 318
REMARK 465 PRO A 319
REMARK 465 GLY A 320
REMARK 465 GLU A 321
REMARK 465 ILE A 322
REMARK 465 GLU A 492
REMARK 465 THR K 317
REMARK 465 ARG K 318
REMARK 465 PRO K 319
REMARK 465 GLY K 320
REMARK 465 GLU K 321
REMARK 465 GLU K 492
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 VAL H 176 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN A 356 O5 NAG A 517 1.50
REMARK 500 CB LYS P 150 OG SER P 193 1.64
REMARK 500 ND2 ASN A 276 O5 NAG A 516 1.70
REMARK 500 ND2 ASN E 332 O5 NAG G 1 1.75
REMARK 500 CG LYS P 150 OG SER P 193 1.80
REMARK 500 ND2 ASN O 332 O5 NAG R 1 1.83
REMARK 500 ND2 ASN O 392 O5 NAG O 516 1.86
REMARK 500 ND2 ASN E 276 O5 NAG E 512 1.90
REMARK 500 N LYS P 150 O SER P 193 1.92
REMARK 500 O2 MAN R 4 O5 MAN R 5 1.94
REMARK 500 O2 MAN V 4 O5 MAN V 5 1.94
REMARK 500 OG SER C 93 OD1 ASP O 325 1.95
REMARK 500 NH2 ARG B 54 OD2 ASP B 78 1.96
REMARK 500 OG SER M 30 OD2 ASP A 325 1.96
REMARK 500 ND2 ASN A 262 O5 NAG A 515 1.98
REMARK 500 ND2 ASN E 411 O5 NAG E 517 2.00
REMARK 500 O4 NAG G 2 O5 BMA G 3 2.02
REMARK 500 O4 NAG V 2 O5 BMA V 3 2.02
REMARK 500 O4 NAG R 2 O5 BMA R 3 2.02
REMARK 500 O4 NAG S 2 O5 BMA S 3 2.02
REMARK 500 ND2 ASN A 339 C2 NAG U 1 2.06
REMARK 500 O3 BMA V 3 C2 MAN V 4 2.06
REMARK 500 O3 BMA R 3 C2 MAN R 4 2.06
REMARK 500 ND2 ASN K 332 C8 NAG V 1 2.11
REMARK 500 O3 NAG S 1 O5 NAG S 2 2.17
REMARK 500 O3 NAG G 1 O5 NAG G 2 2.17
REMARK 500 O3 NAG V 1 O5 NAG V 2 2.17
REMARK 500 O3 NAG R 1 O5 NAG R 2 2.17
REMARK 500 O3 MAN R 7 O5 MAN R 10 2.18
REMARK 500 O3 MAN G 7 O5 MAN G 10 2.18
REMARK 500 O3 MAN S 7 O5 MAN S 10 2.18
REMARK 500 O3 MAN V 7 O5 MAN V 10 2.18
REMARK 500 ND2 ASN E 339 C2 NAG E 514 2.19
REMARK 500 O ILE A 215 O GLY A 250 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO P 40 CD PRO P 40 N 0.163
REMARK 500 ARG N 100 CA ARG N 100 C -0.230
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO P 8 C - N - CD ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO P 40 CA - N - CD ANGL. DEV. = -9.2 DEGREES
REMARK 500 SER P 107 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 PRO Q 14 N - CA - C ANGL. DEV. = 21.0 DEGREES
REMARK 500 PRO Q 165 C - N - CD ANGL. DEV. = 18.6 DEGREES
REMARK 500 SER D 74 N - CA - CB ANGL. DEV. = 9.7 DEGREES
REMARK 500 ILE N 100A C - N - CA ANGL. DEV. = -16.4 DEGREES
REMARK 500 PRO A 206 C - N - CD ANGL. DEV. = 16.5 DEGREES
REMARK 500 PRO A 253 C - N - CD ANGL. DEV. = 12.7 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 ASN E 94 85.89 -168.89
REMARK 500 GLN E 114 -60.34 74.06
REMARK 500 THR E 123 -68.94 -138.96
REMARK 500 ASN E 230 104.14 -57.82
REMARK 500 GLU E 268 -129.71 58.06
REMARK 500 ASN E 356 8.59 80.56
REMARK 500 HIS E 374 96.95 -69.88
REMARK 500 GLU E 399 -167.43 -111.71
REMARK 500 GLN E 422 -34.39 -138.38
REMARK 500 GLU E 462 -131.57 57.14
REMARK 500 SER E 463 -0.87 83.70
REMARK 500 LYS E 485 49.65 -100.73
REMARK 500 PRO F 48 39.55 -90.30
REMARK 500 SER F 49 -168.78 -78.72
REMARK 500 ASN F 73 77.37 46.63
REMARK 500 ASN F 103 53.37 39.17
REMARK 500 THR F 106 -4.55 77.69
REMARK 500 THR F 115 9.30 89.89
REMARK 500 GLN F 165 13.40 53.71
REMARK 500 PRO P 40 134.15 -31.49
REMARK 500 ASN P 50 -130.85 47.08
REMARK 500 ALA P 128 33.23 -85.36
REMARK 500 SER P 153 2.21 86.37
REMARK 500 SER P 169 -9.94 -56.83
REMARK 500 GLU P 199 39.91 71.83
REMARK 500 GLU Q 16 -173.50 -66.70
REMARK 500 ARG Q 54 33.52 -89.64
REMARK 500 GLU Q 55 12.09 51.06
REMARK 500 SER Q 174 -115.87 49.54
REMARK 500 ASP B 10 -163.14 -78.26
REMARK 500 LYS B 21 66.32 -105.63
REMARK 500 ASN B 30 -160.41 -102.32
REMARK 500 PRO B 48 43.00 -88.16
REMARK 500 THR B 106 30.97 87.20
REMARK 500 SER B 125 56.72 -110.94
REMARK 500 ASN C 51 -116.00 66.84
REMARK 500 PRO C 59 -178.85 -68.53
REMARK 500 PRO C 66 -169.86 -78.19
REMARK 500 ASP C 92 -157.15 -115.48
REMARK 500 ASP C 152 -127.93 57.80
REMARK 500 PRO C 165 123.66 -34.83
REMARK 500 SER C 188 -7.86 -56.78
REMARK 500 SER D 28 -166.93 -114.45
REMARK 500 SER D 82B 69.35 31.67
REMARK 500 PHE D 100J 144.49 -12.29
REMARK 500 ALA D 132 -166.09 -74.73
REMARK 500 PRO D 137 -171.06 -67.79
REMARK 500 SER D 138 83.86 -158.36
REMARK 500 ASP D 162 76.08 48.21
REMARK 500 PHE D 164 134.18 -176.40
REMARK 500
REMARK 500 THIS ENTRY HAS 119 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU P 106A SER P 107 -32.04
REMARK 500 LEU M 106A SER M 107 -30.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER P 95 -12.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4R26 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PGT124 UNBOUND
DBREF 4R2G E 199 302 UNP P20871 ENV_HV1JR 197 300
DBREF 4R2G E 320 492 UNP P20871 ENV_HV1JR 317 484
DBREF 4R2G F 1 183 UNP P01730 CD4_HUMAN 26 208
DBREF 4R2G P 4 107 PDB 4R2G 4R2G 4 107
DBREF 4R2G P 108 213 UNP P0DOY3 IGLC3_HUMAN 2 106
DBREF 4R2G Q 1 108 PDB 4R2G 4R2G 1 108
DBREF 4R2G Q 109 235 UNP P0DOX5 IGG1_HUMAN 115 223
DBREF 4R2G B 1 183 UNP P01730 CD4_HUMAN 26 208
DBREF 4R2G C 4 107 PDB 4R2G 4R2G 4 107
DBREF 4R2G C 108 213 UNP P0DOY3 IGLC3_HUMAN 2 106
DBREF 4R2G D 1 108 PDB 4R2G 4R2G 1 108
DBREF 4R2G D 109 235 UNP P0DOX5 IGG1_HUMAN 115 223
DBREF 4R2G H 1 183 UNP P01730 CD4_HUMAN 26 208
DBREF 4R2G I 4 107 PDB 4R2G 4R2G 4 107
DBREF 4R2G I 108 213 UNP P0DOY3 IGLC3_HUMAN 2 106
DBREF 4R2G J 1 108 PDB 4R2G 4R2G 1 108
DBREF 4R2G J 109 235 UNP P0DOX5 IGG1_HUMAN 115 223
DBREF 4R2G L 1 183 UNP P01730 CD4_HUMAN 26 208
DBREF 4R2G M 4 107 PDB 4R2G 4R2G 4 107
DBREF 4R2G M 108 213 UNP P0DOY3 IGLC3_HUMAN 2 106
DBREF 4R2G N 1 108 PDB 4R2G 4R2G 1 108
DBREF 4R2G N 109 235 UNP P0DOX5 IGG1_HUMAN 115 223
DBREF 4R2G O 199 302 UNP P20871 ENV_HV1JR 197 300
DBREF 4R2G O 320 492 UNP P20871 ENV_HV1JR 317 484
DBREF 4R2G A 199 302 UNP P20871 ENV_HV1JR 197 300
DBREF 4R2G A 320 492 UNP P20871 ENV_HV1JR 317 484
DBREF 4R2G K 199 302 UNP P20871 ENV_HV1JR 197 300
DBREF 4R2G K 320 492 UNP P20871 ENV_HV1JR 317 484
SEQADV 4R2G ASP E 92 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PHE E 93 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN E 94 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET E 95 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP E 96 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS E 97 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN E 98 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN E 99 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET E 100 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL E 101 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU E 102 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN E 103 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET E 104 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN E 105 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU E 106 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP E 107 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL E 108 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ILE E 109 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN E 110 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU E 111 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP E 112 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP E 113 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN E 114 UNP P20871 EXPRESSION TAG
SEQADV 4R2G SER E 115 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU E 116 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS E 117 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PRO E 118 UNP P20871 EXPRESSION TAG
SEQADV 4R2G CYS E 119 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL E 120 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS E 121 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU E 122 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR E 123 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY E 197 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY E 198 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR E 317 UNP P20871 LINKER
SEQADV 4R2G ARG E 318 UNP P20871 LINKER
SEQADV 4R2G PRO E 319 UNP P20871 LINKER
SEQADV 4R2G MET F 0 UNP P01730 INITIATING METHIONINE
SEQADV 4R2G MET B 0 UNP P01730 INITIATING METHIONINE
SEQADV 4R2G MET H 0 UNP P01730 INITIATING METHIONINE
SEQADV 4R2G MET L 0 UNP P01730 INITIATING METHIONINE
SEQADV 4R2G ASP O 92 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PHE O 93 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN O 94 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET O 95 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP O 96 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS O 97 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN O 98 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN O 99 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET O 100 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL O 101 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU O 102 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN O 103 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET O 104 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN O 105 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU O 106 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP O 107 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL O 108 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ILE O 109 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN O 110 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU O 111 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP O 112 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP O 113 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN O 114 UNP P20871 EXPRESSION TAG
SEQADV 4R2G SER O 115 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU O 116 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS O 117 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PRO O 118 UNP P20871 EXPRESSION TAG
SEQADV 4R2G CYS O 119 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL O 120 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS O 121 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU O 122 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR O 123 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY O 197 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY O 198 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR O 317 UNP P20871 LINKER
SEQADV 4R2G ARG O 318 UNP P20871 LINKER
SEQADV 4R2G PRO O 319 UNP P20871 LINKER
SEQADV 4R2G ASP A 92 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PHE A 93 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN A 94 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET A 95 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP A 96 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS A 97 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN A 98 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN A 99 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET A 100 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL A 101 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU A 102 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN A 103 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET A 104 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN A 105 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU A 106 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP A 107 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL A 108 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ILE A 109 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN A 110 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU A 111 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP A 112 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP A 113 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN A 114 UNP P20871 EXPRESSION TAG
SEQADV 4R2G SER A 115 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU A 116 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS A 117 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PRO A 118 UNP P20871 EXPRESSION TAG
SEQADV 4R2G CYS A 119 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL A 120 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS A 121 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU A 122 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR A 123 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY A 197 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY A 198 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR A 317 UNP P20871 LINKER
SEQADV 4R2G ARG A 318 UNP P20871 LINKER
SEQADV 4R2G PRO A 319 UNP P20871 LINKER
SEQADV 4R2G ASP K 92 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PHE K 93 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN K 94 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET K 95 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP K 96 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS K 97 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN K 98 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN K 99 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET K 100 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL K 101 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU K 102 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN K 103 UNP P20871 EXPRESSION TAG
SEQADV 4R2G MET K 104 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN K 105 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLU K 106 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP K 107 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL K 108 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ILE K 109 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASN K 110 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU K 111 UNP P20871 EXPRESSION TAG
SEQADV 4R2G TRP K 112 UNP P20871 EXPRESSION TAG
SEQADV 4R2G ASP K 113 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLN K 114 UNP P20871 EXPRESSION TAG
SEQADV 4R2G SER K 115 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU K 116 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS K 117 UNP P20871 EXPRESSION TAG
SEQADV 4R2G PRO K 118 UNP P20871 EXPRESSION TAG
SEQADV 4R2G CYS K 119 UNP P20871 EXPRESSION TAG
SEQADV 4R2G VAL K 120 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LYS K 121 UNP P20871 EXPRESSION TAG
SEQADV 4R2G LEU K 122 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR K 123 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY K 197 UNP P20871 EXPRESSION TAG
SEQADV 4R2G GLY K 198 UNP P20871 EXPRESSION TAG
SEQADV 4R2G THR K 317 UNP P20871 LINKER
SEQADV 4R2G ARG K 318 UNP P20871 LINKER
SEQADV 4R2G PRO K 319 UNP P20871 LINKER
SEQRES 1 E 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET
SEQRES 2 E 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS
SEQRES 3 E 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN
SEQRES 4 E 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS
SEQRES 5 E 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN
SEQRES 6 E 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL
SEQRES 7 E 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL
SEQRES 8 E 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU
SEQRES 9 E 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA
SEQRES 10 E 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE
SEQRES 11 E 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU
SEQRES 12 E 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER
SEQRES 13 E 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU
SEQRES 14 E 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE
SEQRES 15 E 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS
SEQRES 16 E 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER
SEQRES 17 E 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS
SEQRES 18 E 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO
SEQRES 19 E 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL
SEQRES 20 E 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE
SEQRES 21 E 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG
SEQRES 22 E 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG
SEQRES 23 E 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU
SEQRES 24 E 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU
SEQRES 1 F 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL
SEQRES 2 F 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN
SEQRES 3 F 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY
SEQRES 4 F 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU
SEQRES 5 F 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN
SEQRES 6 F 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU
SEQRES 7 F 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS
SEQRES 8 F 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN
SEQRES 9 F 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU
SEQRES 10 F 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN
SEQRES 11 F 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS
SEQRES 12 F 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY
SEQRES 13 F 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL
SEQRES 14 F 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 15 F 184 ALA SER
SEQRES 1 P 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR
SEQRES 2 P 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG
SEQRES 3 P 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO
SEQRES 4 P 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY
SEQRES 5 P 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE
SEQRES 6 P 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL
SEQRES 7 P 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER
SEQRES 8 P 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG
SEQRES 9 P 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 P 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 P 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 P 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 P 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 P 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 P 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS
SEQRES 16 P 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 P 214 ALA PRO THR GLU CYS SER
SEQRES 1 Q 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG
SEQRES 2 Q 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY
SEQRES 3 Q 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN
SEQRES 4 Q 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER
SEQRES 5 Q 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER
SEQRES 6 Q 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU
SEQRES 7 Q 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA
SEQRES 8 Q 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE
SEQRES 9 Q 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR
SEQRES 10 Q 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL
SEQRES 11 Q 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 12 Q 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 13 Q 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 14 Q 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 15 Q 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 16 Q 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 17 Q 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 18 Q 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 19 Q 236 CYS ASP
SEQRES 1 B 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL
SEQRES 2 B 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN
SEQRES 3 B 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY
SEQRES 4 B 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU
SEQRES 5 B 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN
SEQRES 6 B 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU
SEQRES 7 B 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS
SEQRES 8 B 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN
SEQRES 9 B 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU
SEQRES 10 B 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN
SEQRES 11 B 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS
SEQRES 12 B 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY
SEQRES 13 B 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL
SEQRES 14 B 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 15 B 184 ALA SER
SEQRES 1 C 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR
SEQRES 2 C 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG
SEQRES 3 C 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO
SEQRES 4 C 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY
SEQRES 5 C 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE
SEQRES 6 C 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL
SEQRES 7 C 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER
SEQRES 8 C 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG
SEQRES 9 C 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 C 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 C 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 C 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 C 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 C 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 C 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS
SEQRES 16 C 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 C 214 ALA PRO THR GLU CYS SER
SEQRES 1 D 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG
SEQRES 2 D 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY
SEQRES 3 D 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN
SEQRES 4 D 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER
SEQRES 5 D 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER
SEQRES 6 D 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU
SEQRES 7 D 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA
SEQRES 8 D 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE
SEQRES 9 D 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR
SEQRES 10 D 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL
SEQRES 11 D 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 12 D 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 13 D 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 14 D 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 15 D 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 16 D 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 17 D 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 18 D 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 19 D 236 CYS ASP
SEQRES 1 H 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL
SEQRES 2 H 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN
SEQRES 3 H 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY
SEQRES 4 H 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU
SEQRES 5 H 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN
SEQRES 6 H 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU
SEQRES 7 H 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS
SEQRES 8 H 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN
SEQRES 9 H 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU
SEQRES 10 H 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN
SEQRES 11 H 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS
SEQRES 12 H 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY
SEQRES 13 H 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL
SEQRES 14 H 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 15 H 184 ALA SER
SEQRES 1 I 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR
SEQRES 2 I 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG
SEQRES 3 I 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO
SEQRES 4 I 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY
SEQRES 5 I 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE
SEQRES 6 I 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL
SEQRES 7 I 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER
SEQRES 8 I 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG
SEQRES 9 I 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 I 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 I 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 I 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 I 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 I 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 I 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS
SEQRES 16 I 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 I 214 ALA PRO THR GLU CYS SER
SEQRES 1 J 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG
SEQRES 2 J 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY
SEQRES 3 J 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN
SEQRES 4 J 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER
SEQRES 5 J 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER
SEQRES 6 J 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU
SEQRES 7 J 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA
SEQRES 8 J 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE
SEQRES 9 J 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR
SEQRES 10 J 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL
SEQRES 11 J 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 12 J 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 13 J 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 14 J 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 15 J 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 16 J 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 17 J 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 18 J 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 19 J 236 CYS ASP
SEQRES 1 L 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL
SEQRES 2 L 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN
SEQRES 3 L 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY
SEQRES 4 L 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU
SEQRES 5 L 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN
SEQRES 6 L 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU
SEQRES 7 L 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS
SEQRES 8 L 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN
SEQRES 9 L 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU
SEQRES 10 L 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN
SEQRES 11 L 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS
SEQRES 12 L 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY
SEQRES 13 L 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL
SEQRES 14 L 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 15 L 184 ALA SER
SEQRES 1 M 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR
SEQRES 2 M 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG
SEQRES 3 M 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO
SEQRES 4 M 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY
SEQRES 5 M 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE
SEQRES 6 M 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL
SEQRES 7 M 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER
SEQRES 8 M 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG
SEQRES 9 M 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 M 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 M 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 M 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 M 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 M 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 M 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS
SEQRES 16 M 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 M 214 ALA PRO THR GLU CYS SER
SEQRES 1 N 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG
SEQRES 2 N 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY
SEQRES 3 N 236 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN
SEQRES 4 N 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER
SEQRES 5 N 236 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER
SEQRES 6 N 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU
SEQRES 7 N 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA
SEQRES 8 N 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE
SEQRES 9 N 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR
SEQRES 10 N 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL
SEQRES 11 N 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 12 N 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 13 N 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 14 N 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 15 N 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 16 N 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 17 N 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 18 N 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 19 N 236 CYS ASP
SEQRES 1 O 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET
SEQRES 2 O 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS
SEQRES 3 O 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN
SEQRES 4 O 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS
SEQRES 5 O 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN
SEQRES 6 O 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL
SEQRES 7 O 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL
SEQRES 8 O 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU
SEQRES 9 O 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA
SEQRES 10 O 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE
SEQRES 11 O 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU
SEQRES 12 O 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER
SEQRES 13 O 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU
SEQRES 14 O 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE
SEQRES 15 O 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS
SEQRES 16 O 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER
SEQRES 17 O 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS
SEQRES 18 O 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO
SEQRES 19 O 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL
SEQRES 20 O 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE
SEQRES 21 O 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG
SEQRES 22 O 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG
SEQRES 23 O 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU
SEQRES 24 O 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU
SEQRES 1 A 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET
SEQRES 2 A 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS
SEQRES 3 A 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN
SEQRES 4 A 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS
SEQRES 5 A 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN
SEQRES 6 A 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL
SEQRES 7 A 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL
SEQRES 8 A 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU
SEQRES 9 A 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA
SEQRES 10 A 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE
SEQRES 11 A 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU
SEQRES 12 A 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER
SEQRES 13 A 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU
SEQRES 14 A 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE
SEQRES 15 A 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS
SEQRES 16 A 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER
SEQRES 17 A 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS
SEQRES 18 A 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO
SEQRES 19 A 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL
SEQRES 20 A 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE
SEQRES 21 A 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG
SEQRES 22 A 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG
SEQRES 23 A 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU
SEQRES 24 A 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU
SEQRES 1 K 309 ASP PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN MET
SEQRES 2 K 309 GLN GLU ASP VAL ILE ASN LEU TRP ASP GLN SER LEU LYS
SEQRES 3 K 309 PRO CYS VAL LYS LEU THR GLY GLY SER VAL ILE THR GLN
SEQRES 4 K 309 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS
SEQRES 5 K 309 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN
SEQRES 6 K 309 ASN LYS THR PHE ASN GLY LYS GLY GLN CYS LYS ASN VAL
SEQRES 7 K 309 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL
SEQRES 8 K 309 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU
SEQRES 9 K 309 LYS VAL VAL ILE ARG SER ASP ASN PHE THR ASP ASN ALA
SEQRES 10 K 309 LYS THR ILE ILE VAL GLN LEU ASN GLU SER VAL LYS ILE
SEQRES 11 K 309 ASN CYS THR ARG PRO SER ASN ASN THR ARG PRO GLY GLU
SEQRES 12 K 309 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER
SEQRES 13 K 309 ARG ALA GLN TRP ASN ASN THR LEU LYS GLN ILE VAL GLU
SEQRES 14 K 309 LYS LEU ARG GLU GLN PHE ASN ASN LYS THR ILE VAL PHE
SEQRES 15 K 309 THR HIS SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS
SEQRES 16 K 309 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SER
SEQRES 17 K 309 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU LYS
SEQRES 18 K 309 SER SER GLY THR GLU GLY ASN ASP THR ILE ILE LEU PRO
SEQRES 19 K 309 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL
SEQRES 20 K 309 GLY LYS ALA MET TYR ALA PRO PRO ILE LYS GLY GLN ILE
SEQRES 21 K 309 ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG
SEQRES 22 K 309 ASP GLY GLY LYS ASN GLU SER GLU ILE GLU ILE PHE ARG
SEQRES 23 K 309 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU
SEQRES 24 K 309 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU
MODRES 4R2G ASN O 332 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 386 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 276 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 339 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN O 448 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 392 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 448 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 411 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 392 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 262 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN O 276 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 295 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN O 386 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 339 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN K 339 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN K 276 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 276 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN O 262 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 386 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN K 332 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN K 295 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 332 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN K 386 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 356 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN E 448 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN O 295 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 295 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN O 339 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN K 262 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 262 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN O 392 ASN GLYCOSYLATION SITE
MODRES 4R2G ASN A 332 ASN GLYCOSYLATION SITE
MODRES 4R2G THR K 404 THR GLYCOSYLATION SITE
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 MAN G 6 11
HET MAN G 7 11
HET MAN G 8 11
HET MAN G 9 11
HET MAN G 10 11
HET NAG R 1 14
HET NAG R 2 14
HET BMA R 3 11
HET MAN R 4 11
HET MAN R 5 11
HET MAN R 6 11
HET MAN R 7 11
HET MAN R 8 11
HET MAN R 9 11
HET MAN R 10 11
HET NAG S 1 14
HET NAG S 2 14
HET BMA S 3 11
HET MAN S 4 11
HET MAN S 5 11
HET MAN S 6 11
HET MAN S 7 11
HET MAN S 8 11
HET MAN S 9 11
HET MAN S 10 11
HET NAG T 1 14
HET NAG T 2 14
HET NAG U 1 14
HET NAG U 2 14
HET NAG V 1 14
HET NAG V 2 14
HET BMA V 3 11
HET MAN V 4 11
HET MAN V 5 11
HET MAN V 6 11
HET MAN V 7 11
HET MAN V 8 11
HET MAN V 9 11
HET MAN V 10 11
HET NAG E 511 14
HET NAG E 512 14
HET NAG E 513 14
HET NAG E 514 14
HET NAG E 515 14
HET NAG E 516 14
HET NAG E 517 14
HET NAG E 518 14
HET CL E 519 1
HET GOL Q 301 6
HET GOL D 301 6
HET GOL J 301 6
HET GOL N 301 6
HET NAG O 511 14
HET NAG O 512 14
HET NAG O 513 14
HET NAG O 514 14
HET NAG O 515 14
HET NAG O 516 14
HET NAG O 517 14
HET CL O 518 1
HET NAG A 515 14
HET NAG A 516 14
HET NAG A 517 14
HET NAG A 518 14
HET NAG A 519 14
HET NAG A 520 14
HET CL A 521 1
HET NAG K 511 14
HET NAG K 512 14
HET NAG K 513 14
HET NAG K 514 14
HET NAG K 515 14
HET CL K 516 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 17 NAG 38(C8 H15 N O6)
FORMUL 17 BMA 4(C6 H12 O6)
FORMUL 17 MAN 28(C6 H12 O6)
FORMUL 31 CL 4(CL 1-)
FORMUL 32 GOL 4(C3 H8 O3)
HELIX 1 1 ASN E 94 ASN E 98 5 5
HELIX 2 2 ASN E 99 LEU E 116 1 18
HELIX 3 3 ARG E 335 PHE E 353 1 19
HELIX 4 4 ASP E 368 MET E 373 1 6
HELIX 5 5 SER E 387 PHE E 391 5 5
HELIX 6 6 ASP E 474 TYR E 484 1 11
HELIX 7 7 ARG F 58 GLY F 65 5 8
HELIX 8 8 LYS F 75 SER F 79 5 5
HELIX 9 9 GLU P 79 GLU P 83 5 5
HELIX 10 10 SER P 122 ALA P 128 1 7
HELIX 11 11 THR P 182 SER P 188 1 7
HELIX 12 12 SER Q 28 TYR Q 32 5 5
HELIX 13 13 PRO Q 61 ASN Q 64 5 4
HELIX 14 14 THR Q 83 THR Q 87 5 5
HELIX 15 15 VAL Q 100D GLY Q 100H 5 5
HELIX 16 16 SER Q 205 LEU Q 207 5 3
HELIX 17 17 SER B 49 ASP B 53 5 5
HELIX 18 18 ARG B 58 GLY B 65 5 8
HELIX 19 19 GLU B 150 SER B 154 5 5
HELIX 20 20 GLU C 79 GLU C 83 5 5
HELIX 21 21 SER C 122 ALA C 128 1 7
HELIX 22 22 THR C 182 HIS C 189 1 8
HELIX 23 23 PRO D 61 ASN D 64 5 4
HELIX 24 24 THR D 83 THR D 87 5 5
HELIX 25 25 ARG H 58 ASP H 63 1 6
HELIX 26 26 LYS H 75 SER H 79 5 5
HELIX 27 27 GLU I 79 GLU I 83 5 5
HELIX 28 28 SER I 122 ALA I 128 1 7
HELIX 29 29 THR I 182 SER I 188 1 7
HELIX 30 30 SER J 28 TYR J 32 5 5
HELIX 31 31 PRO J 61 ASN J 64 5 4
HELIX 32 32 VAL J 100D GLY J 100H 5 5
HELIX 33 33 SER J 205 LEU J 207 5 3
HELIX 34 34 ARG L 58 GLY L 65 5 8
HELIX 35 35 LYS L 75 SER L 79 5 5
HELIX 36 36 GLU L 150 SER L 154 5 5
HELIX 37 37 GLU M 79 GLU M 83 5 5
HELIX 38 38 SER M 122 GLN M 127 1 6
HELIX 39 39 THR M 182 SER M 188 1 7
HELIX 40 40 PRO N 61 ASN N 64 5 4
HELIX 41 41 THR N 83 THR N 87 5 5
HELIX 42 42 SER N 174 LEU N 177 5 4
HELIX 43 43 ASN O 99 LEU O 116 1 18
HELIX 44 44 ARG O 335 PHE O 353 1 19
HELIX 45 45 ASP O 368 MET O 373 1 6
HELIX 46 46 ASP O 474 TYR O 484 1 11
HELIX 47 47 TRP A 96 ASN A 98 5 3
HELIX 48 48 ASN A 99 LEU A 116 1 18
HELIX 49 49 ARG A 335 PHE A 353 1 19
HELIX 50 50 ASP A 368 MET A 373 1 6
HELIX 51 51 ASP A 474 TYR A 484 1 11
HELIX 52 52 MET K 100 LEU K 116 1 17
HELIX 53 53 ARG K 335 PHE K 353 1 19
HELIX 54 54 ASP K 368 MET K 373 1 6
HELIX 55 55 ASP K 474 TYR K 484 1 11
SHEET 1 A 3 VAL E 120 LEU E 122 0
SHEET 2 A 3 LYS E 432 MET E 434 -1 O LYS E 432 N LEU E 122
SHEET 3 A 3 ILE E 423 ASN E 425 -1 N ILE E 424 O ALA E 433
SHEET 1 B 3 VAL E 242 VAL E 245 0
SHEET 2 B 3 PHE E 223 CYS E 228 -1 N LYS E 227 O SER E 243
SHEET 3 B 3 LYS E 487 LYS E 490 -1 O LYS E 487 N LEU E 226
SHEET 1 C 7 LEU E 259 LEU E 261 0
SHEET 2 C 7 ILE E 443 ARG E 456 -1 O GLY E 451 N LEU E 260
SHEET 3 C 7 ILE E 284 ARG E 298 -1 N ILE E 294 O SER E 447
SHEET 4 C 7 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295
SHEET 5 C 7 THR E 413 LYS E 421 -1 O LEU E 416 N CYS E 331
SHEET 6 C 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419
SHEET 7 C 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385
SHEET 1 D 7 VAL E 271 ARG E 273 0
SHEET 2 D 7 ILE E 284 ARG E 298 -1 O GLN E 287 N VAL E 271
SHEET 3 D 7 ILE E 443 ARG E 456 -1 O SER E 447 N ILE E 294
SHEET 4 D 7 ILE E 465 PRO E 470 -1 O ARG E 469 N THR E 455
SHEET 5 D 7 THR E 358 PHE E 361 1 N VAL E 360 O PHE E 468
SHEET 6 D 7 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359
SHEET 7 D 7 SER E 401 SER E 402 -1 O SER E 402 N THR E 394
SHEET 1 E 6 LYS F 2 LYS F 7 0
SHEET 2 E 6 LYS F 90 THR F 101 1 O LEU F 96 N VAL F 4
SHEET 3 E 6 ASP F 80 VAL F 86 -1 N ASP F 80 O LEU F 95
SHEET 4 E 6 PHE F 26 ASN F 30 -1 N LYS F 29 O ILE F 83
SHEET 5 E 6 LYS F 35 GLN F 40 -1 O LEU F 37 N TRP F 28
SHEET 6 E 6 PHE F 43 LYS F 46 -1 O THR F 45 N GLY F 38
SHEET 1 F 4 LYS F 2 LYS F 7 0
SHEET 2 F 4 LYS F 90 THR F 101 1 O LEU F 96 N VAL F 4
SHEET 3 F 4 THR F 115 GLU F 119 -1 O THR F 117 N THR F 101
SHEET 4 F 4 THR F 143 SER F 145 -1 O LEU F 144 N LEU F 116
SHEET 1 G 3 VAL F 12 LEU F 14 0
SHEET 2 G 3 LEU F 69 ILE F 71 -1 O LEU F 69 N LEU F 14
SHEET 3 G 3 ALA F 55 ASP F 56 -1 N ASP F 56 O ILE F 70
SHEET 1 H 4 ASN F 137 GLY F 140 0
SHEET 2 H 4 SER F 127 ARG F 131 -1 N CYS F 130 O ILE F 138
SHEET 3 H 4 GLY F 155 GLN F 163 -1 O THR F 160 N GLN F 129
SHEET 4 H 4 LYS F 166 ILE F 174 -1 O ILE F 174 N GLY F 155
SHEET 1 I 5 PRO P 8 ALA P 14 0
SHEET 2 I 5 ALA P 101 LEU P 106A 1 O LEU P 106A N VAL P 13
SHEET 3 I 5 ASP P 85 HIS P 89 -1 N TYR P 86 O THR P 102
SHEET 4 I 5 GLN P 34 HIS P 38 -1 N GLN P 34 O HIS P 89
SHEET 5 I 5 ILE P 45 ILE P 48 -1 O ILE P 45 N GLN P 37
SHEET 1 J 3 ALA P 19 SER P 22 0
SHEET 2 J 3 THR P 72 ILE P 75 -1 O ILE P 75 N ALA P 19
SHEET 3 J 3 PHE P 62 SER P 63 -1 N SER P 63 O THR P 74
SHEET 1 K 3 ALA P 131 PHE P 140 0
SHEET 2 K 3 TYR P 173 LEU P 181 -1 O LEU P 181 N ALA P 131
SHEET 3 K 3 VAL P 160 THR P 162 -1 N GLU P 161 O TYR P 178
SHEET 1 L 3 ALA P 131 PHE P 140 0
SHEET 2 L 3 TYR P 173 LEU P 181 -1 O LEU P 181 N ALA P 131
SHEET 3 L 3 SER P 166 LYS P 167 -1 N SER P 166 O ALA P 174
SHEET 1 M 3 THR P 146 TRP P 149 0
SHEET 2 M 3 TYR P 192 THR P 197 -1 O GLN P 195 N ALA P 148
SHEET 3 M 3 THR P 202 VAL P 207 -1 O VAL P 203 N VAL P 196
SHEET 1 N 4 GLN Q 3 SER Q 7 0
SHEET 2 N 4 LEU Q 18 SER Q 25 -1 O THR Q 21 N SER Q 7
SHEET 3 N 4 GLN Q 77 LEU Q 82 -1 O LEU Q 80 N VAL Q 20
SHEET 4 N 4 ALA Q 67 ASP Q 72 -1 N ASP Q 72 O GLN Q 77
SHEET 1 O 6 LEU Q 11 VAL Q 12 0
SHEET 2 O 6 THR Q 107 VAL Q 111 1 O THR Q 110 N VAL Q 12
SHEET 3 O 6 ALA Q 88 ILE Q 100A-1 N TYR Q 90 O THR Q 107
SHEET 4 O 6 TYR Q 33 GLN Q 39 -1 N ILE Q 37 O PHE Q 91
SHEET 5 O 6 LEU Q 45 ILE Q 51 -1 O ILE Q 51 N TRP Q 34
SHEET 6 O 6 THR Q 57 TYR Q 59 -1 O THR Q 58 N TYR Q 50
SHEET 1 P 4 LEU Q 11 VAL Q 12 0
SHEET 2 P 4 THR Q 107 VAL Q 111 1 O THR Q 110 N VAL Q 12
SHEET 3 P 4 ALA Q 88 ILE Q 100A-1 N TYR Q 90 O THR Q 107
SHEET 4 P 4 PHE Q 100J TYR Q 100O-1 O PHE Q 100K N ARG Q 100
SHEET 1 Q 4 SER Q 138 LEU Q 142 0
SHEET 2 Q 4 THR Q 153 TYR Q 163 -1 O GLY Q 157 N LEU Q 142
SHEET 3 Q 4 TYR Q 194 PRO Q 203 -1 O VAL Q 202 N ALA Q 154
SHEET 4 Q 4 VAL Q 181 THR Q 183 -1 N HIS Q 182 O VAL Q 199
SHEET 1 R 4 SER Q 138 LEU Q 142 0
SHEET 2 R 4 THR Q 153 TYR Q 163 -1 O GLY Q 157 N LEU Q 142
SHEET 3 R 4 TYR Q 194 PRO Q 203 -1 O VAL Q 202 N ALA Q 154
SHEET 4 R 4 VAL Q 187 LEU Q 188 -1 N VAL Q 187 O SER Q 195
SHEET 1 S 3 THR Q 169 TRP Q 172 0
SHEET 2 S 3 TYR Q 212 HIS Q 218 -1 O ASN Q 217 N THR Q 169
SHEET 3 S 3 THR Q 223 VAL Q 229 -1 O VAL Q 225 N VAL Q 216
SHEET 1 T 6 LYS B 2 LYS B 7 0
SHEET 2 T 6 LYS B 90 THR B 101 1 O GLN B 94 N LYS B 2
SHEET 3 T 6 ASP B 80 VAL B 86 -1 N ASP B 80 O LEU B 95
SHEET 4 T 6 PHE B 26 LYS B 29 -1 N LYS B 29 O ILE B 83
SHEET 5 T 6 LYS B 35 GLN B 40 -1 O LEU B 37 N TRP B 28
SHEET 6 T 6 PHE B 43 LYS B 46 -1 O THR B 45 N GLY B 38
SHEET 1 U 4 LYS B 2 LYS B 7 0
SHEET 2 U 4 LYS B 90 THR B 101 1 O GLN B 94 N LYS B 2
SHEET 3 U 4 LEU B 114 GLU B 119 -1 O THR B 117 N THR B 101
SHEET 4 U 4 THR B 143 VAL B 146 -1 O LEU B 144 N LEU B 116
SHEET 1 V 3 VAL B 12 LEU B 14 0
SHEET 2 V 3 LEU B 69 ILE B 71 -1 O LEU B 69 N LEU B 14
SHEET 3 V 3 ALA B 55 ASP B 56 -1 N ASP B 56 O ILE B 70
SHEET 1 W 4 ASN B 137 GLY B 140 0
SHEET 2 W 4 SER B 127 ARG B 131 -1 N CYS B 130 O ILE B 138
SHEET 3 W 4 GLY B 155 GLN B 163 -1 O THR B 160 N GLN B 129
SHEET 4 W 4 LYS B 166 ILE B 174 -1 O ILE B 174 N GLY B 155
SHEET 1 X 5 SER C 7 ALA C 14 0
SHEET 2 X 5 ALA C 101 LEU C 106A 1 O ARG C 103 N SER C 7
SHEET 3 X 5 ALA C 84 TRP C 91 -1 N ALA C 84 O LEU C 104
SHEET 4 X 5 ALA C 32 HIS C 38 -1 N ALA C 32 O TRP C 91
SHEET 5 X 5 ILE C 45 ILE C 48 -1 O ILE C 45 N GLN C 37
SHEET 1 Y 3 ALA C 19 SER C 22 0
SHEET 2 Y 3 THR C 72 ILE C 75 -1 O LEU C 73 N ILE C 21
SHEET 3 Y 3 PHE C 62 SER C 63 -1 N SER C 63 O THR C 74
SHEET 1 Z 4 THR C 117 PHE C 119 0
SHEET 2 Z 4 ALA C 131 PHE C 140 -1 O LEU C 136 N THR C 117
SHEET 3 Z 4 TYR C 173 LEU C 181 -1 O TYR C 173 N PHE C 140
SHEET 4 Z 4 VAL C 160 THR C 162 -1 N GLU C 161 O TYR C 178
SHEET 1 AA 4 SER C 154 PRO C 155 0
SHEET 2 AA 4 THR C 146 ALA C 151 -1 N ALA C 151 O SER C 154
SHEET 3 AA 4 TYR C 192 HIS C 198 -1 O GLN C 195 N ALA C 148
SHEET 4 AA 4 SER C 201 VAL C 207 -1 O LYS C 205 N CYS C 194
SHEET 1 AB 4 LEU D 4 SER D 7 0
SHEET 2 AB 4 LEU D 18 VAL D 24 -1 O THR D 21 N SER D 7
SHEET 3 AB 4 GLN D 77 LEU D 82 -1 O LEU D 80 N VAL D 20
SHEET 4 AB 4 ALA D 67 ASP D 72 -1 N SER D 70 O SER D 79
SHEET 1 AC 6 LEU D 11 VAL D 12 0
SHEET 2 AC 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12
SHEET 3 AC 6 ALA D 88 ARG D 100 -1 N TYR D 90 O THR D 107
SHEET 4 AC 6 TYR D 33 GLN D 39 -1 N ILE D 37 O PHE D 91
SHEET 5 AC 6 LEU D 45 ILE D 51 -1 O ILE D 51 N TRP D 34
SHEET 6 AC 6 THR D 57 TYR D 59 -1 O THR D 58 N TYR D 50
SHEET 1 AD 4 LEU D 11 VAL D 12 0
SHEET 2 AD 4 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12
SHEET 3 AD 4 ALA D 88 ARG D 100 -1 N TYR D 90 O THR D 107
SHEET 4 AD 4 PHE D 100K TRP D 103 -1 O PHE D 100K N ARG D 100
SHEET 1 AE 4 VAL D 139 LEU D 142 0
SHEET 2 AE 4 THR D 153 TYR D 163 -1 O LEU D 159 N PHE D 140
SHEET 3 AE 4 TYR D 194 PRO D 203 -1 O TYR D 194 N TYR D 163
SHEET 4 AE 4 VAL D 181 THR D 183 -1 N HIS D 182 O VAL D 199
SHEET 1 AF 3 THR D 169 TRP D 172 0
SHEET 2 AF 3 ILE D 213 ASN D 217 -1 O ASN D 217 N THR D 169
SHEET 3 AF 3 LYS D 227 LYS D 228 -1 O LYS D 227 N CYS D 214
SHEET 1 AG 6 VAL H 3 LYS H 7 0
SHEET 2 AG 6 LYS H 90 ALA H 102 1 O LEU H 96 N GLY H 6
SHEET 3 AG 6 ASP H 80 GLU H 85 -1 N TYR H 82 O VAL H 93
SHEET 4 AG 6 HIS H 27 LYS H 29 -1 N LYS H 29 O ILE H 83
SHEET 5 AG 6 LYS H 35 GLN H 40 -1 O ILE H 36 N TRP H 28
SHEET 6 AG 6 PHE H 43 LYS H 46 -1 O THR H 45 N GLY H 38
SHEET 1 AH 3 VAL H 3 LYS H 7 0
SHEET 2 AH 3 LYS H 90 ALA H 102 1 O LEU H 96 N GLY H 6
SHEET 3 AH 3 LEU H 116 GLU H 119 -1 O THR H 117 N THR H 101
SHEET 1 AI 3 VAL H 12 LEU H 14 0
SHEET 2 AI 3 LEU H 69 ILE H 71 -1 O ILE H 71 N VAL H 12
SHEET 3 AI 3 ALA H 55 ASP H 56 -1 N ASP H 56 O ILE H 70
SHEET 1 AJ 4 ASN H 137 GLY H 140 0
SHEET 2 AJ 4 SER H 127 ARG H 131 -1 N CYS H 130 O ILE H 138
SHEET 3 AJ 4 THR H 156 GLN H 163 -1 O THR H 158 N ARG H 131
SHEET 4 AJ 4 LYS H 166 ASP H 173 -1 O ILE H 172 N TRP H 157
SHEET 1 AK 5 SER I 7 ALA I 14 0
SHEET 2 AK 5 ALA I 101 LEU I 106A 1 O ALA I 101 N SER I 7
SHEET 3 AK 5 ALA I 84 ASP I 92 -1 N ALA I 84 O LEU I 104
SHEET 4 AK 5 ARG I 31 HIS I 38 -1 N TYR I 36 O TYR I 87
SHEET 5 AK 5 ILE I 45 ILE I 48 -1 O ILE I 45 N GLN I 37
SHEET 1 AL 3 ALA I 19 SER I 22 0
SHEET 2 AL 3 THR I 72 ILE I 75 -1 O ILE I 75 N ALA I 19
SHEET 3 AL 3 PHE I 62 SER I 63 -1 N SER I 63 O THR I 74
SHEET 1 AM 4 SER I 115 PHE I 119 0
SHEET 2 AM 4 ALA I 131 PHE I 140 -1 O SER I 138 N SER I 115
SHEET 3 AM 4 TYR I 173 LEU I 181 -1 O LEU I 179 N LEU I 133
SHEET 4 AM 4 VAL I 160 THR I 162 -1 N GLU I 161 O TYR I 178
SHEET 1 AN 4 SER I 154 PRO I 155 0
SHEET 2 AN 4 THR I 146 ALA I 151 -1 N ALA I 151 O SER I 154
SHEET 3 AN 4 TYR I 192 THR I 197 -1 O THR I 197 N THR I 146
SHEET 4 AN 4 THR I 202 VAL I 207 -1 O VAL I 203 N VAL I 196
SHEET 1 AO 4 LEU J 4 SER J 7 0
SHEET 2 AO 4 LEU J 18 VAL J 24 -1 O ILE J 23 N GLN J 5
SHEET 3 AO 4 GLN J 77 LEU J 82 -1 O LEU J 80 N VAL J 20
SHEET 4 AO 4 ALA J 67 ASP J 72 -1 N SER J 70 O SER J 79
SHEET 1 AP 6 LEU J 11 VAL J 12 0
SHEET 2 AP 6 THR J 107 VAL J 111 1 O THR J 110 N VAL J 12
SHEET 3 AP 6 ALA J 88 THR J 94 -1 N TYR J 90 O THR J 107
SHEET 4 AP 6 TRP J 34 GLN J 39 -1 N ILE J 37 O PHE J 91
SHEET 5 AP 6 LEU J 45 ILE J 51 -1 O GLU J 46 N ARG J 38
SHEET 6 AP 6 THR J 57 TYR J 59 -1 O THR J 58 N TYR J 50
SHEET 1 AQ 2 ARG J 96 ILE J 100A 0
SHEET 2 AQ 2 PHE J 100J TYR J 100O-1 O TYR J 100O N ARG J 96
SHEET 1 AR 4 SER J 138 LEU J 142 0
SHEET 2 AR 4 THR J 153 LYS J 161 -1 O GLY J 157 N LEU J 142
SHEET 3 AR 4 SER J 197 PRO J 203 -1 O VAL J 202 N ALA J 154
SHEET 4 AR 4 HIS J 182 THR J 183 -1 N HIS J 182 O VAL J 199
SHEET 1 AS 3 THR J 169 TRP J 172 0
SHEET 2 AS 3 TYR J 212 HIS J 218 -1 O ASN J 215 N SER J 171
SHEET 3 AS 3 THR J 223 VAL J 229 -1 O VAL J 225 N VAL J 216
SHEET 1 AT 6 VAL L 4 LYS L 7 0
SHEET 2 AT 6 LYS L 90 PHE L 98 1 O LEU L 96 N GLY L 6
SHEET 3 AT 6 ASP L 80 VAL L 86 -1 N CYS L 84 O GLU L 91
SHEET 4 AT 6 PHE L 26 LYS L 29 -1 N HIS L 27 O GLU L 85
SHEET 5 AT 6 LYS L 35 GLN L 40 -1 O LEU L 37 N TRP L 28
SHEET 6 AT 6 PHE L 43 LYS L 46 -1 O THR L 45 N GLY L 38
SHEET 1 AU 3 VAL L 12 LEU L 14 0
SHEET 2 AU 3 LEU L 69 ILE L 71 -1 O LEU L 69 N LEU L 14
SHEET 3 AU 3 ALA L 55 ASP L 56 -1 N ASP L 56 O ILE L 70
SHEET 1 AV 2 LEU L 114 THR L 117 0
SHEET 2 AV 2 THR L 143 VAL L 146 -1 O VAL L 146 N LEU L 114
SHEET 1 AW 4 ASN L 137 GLY L 141 0
SHEET 2 AW 4 SER L 127 ARG L 131 -1 N CYS L 130 O ILE L 138
SHEET 3 AW 4 GLY L 155 GLN L 163 -1 O THR L 160 N GLN L 129
SHEET 4 AW 4 LYS L 166 ILE L 174 -1 O PHE L 170 N CYS L 159
SHEET 1 AX 5 VAL M 6 ALA M 14 0
SHEET 2 AX 5 ALA M 101 LEU M 106A 1 O ALA M 101 N SER M 7
SHEET 3 AX 5 ASP M 85 ASP M 92 -1 N TYR M 86 O THR M 102
SHEET 4 AX 5 ARG M 31 HIS M 38 -1 N TYR M 36 O TYR M 87
SHEET 5 AX 5 ILE M 45 ILE M 48 -1 O ILE M 48 N TRP M 35
SHEET 1 AY 3 ALA M 19 SER M 22 0
SHEET 2 AY 3 THR M 72 ILE M 75 -1 O ILE M 75 N ALA M 19
SHEET 3 AY 3 PHE M 62 SER M 63 -1 N SER M 63 O THR M 74
SHEET 1 AZ 4 SER M 115 PHE M 119 0
SHEET 2 AZ 4 ALA M 131 PHE M 140 -1 O LEU M 136 N THR M 117
SHEET 3 AZ 4 TYR M 173 LEU M 181 -1 O TYR M 173 N PHE M 140
SHEET 4 AZ 4 VAL M 160 THR M 162 -1 N GLU M 161 O TYR M 178
SHEET 1 BA 4 SER M 115 PHE M 119 0
SHEET 2 BA 4 ALA M 131 PHE M 140 -1 O LEU M 136 N THR M 117
SHEET 3 BA 4 TYR M 173 LEU M 181 -1 O TYR M 173 N PHE M 140
SHEET 4 BA 4 SER M 166 LYS M 167 -1 N SER M 166 O ALA M 174
SHEET 1 BB 4 SER M 154 PRO M 155 0
SHEET 2 BB 4 THR M 146 ALA M 151 -1 N ALA M 151 O SER M 154
SHEET 3 BB 4 TYR M 192 HIS M 198 -1 O GLN M 195 N ALA M 148
SHEET 4 BB 4 SER M 201 VAL M 207 -1 O VAL M 203 N VAL M 196
SHEET 1 BC 4 GLN N 3 SER N 7 0
SHEET 2 BC 4 LEU N 18 SER N 25 -1 O SER N 25 N GLN N 3
SHEET 3 BC 4 GLN N 77 LEU N 82 -1 O LEU N 78 N CYS N 22
SHEET 4 BC 4 ALA N 67 ASP N 72 -1 N ASP N 72 O GLN N 77
SHEET 1 BD 6 LEU N 11 VAL N 12 0
SHEET 2 BD 6 THR N 107 VAL N 111 1 O THR N 110 N VAL N 12
SHEET 3 BD 6 ALA N 88 ILE N 100A-1 N TYR N 90 O THR N 107
SHEET 4 BD 6 TRP N 34 GLN N 39 -1 N ILE N 37 O PHE N 91
SHEET 5 BD 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38
SHEET 6 BD 6 THR N 57 TYR N 59 -1 O THR N 58 N TYR N 50
SHEET 1 BE 4 LEU N 11 VAL N 12 0
SHEET 2 BE 4 THR N 107 VAL N 111 1 O THR N 110 N VAL N 12
SHEET 3 BE 4 ALA N 88 ILE N 100A-1 N TYR N 90 O THR N 107
SHEET 4 BE 4 PHE N 100J TRP N 103 -1 O PHE N 100K N ARG N 100
SHEET 1 BF 4 SER N 138 LEU N 142 0
SHEET 2 BF 4 THR N 153 TYR N 163 -1 O GLY N 157 N LEU N 142
SHEET 3 BF 4 TYR N 194 PRO N 203 -1 O LEU N 196 N VAL N 160
SHEET 4 BF 4 VAL N 181 THR N 183 -1 N HIS N 182 O VAL N 199
SHEET 1 BG 4 SER N 138 LEU N 142 0
SHEET 2 BG 4 THR N 153 TYR N 163 -1 O GLY N 157 N LEU N 142
SHEET 3 BG 4 TYR N 194 PRO N 203 -1 O LEU N 196 N VAL N 160
SHEET 4 BG 4 VAL N 187 LEU N 188 -1 N VAL N 187 O SER N 195
SHEET 1 BH 3 THR N 169 TRP N 172 0
SHEET 2 BH 3 ILE N 213 HIS N 218 -1 O ASN N 215 N SER N 171
SHEET 3 BH 3 THR N 223 LYS N 228 -1 O THR N 223 N HIS N 218
SHEET 1 BI 4 SER O 199 THR O 202 0
SHEET 2 BI 4 VAL O 120 THR O 123 -1 N LYS O 121 O ILE O 201
SHEET 3 BI 4 LYS O 432 MET O 434 -1 O LYS O 432 N LEU O 122
SHEET 4 BI 4 ILE O 423 ASN O 425 -1 N ILE O 424 O ALA O 433
SHEET 1 BJ 3 VAL O 242 VAL O 245 0
SHEET 2 BJ 3 PHE O 223 CYS O 228 -1 N LYS O 227 O SER O 243
SHEET 3 BJ 3 TYR O 486 LYS O 490 -1 O VAL O 489 N ALA O 224
SHEET 1 BK 7 LEU O 259 LEU O 261 0
SHEET 2 BK 7 ILE O 443 ARG O 456 -1 O THR O 450 N LEU O 260
SHEET 3 BK 7 ILE O 284 ARG O 298 -1 N ILE O 294 O SER O 447
SHEET 4 BK 7 HIS O 330 SER O 334 -1 O ASN O 332 N ASN O 295
SHEET 5 BK 7 THR O 413 LYS O 421 -1 O ILE O 414 N ILE O 333
SHEET 6 BK 7 GLU O 381 CYS O 385 -1 N TYR O 384 O ARG O 419
SHEET 7 BK 7 HIS O 374 CYS O 378 -1 N HIS O 374 O CYS O 385
SHEET 1 BL 7 VAL O 271 ARG O 273 0
SHEET 2 BL 7 ILE O 284 ARG O 298 -1 O ILE O 285 N ARG O 273
SHEET 3 BL 7 ILE O 443 ARG O 456 -1 O SER O 447 N ILE O 294
SHEET 4 BL 7 ILE O 465 PRO O 470 -1 O ARG O 469 N THR O 455
SHEET 5 BL 7 THR O 358 PHE O 361 1 N VAL O 360 O PHE O 468
SHEET 6 BL 7 SER O 393 TRP O 395 -1 O SER O 393 N PHE O 361
SHEET 7 BL 7 SER O 401 SER O 402 -1 O SER O 402 N THR O 394
SHEET 1 BM 2 PHE A 93 ASN A 94 0
SHEET 2 BM 2 LYS A 236 GLY A 237 -1 O GLY A 237 N PHE A 93
SHEET 1 BN 4 VAL A 200 THR A 202 0
SHEET 2 BN 4 VAL A 120 LEU A 122 -1 N LYS A 121 O ILE A 201
SHEET 3 BN 4 LYS A 432 MET A 434 -1 O LYS A 432 N LEU A 122
SHEET 4 BN 4 ILE A 423 ASN A 425 -1 N ILE A 424 O ALA A 433
SHEET 1 BO 3 VAL A 242 VAL A 245 0
SHEET 2 BO 3 PHE A 223 CYS A 228 -1 N LYS A 227 O SER A 243
SHEET 3 BO 3 VAL A 488 LYS A 490 -1 O VAL A 489 N ALA A 224
SHEET 1 BP 7 LEU A 259 LEU A 261 0
SHEET 2 BP 7 ILE A 443 ARG A 456 -1 O GLY A 451 N LEU A 260
SHEET 3 BP 7 ILE A 284 ARG A 298 -1 N VAL A 292 O ILE A 449
SHEET 4 BP 7 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295
SHEET 5 BP 7 THR A 413 LYS A 421 -1 O LEU A 416 N CYS A 331
SHEET 6 BP 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419
SHEET 7 BP 7 HIS A 374 CYS A 378 -1 N CYS A 378 O GLU A 381
SHEET 1 BQ 6 VAL A 271 ARG A 273 0
SHEET 2 BQ 6 ILE A 284 ARG A 298 -1 O GLN A 287 N VAL A 271
SHEET 3 BQ 6 ILE A 443 ARG A 456 -1 O ILE A 449 N VAL A 292
SHEET 4 BQ 6 ILE A 465 PRO A 470 -1 O ARG A 469 N THR A 455
SHEET 5 BQ 6 THR A 358 PHE A 361 1 N VAL A 360 O PHE A 468
SHEET 6 BQ 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361
SHEET 1 BR 4 ILE K 201 THR K 202 0
SHEET 2 BR 4 VAL K 120 LEU K 122 -1 N LYS K 121 O ILE K 201
SHEET 3 BR 4 LYS K 432 MET K 434 -1 O LYS K 432 N LEU K 122
SHEET 4 BR 4 ILE K 423 ASN K 425 -1 N ILE K 424 O ALA K 433
SHEET 1 BS 2 PHE K 223 ILE K 225 0
SHEET 2 BS 2 VAL K 488 LYS K 490 -1 O VAL K 489 N ALA K 224
SHEET 1 BT 7 LEU K 259 LEU K 261 0
SHEET 2 BT 7 ARG K 444 ARG K 456 -1 O THR K 450 N LEU K 260
SHEET 3 BT 7 ILE K 284 THR K 297 -1 N ILE K 294 O SER K 447
SHEET 4 BT 7 HIS K 330 SER K 334 -1 O ASN K 332 N ASN K 295
SHEET 5 BT 7 THR K 413 LYS K 421 -1 O ILE K 414 N ILE K 333
SHEET 6 BT 7 GLU K 381 CYS K 385 -1 N TYR K 384 O ARG K 419
SHEET 7 BT 7 HIS K 374 CYS K 378 -1 N HIS K 374 O CYS K 385
SHEET 1 BU 7 VAL K 271 ARG K 273 0
SHEET 2 BU 7 ILE K 284 THR K 297 -1 O GLN K 287 N VAL K 271
SHEET 3 BU 7 ARG K 444 ARG K 456 -1 O SER K 447 N ILE K 294
SHEET 4 BU 7 GLU K 466 PRO K 470 -1 O ARG K 469 N THR K 455
SHEET 5 BU 7 ILE K 359 PHE K 361 1 N VAL K 360 O PHE K 468
SHEET 6 BU 7 SER K 393 TRP K 395 -1 O SER K 393 N PHE K 361
SHEET 7 BU 7 SER K 401 SER K 402 -1 O SER K 402 N THR K 394
SSBOND 1 CYS E 119 CYS E 205 1555 1555 2.04
SSBOND 2 CYS E 218 CYS E 247 1555 1555 2.04
SSBOND 3 CYS E 228 CYS E 239 1555 1555 2.07
SSBOND 4 CYS E 296 CYS E 331 1555 1555 1.98
SSBOND 5 CYS E 378 CYS E 445 1555 1555 2.04
SSBOND 6 CYS E 385 CYS E 418 1555 1555 2.10
SSBOND 7 CYS F 16 CYS F 84 1555 1555 2.05
SSBOND 8 CYS F 130 CYS F 159 1555 1555 2.03
SSBOND 9 CYS P 23 CYS P 88 1555 1555 2.05
SSBOND 10 CYS P 135 CYS P 194 1555 1555 2.03
SSBOND 11 CYS Q 22 CYS Q 92 1555 1555 2.03
SSBOND 12 CYS Q 158 CYS Q 214 1555 1555 2.03
SSBOND 13 CYS B 16 CYS B 84 1555 1555 1.92
SSBOND 14 CYS B 130 CYS B 159 1555 1555 2.04
SSBOND 15 CYS C 23 CYS C 88 1555 1555 2.05
SSBOND 16 CYS C 135 CYS C 194 1555 1555 2.03
SSBOND 17 CYS D 22 CYS D 92 1555 1555 2.03
SSBOND 18 CYS D 158 CYS D 214 1555 1555 2.04
SSBOND 19 CYS H 16 CYS H 84 1555 1555 2.05
SSBOND 20 CYS H 130 CYS H 159 1555 1555 2.03
SSBOND 21 CYS I 23 CYS I 88 1555 1555 2.51
SSBOND 22 CYS I 135 CYS I 194 1555 1555 2.03
SSBOND 23 CYS J 22 CYS J 92 1555 1555 2.04
SSBOND 24 CYS J 158 CYS J 214 1555 1555 2.04
SSBOND 25 CYS L 16 CYS L 84 1555 1555 2.04
SSBOND 26 CYS L 130 CYS L 159 1555 1555 2.04
SSBOND 27 CYS M 23 CYS M 88 1555 1555 2.06
SSBOND 28 CYS M 135 CYS M 194 1555 1555 2.09
SSBOND 29 CYS N 22 CYS N 92 1555 1555 2.04
SSBOND 30 CYS N 158 CYS N 214 1555 1555 2.04
SSBOND 31 CYS O 119 CYS O 205 1555 1555 2.03
SSBOND 32 CYS O 218 CYS O 247 1555 1555 1.83
SSBOND 33 CYS O 228 CYS O 239 1555 1555 2.03
SSBOND 34 CYS O 296 CYS O 331 1555 1555 2.21
SSBOND 35 CYS O 331 CYS O 385 1555 1555 2.57
SSBOND 36 CYS O 378 CYS O 445 1555 1555 2.04
SSBOND 37 CYS O 385 CYS O 418 1555 1555 2.06
SSBOND 38 CYS A 119 CYS A 205 1555 1555 2.45
SSBOND 39 CYS A 228 CYS A 239 1555 1555 2.04
SSBOND 40 CYS A 296 CYS A 331 1555 1555 2.20
SSBOND 41 CYS A 331 CYS A 385 1555 1555 2.53
SSBOND 42 CYS A 378 CYS A 445 1555 1555 2.04
SSBOND 43 CYS A 385 CYS A 418 1555 1555 2.00
SSBOND 44 CYS K 119 CYS K 205 1555 1555 2.04
SSBOND 45 CYS K 218 CYS K 247 1555 1555 2.03
SSBOND 46 CYS K 228 CYS K 239 1555 1555 2.48
SSBOND 47 CYS K 296 CYS K 331 1555 1555 2.21
SSBOND 48 CYS K 331 CYS K 385 1555 1555 2.94
SSBOND 49 CYS K 378 CYS K 445 1555 1555 2.04
SSBOND 50 CYS K 385 CYS K 418 1555 1555 2.05
LINK ND2 ASN E 262 C1 NAG E 511 1555 1555 1.43
LINK ND2 ASN E 276 C1 NAG E 512 1555 1555 1.45
LINK ND2 ASN E 295 C1 NAG E 513 1555 1555 1.43
LINK ND2 ASN E 332 C1 NAG G 1 1555 1555 1.46
LINK ND2 ASN E 339 C1 NAG E 514 1555 1555 1.44
LINK ND2 ASN E 386 C1 NAG E 515 1555 1555 1.35
LINK ND2 ASN E 392 C1 NAG E 516 1555 1555 1.39
LINK ND2 ASN E 411 C1 NAG E 517 1555 1555 1.41
LINK ND2 ASN E 448 C1 NAG E 518 1555 1555 1.46
LINK ND2 ASN O 262 C1 NAG O 511 1555 1555 1.45
LINK ND2 ASN O 276 C1 NAG O 512 1555 1555 1.43
LINK ND2 ASN O 295 C1 NAG O 513 1555 1555 1.47
LINK ND2 ASN O 332 C1 NAG R 1 1555 1555 1.24
LINK ND2 ASN O 339 C1 NAG O 514 1555 1555 1.47
LINK ND2 ASN O 386 C1 NAG O 515 1555 1555 1.44
LINK ND2 ASN O 392 C1 NAG O 516 1555 1555 1.50
LINK ND2 ASN O 448 C1 NAG O 517 1555 1555 1.38
LINK ND2 ASN A 262 C1 NAG A 515 1555 1555 1.48
LINK ND2 ASN A 276 C1 NAG A 516 1555 1555 1.35
LINK ND2 ASN A 295 C1 NAG T 1 1555 1555 1.47
LINK ND2 ASN A 332 C1 NAG S 1 1555 1555 1.66
LINK ND2 ASN A 339 C1 NAG U 1 1555 1555 1.35
LINK ND2 ASN A 356 C1 NAG A 517 1555 1555 1.46
LINK ND2 ASN A 386 C1 NAG A 518 1555 1555 1.45
LINK ND2 ASN A 392 C1 NAG A 519 1555 1555 1.42
LINK ND2 ASN A 448 C1 NAG A 520 1555 1555 1.40
LINK ND2 ASN K 262 C1 NAG K 512 1555 1555 1.47
LINK ND2 ASN K 276 C1 NAG K 511 1555 1555 1.44
LINK ND2 ASN K 295 C1 NAG K 513 1555 1555 1.46
LINK ND2 ASN K 332 C1 NAG V 1 1555 1555 1.45
LINK ND2 ASN K 339 C1 NAG K 514 1555 1555 1.44
LINK ND2 ASN K 386 C1 NAG K 515 1555 1555 1.46
LINK OG1 THR K 404 O7 NAG K 514 1555 1555 2.03
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.34
LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.31
LINK O6 BMA G 3 C1 MAN G 7 1555 1555 1.44
LINK O2 MAN G 4 C1 MAN G 5 1555 1555 1.44
LINK O2 MAN G 5 C1 MAN G 6 1555 1555 1.44
LINK O6 MAN G 7 C1 MAN G 8 1555 1555 1.44
LINK O3 MAN G 7 C1 MAN G 10 1555 1555 1.57
LINK O2 MAN G 8 C1 MAN G 9 1555 1555 1.44
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44
LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.34
LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.32
LINK O6 BMA R 3 C1 MAN R 7 1555 1555 1.44
LINK O2 MAN R 4 C1 MAN R 5 1555 1555 1.59
LINK O2 MAN R 5 C1 MAN R 6 1555 1555 1.44
LINK O6 MAN R 7 C1 MAN R 8 1555 1555 1.44
LINK O3 MAN R 7 C1 MAN R 10 1555 1555 1.57
LINK O2 MAN R 8 C1 MAN R 9 1555 1555 1.44
LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44
LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.34
LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.50
LINK O6 BMA S 3 C1 MAN S 7 1555 1555 1.44
LINK O2 MAN S 4 C1 MAN S 5 1555 1555 1.44
LINK O2 MAN S 5 C1 MAN S 6 1555 1555 1.44
LINK O6 MAN S 7 C1 MAN S 8 1555 1555 1.44
LINK O3 MAN S 7 C1 MAN S 10 1555 1555 1.57
LINK O2 MAN S 8 C1 MAN S 9 1555 1555 1.44
LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.48
LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.47
LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44
LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.34
LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.32
LINK O6 BMA V 3 C1 MAN V 7 1555 1555 1.44
LINK O2 MAN V 4 C1 MAN V 5 1555 1555 1.59
LINK O2 MAN V 5 C1 MAN V 6 1555 1555 1.44
LINK O6 MAN V 7 C1 MAN V 8 1555 1555 1.44
LINK O3 MAN V 7 C1 MAN V 10 1555 1555 1.57
LINK O2 MAN V 8 C1 MAN V 9 1555 1555 1.44
CISPEP 1 GLY E 197 GLY E 198 0 -0.46
CISPEP 2 LEU F 114 THR F 115 0 13.01
CISPEP 3 TYR P 141 PRO P 142 0 8.62
CISPEP 4 GLY Q 151 GLY Q 152 0 5.17
CISPEP 5 PHE Q 164 PRO Q 165 0 -4.27
CISPEP 6 GLU Q 166 PRO Q 167 0 13.61
CISPEP 7 SER Q 179 GLY Q 180 0 -0.74
CISPEP 8 SER Q 221 ASN Q 222 0 -14.30
CISPEP 9 LEU C 106A SER C 107 0 -20.13
CISPEP 10 TYR C 141 PRO C 142 0 1.93
CISPEP 11 GLY D 27 SER D 28 0 -6.62
CISPEP 12 PHE D 100G GLY D 100H 0 1.05
CISPEP 13 PHE D 164 PRO D 165 0 -4.03
CISPEP 14 GLU D 166 PRO D 167 0 -1.60
CISPEP 15 ALA D 176 LEU D 177 0 4.80
CISPEP 16 SER D 179 GLY D 180 0 -0.31
CISPEP 17 SER D 205 SER D 206 0 -0.57
CISPEP 18 SER D 221 ASN D 222 0 -1.30
CISPEP 19 GLY H 141 LYS H 142 0 0.54
CISPEP 20 TYR I 5 VAL I 6 0 -1.02
CISPEP 21 TYR I 141 PRO I 142 0 5.12
CISPEP 22 GLY J 26 GLY J 27 0 5.87
CISPEP 23 GLY J 151 GLY J 152 0 -0.98
CISPEP 24 PHE J 164 PRO J 165 0 -2.35
CISPEP 25 GLU J 166 PRO J 167 0 2.31
CISPEP 26 SER J 179 GLY J 180 0 11.91
CISPEP 27 SER J 221 ASN J 222 0 -13.83
CISPEP 28 ASN L 103 SER L 104 0 -8.10
CISPEP 29 TYR M 141 PRO M 142 0 0.23
CISPEP 30 PHE N 100G GLY N 100H 0 -3.68
CISPEP 31 GLY N 151 GLY N 152 0 -1.82
CISPEP 32 PHE N 164 PRO N 165 0 -4.03
CISPEP 33 GLU N 166 PRO N 167 0 3.59
CISPEP 34 SER N 179 GLY N 180 0 1.85
CISPEP 35 SER N 221 ASN N 222 0 3.76
CISPEP 36 ILE O 323 GLY O 324 0 3.46
CISPEP 37 CYS A 205 PRO A 206 0 -14.96
CISPEP 38 HIS A 249 GLY A 250 0 -7.07
CISPEP 39 GLY K 197 GLY K 198 0 -4.97
CISPEP 40 ILE K 323 GLY K 324 0 -10.61
CISPEP 41 LYS K 460 ASN K 461 0 -0.28
CRYST1 164.406 165.438 229.712 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006045 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004353 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
