HEADER IMMUNE SYSTEM 09-MAR-17 5V4E
TITLE ENGINEERED HUMAN IGG FC DOMAIN GLYCO801 (FC801)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IG GAMMA-1 CHAIN C REGION;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: RESIDUES 104-329;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IGHG1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293
KEYWDS ANTIBODY ENGINEERING, FC FRAGMENT, IGG, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR W.YAN,N.MARSHALL,Y.J.ZHANG
REVDAT 5 29-JUL-20 5V4E 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 27-SEP-17 5V4E 1 REMARK
REVDAT 3 02-AUG-17 5V4E 1 JRNL
REVDAT 2 28-JUN-17 5V4E 1 JRNL
REVDAT 1 21-JUN-17 5V4E 0
JRNL AUTH C.H.LEE,G.ROMAIN,W.YAN,M.WATANABE,W.CHARAB,B.TODOROVA,J.LEE,
JRNL AUTH 2 K.TRIPLETT,M.DONKOR,O.I.LUNGU,A.LUX,N.MARSHALL,
JRNL AUTH 3 M.A.LINDORFER,O.R.GOFF,B.BALBINO,T.H.KANG,H.TANNO,
JRNL AUTH 4 G.DELIDAKIS,C.ALFORD,R.P.TAYLOR,F.NIMMERJAHN,N.VARADARAJAN,
JRNL AUTH 5 P.BRUHNS,Y.J.ZHANG,G.GEORGIOU
JRNL TITL IGG FC DOMAINS THAT BIND C1Q BUT NOT EFFECTOR FC GAMMA
JRNL TITL 2 RECEPTORS DELINEATE THE IMPORTANCE OF COMPLEMENT-MEDIATED
JRNL TITL 3 EFFECTOR FUNCTIONS.
JRNL REF NAT. IMMUNOL. V. 18 889 2017
JRNL REFN ESSN 1529-2916
JRNL PMID 28604720
JRNL DOI 10.1038/NI.3770
REMARK 2
REMARK 2 RESOLUTION. 3.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
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) : 3.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 72629
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250
REMARK 3 FREE R VALUE TEST SET COUNT : 3813
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 39.8889 - 9.6049 0.99 2524 162 0.2564 0.3250
REMARK 3 2 9.6049 - 7.6413 1.00 2577 122 0.2078 0.2032
REMARK 3 3 7.6413 - 6.6805 1.00 2511 161 0.2200 0.2847
REMARK 3 4 6.6805 - 6.0720 1.00 2585 122 0.2512 0.3067
REMARK 3 5 6.0720 - 5.6381 1.00 2582 116 0.2276 0.2322
REMARK 3 6 5.6381 - 5.3065 1.00 2553 148 0.2241 0.2843
REMARK 3 7 5.3065 - 5.0412 1.00 2552 151 0.2047 0.2605
REMARK 3 8 5.0412 - 4.8222 1.00 2553 146 0.1995 0.2313
REMARK 3 9 4.8222 - 4.6368 1.00 2583 120 0.1830 0.2241
REMARK 3 10 4.6368 - 4.4770 1.00 2554 150 0.1979 0.2545
REMARK 3 11 4.4770 - 4.3372 1.00 2510 156 0.2154 0.2330
REMARK 3 12 4.3372 - 4.2134 1.00 2565 139 0.2168 0.1978
REMARK 3 13 4.2134 - 4.1026 1.00 2535 151 0.2306 0.2864
REMARK 3 14 4.1026 - 4.0026 1.00 2537 176 0.2375 0.2841
REMARK 3 15 4.0026 - 3.9117 1.00 2544 166 0.2382 0.2763
REMARK 3 16 3.9117 - 3.8285 1.00 2532 143 0.2558 0.2675
REMARK 3 17 3.8285 - 3.7520 1.00 2617 127 0.2778 0.3524
REMARK 3 18 3.7520 - 3.6812 1.00 2563 145 0.2793 0.3380
REMARK 3 19 3.6812 - 3.6155 1.00 2523 169 0.2767 0.3372
REMARK 3 20 3.6155 - 3.5543 1.00 2613 116 0.2754 0.3234
REMARK 3 21 3.5543 - 3.4970 1.00 2523 140 0.2747 0.3541
REMARK 3 22 3.4970 - 3.4432 1.00 2500 148 0.2741 0.3464
REMARK 3 23 3.4432 - 3.3926 1.00 2632 126 0.2728 0.3266
REMARK 3 24 3.3926 - 3.3448 1.00 2545 130 0.2814 0.3223
REMARK 3 25 3.3448 - 3.2996 1.00 2643 121 0.2735 0.3066
REMARK 3 26 3.2996 - 3.2568 1.00 2547 127 0.2988 0.3891
REMARK 3 27 3.2568 - 3.2161 0.92 2313 135 0.3213 0.4267
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) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.560
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 : 0.003 12285
REMARK 3 ANGLE : 0.614 16977
REMARK 3 CHIRALITY : 0.043 2041
REMARK 3 PLANARITY : 0.004 2160
REMARK 3 DIHEDRAL : 13.055 7333
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 5V4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226853.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97648
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36958
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.220
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6920
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.28
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.550
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 (%): 61.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 MM POTASSIUM PHOSPHATE 16% W/V PEG
REMARK 280 8000 20% V/V GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 70.51000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, L
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, M, N
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 ASP A 221
REMARK 465 LYS A 222
REMARK 465 THR A 223
REMARK 465 HIS A 224
REMARK 465 THR A 225
REMARK 465 CYS A 226
REMARK 465 PRO A 445
REMARK 465 GLY A 446
REMARK 465 ASP B 221
REMARK 465 LYS B 222
REMARK 465 THR B 223
REMARK 465 HIS B 224
REMARK 465 THR B 225
REMARK 465 CYS B 226
REMARK 465 PRO B 227
REMARK 465 PRO B 228
REMARK 465 CYS B 229
REMARK 465 PRO B 230
REMARK 465 ALA B 231
REMARK 465 PRO B 232
REMARK 465 GLU B 233
REMARK 465 LEU B 234
REMARK 465 LEU B 235
REMARK 465 GLY B 236
REMARK 465 GLY B 237
REMARK 465 PRO B 238
REMARK 465 SER B 239
REMARK 465 VAL B 240
REMARK 465 PHE B 241
REMARK 465 VAL B 266
REMARK 465 SER B 267
REMARK 465 HIS B 268
REMARK 465 GLU B 269
REMARK 465 GLU B 294
REMARK 465 GLN B 295
REMARK 465 TYR B 296
REMARK 465 ASN B 297
REMARK 465 SER B 298
REMARK 465 SER B 324
REMARK 465 ASN B 325
REMARK 465 LYS B 326
REMARK 465 ALA B 327
REMARK 465 LEU B 328
REMARK 465 PRO B 329
REMARK 465 ALA B 330
REMARK 465 PRO B 331
REMARK 465 PRO B 445
REMARK 465 GLY B 446
REMARK 465 ASP C 221
REMARK 465 LYS C 222
REMARK 465 THR C 223
REMARK 465 HIS C 224
REMARK 465 THR C 225
REMARK 465 CYS C 226
REMARK 465 PRO C 227
REMARK 465 PRO C 228
REMARK 465 CYS C 229
REMARK 465 PRO C 230
REMARK 465 ALA C 231
REMARK 465 PRO C 232
REMARK 465 GLU C 233
REMARK 465 LEU C 234
REMARK 465 LEU C 235
REMARK 465 GLY C 236
REMARK 465 GLY C 237
REMARK 465 PRO C 238
REMARK 465 SER C 239
REMARK 465 VAL C 240
REMARK 465 PHE C 241
REMARK 465 VAL C 262
REMARK 465 VAL C 263
REMARK 465 VAL C 264
REMARK 465 ASP C 265
REMARK 465 VAL C 266
REMARK 465 SER C 267
REMARK 465 HIS C 268
REMARK 465 GLU C 269
REMARK 465 ASP C 270
REMARK 465 PRO C 271
REMARK 465 GLU C 272
REMARK 465 VAL C 273
REMARK 465 LYS C 274
REMARK 465 LYS C 290
REMARK 465 PRO C 291
REMARK 465 ARG C 292
REMARK 465 GLU C 293
REMARK 465 GLU C 294
REMARK 465 GLN C 295
REMARK 465 TYR C 296
REMARK 465 ASN C 297
REMARK 465 SER C 298
REMARK 465 THR C 299
REMARK 465 TYR C 300
REMARK 465 ARG C 301
REMARK 465 VAL C 302
REMARK 465 VAL C 303
REMARK 465 LYS C 322
REMARK 465 VAL C 323
REMARK 465 SER C 324
REMARK 465 ASN C 325
REMARK 465 LYS C 326
REMARK 465 ALA C 327
REMARK 465 LEU C 328
REMARK 465 PRO C 329
REMARK 465 ALA C 330
REMARK 465 PRO C 331
REMARK 465 ILE C 332
REMARK 465 GLU C 333
REMARK 465 LYS C 334
REMARK 465 THR C 335
REMARK 465 PRO C 445
REMARK 465 GLY C 446
REMARK 465 ASP D 221
REMARK 465 LYS D 222
REMARK 465 THR D 223
REMARK 465 HIS D 224
REMARK 465 THR D 225
REMARK 465 CYS D 226
REMARK 465 PRO D 227
REMARK 465 PRO D 228
REMARK 465 CYS D 229
REMARK 465 PRO D 230
REMARK 465 ALA D 231
REMARK 465 PRO D 232
REMARK 465 GLU D 233
REMARK 465 LEU D 234
REMARK 465 LEU D 235
REMARK 465 GLY D 236
REMARK 465 GLY D 237
REMARK 465 HIS D 268
REMARK 465 GLU D 269
REMARK 465 GLU D 294
REMARK 465 GLN D 295
REMARK 465 TYR D 296
REMARK 465 ALA D 330
REMARK 465 SER D 444
REMARK 465 PRO D 445
REMARK 465 GLY D 446
REMARK 465 ASP E 221
REMARK 465 LYS E 222
REMARK 465 THR E 223
REMARK 465 HIS E 224
REMARK 465 THR E 225
REMARK 465 CYS E 226
REMARK 465 PRO E 227
REMARK 465 PRO E 228
REMARK 465 CYS E 229
REMARK 465 PRO E 230
REMARK 465 ALA E 231
REMARK 465 PRO E 232
REMARK 465 GLU E 233
REMARK 465 LEU E 234
REMARK 465 LEU E 235
REMARK 465 GLY E 236
REMARK 465 PRO E 445
REMARK 465 GLY E 446
REMARK 465 ASP F 221
REMARK 465 LYS F 222
REMARK 465 THR F 223
REMARK 465 HIS F 224
REMARK 465 THR F 225
REMARK 465 CYS F 226
REMARK 465 PRO F 227
REMARK 465 PRO F 228
REMARK 465 CYS F 229
REMARK 465 PRO F 230
REMARK 465 ALA F 231
REMARK 465 PRO F 232
REMARK 465 GLU F 233
REMARK 465 LEU F 234
REMARK 465 LEU F 235
REMARK 465 GLY F 236
REMARK 465 GLY F 237
REMARK 465 PRO F 238
REMARK 465 ASP F 265
REMARK 465 VAL F 266
REMARK 465 SER F 267
REMARK 465 HIS F 268
REMARK 465 GLU F 269
REMARK 465 ASP F 270
REMARK 465 PRO F 271
REMARK 465 GLU F 272
REMARK 465 VAL F 273
REMARK 465 LYS F 274
REMARK 465 PHE F 275
REMARK 465 ASN F 276
REMARK 465 TRP F 277
REMARK 465 GLU F 294
REMARK 465 GLN F 295
REMARK 465 TYR F 296
REMARK 465 ASN F 297
REMARK 465 SER F 298
REMARK 465 THR F 299
REMARK 465 TYR F 300
REMARK 465 SER F 324
REMARK 465 ASN F 325
REMARK 465 LYS F 326
REMARK 465 ALA F 327
REMARK 465 LEU F 328
REMARK 465 PRO F 329
REMARK 465 ALA F 330
REMARK 465 PRO F 331
REMARK 465 SER F 444
REMARK 465 PRO F 445
REMARK 465 GLY F 446
REMARK 465 ASP G 221
REMARK 465 LYS G 222
REMARK 465 THR G 223
REMARK 465 HIS G 224
REMARK 465 THR G 225
REMARK 465 PRO G 445
REMARK 465 GLY G 446
REMARK 465 ASP H 221
REMARK 465 LYS H 222
REMARK 465 THR H 223
REMARK 465 HIS H 224
REMARK 465 THR H 225
REMARK 465 ILE H 253
REMARK 465 SER H 254
REMARK 465 SER H 444
REMARK 465 PRO H 445
REMARK 465 GLY H 446
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 LEU A 234 CG CD1 CD2
REMARK 470 LEU A 235 CG CD1 CD2
REMARK 470 SER A 239 OG
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 ILE A 253 CG1 CG2 CD1
REMARK 470 SER A 254 OG
REMARK 470 VAL A 263 CG1 CG2
REMARK 470 VAL A 264 CG1 CG2
REMARK 470 SER A 267 OG
REMARK 470 HIS A 268 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 269 CG CD OE1 OE2
REMARK 470 ASP A 270 CG OD1 OD2
REMARK 470 GLU A 272 CG CD OE1 OE2
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 TYR A 278 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 283 CG CD OE1 OE2
REMARK 470 VAL A 284 CG1 CG2
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 LYS A 290 CG CD CE NZ
REMARK 470 LEU A 309 CG CD1 CD2
REMARK 470 GLN A 311 CG CD OE1 NE2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 LYS A 322 CG CD CE NZ
REMARK 470 SER A 324 OG
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 LEU A 328 CG CD1 CD2
REMARK 470 ILE A 332 CG1 CG2 CD1
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 LYS A 334 CE NZ
REMARK 470 ILE A 336 CG1 CG2 CD1
REMARK 470 LYS A 338 CG CD CE NZ
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 ARG A 355 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 358 CG CD1 CD2
REMARK 470 LYS A 360 CG CD CE NZ
REMARK 470 LYS A 370 NZ
REMARK 470 ASN A 384 CG OD1 ND2
REMARK 470 ARG A 386 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 389 CG OD1 ND2
REMARK 470 LYS A 414 CG CD CE NZ
REMARK 470 GLN A 418 CG CD OE1 NE2
REMARK 470 GLN A 419 CG CD OE1 NE2
REMARK 470 VAL A 422 CG1 CG2
REMARK 470 LEU B 242 CG CD1 CD2
REMARK 470 PHE B 243 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 246 CG CD CE NZ
REMARK 470 THR B 250 OG1 CG2
REMARK 470 MET B 252 CG SD CE
REMARK 470 ILE B 253 CG1 CG2 CD1
REMARK 470 SER B 254 OG
REMARK 470 ARG B 255 CG CD NE CZ NH1 NH2
REMARK 470 THR B 256 OG1 CG2
REMARK 470 VAL B 259 CG1 CG2
REMARK 470 VAL B 262 CG1 CG2
REMARK 470 VAL B 263 CG1 CG2
REMARK 470 VAL B 264 CG1 CG2
REMARK 470 ASP B 265 CG OD1 OD2
REMARK 470 ASP B 270 CG OD1 OD2
REMARK 470 GLU B 272 CG CD OE1 OE2
REMARK 470 LYS B 274 CG CD CE NZ
REMARK 470 PHE B 275 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B 276 CG OD1 ND2
REMARK 470 ASP B 280 CG OD1 OD2
REMARK 470 VAL B 282 CG1 CG2
REMARK 470 GLU B 283 CG CD OE1 OE2
REMARK 470 VAL B 284 CG1 CG2
REMARK 470 HIS B 285 CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 286 CG OD1 ND2
REMARK 470 LYS B 290 CG CD CE NZ
REMARK 470 ARG B 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 293 CG CD OE1 OE2
REMARK 470 THR B 299 OG1 CG2
REMARK 470 TYR B 300 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 301 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 302 CG1 CG2
REMARK 470 VAL B 303 CG1 CG2
REMARK 470 LEU B 306 CG CD1 CD2
REMARK 470 THR B 307 OG1 CG2
REMARK 470 LEU B 309 CG CD1 CD2
REMARK 470 GLN B 311 CG CD OE1 NE2
REMARK 470 LEU B 314 CG CD1 CD2
REMARK 470 ASN B 315 CG OD1 ND2
REMARK 470 LYS B 322 CG CD CE NZ
REMARK 470 ILE B 332 CG1 CG2 CD1
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 ILE B 336 CG1 CG2 CD1
REMARK 470 SER B 337 OG
REMARK 470 LYS B 338 CG CD CE NZ
REMARK 470 LYS B 340 CG CD CE NZ
REMARK 470 GLN B 342 CG CD OE1 NE2
REMARK 470 ARG B 344 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 355 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 356 CG OD1 OD2
REMARK 470 GLU B 357 CG CD OE1 OE2
REMARK 470 LEU B 358 CG CD1 CD2
REMARK 470 LEU B 365 CG CD1 CD2
REMARK 470 SER B 383 OG
REMARK 470 ARG B 386 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 390 CG OD1 ND2
REMARK 470 LYS B 392 CG CD CE NZ
REMARK 470 GLN B 418 CG CD OE1 NE2
REMARK 470 GLN B 419 CG CD OE1 NE2
REMARK 470 VAL B 422 CG1 CG2
REMARK 470 SER B 424 OG
REMARK 470 SER B 426 OG
REMARK 470 GLU B 430 OE1 OE2
REMARK 470 LYS B 439 CG CD CE NZ
REMARK 470 SER B 442 OG
REMARK 470 LEU B 443 CG CD1 CD2
REMARK 470 LEU C 242 CG CD1 CD2
REMARK 470 LYS C 246 CG CD CE NZ
REMARK 470 ILE C 253 CG1 CG2 CD1
REMARK 470 THR C 256 OG1 CG2
REMARK 470 VAL C 259 CG1 CG2
REMARK 470 THR C 260 OG1 CG2
REMARK 470 PHE C 275 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP C 277 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 277 CZ3 CH2
REMARK 470 TYR C 278 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL C 279 CG1 CG2
REMARK 470 VAL C 282 CG1 CG2
REMARK 470 GLU C 283 CG CD OE1 OE2
REMARK 470 VAL C 284 CG1 CG2
REMARK 470 ASN C 286 CG OD1 ND2
REMARK 470 LYS C 288 CD CE NZ
REMARK 470 VAL C 305 CG1 CG2
REMARK 470 LEU C 306 CG CD1 CD2
REMARK 470 VAL C 308 CG1 CG2
REMARK 470 LEU C 309 CG CD1 CD2
REMARK 470 GLN C 311 CG CD OE1 NE2
REMARK 470 ASP C 312 CG OD1 OD2
REMARK 470 LYS C 317 CG CD CE NZ
REMARK 470 GLU C 318 CG CD OE1 OE2
REMARK 470 TYR C 319 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE C 336 CG1 CG2 CD1
REMARK 470 LYS C 338 CG CD CE NZ
REMARK 470 LYS C 340 CG CD CE NZ
REMARK 470 GLN C 342 CG CD OE1 NE2
REMARK 470 ARG C 344 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 347 CG CD OE1 NE2
REMARK 470 LYS C 360 CG CD CE NZ
REMARK 470 SER C 444 OG
REMARK 470 SER D 239 OG
REMARK 470 VAL D 240 CG1 CG2
REMARK 470 PHE D 241 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 246 CG CD CE NZ
REMARK 470 LYS D 248 CG CD CE NZ
REMARK 470 LEU D 251 CG CD1 CD2
REMARK 470 MET D 252 CG SD CE
REMARK 470 ILE D 253 CG1 CG2 CD1
REMARK 470 SER D 254 OG
REMARK 470 ARG D 255 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 264 CG1 CG2
REMARK 470 ASP D 265 CG OD1 OD2
REMARK 470 VAL D 266 CG1 CG2
REMARK 470 ASP D 270 CG OD1 OD2
REMARK 470 GLU D 272 CG CD OE1 OE2
REMARK 470 LYS D 274 CG CD CE NZ
REMARK 470 VAL D 282 CG1 CG2
REMARK 470 GLU D 283 CG CD OE1 OE2
REMARK 470 LYS D 288 CG CD CE NZ
REMARK 470 LYS D 290 CG CD CE NZ
REMARK 470 ARG D 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 293 CG CD OE1 OE2
REMARK 470 ASN D 297 CG OD1 ND2
REMARK 470 THR D 299 OG1 CG2
REMARK 470 TYR D 300 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 301 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 303 CG1 CG2
REMARK 470 LEU D 309 CG CD1 CD2
REMARK 470 GLN D 311 CG CD OE1 NE2
REMARK 470 LEU D 314 CG CD1 CD2
REMARK 470 LYS D 317 CG CD CE NZ
REMARK 470 GLU D 318 CG CD OE1 OE2
REMARK 470 LYS D 322 CG CD CE NZ
REMARK 470 VAL D 323 CG1 CG2
REMARK 470 ASN D 325 CG OD1 ND2
REMARK 470 LYS D 326 CG CD CE NZ
REMARK 470 LEU D 328 CG CD1 CD2
REMARK 470 ILE D 332 CG1 CG2 CD1
REMARK 470 LYS D 334 CG CD CE NZ
REMARK 470 LYS D 338 CG CD CE NZ
REMARK 470 LYS D 340 CG CD CE NZ
REMARK 470 ARG D 344 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 355 CG CD NE CZ NH1 NH2
REMARK 470 THR D 359 OG1 CG2
REMARK 470 LYS D 360 CG CD CE NZ
REMARK 470 SER D 383 OG
REMARK 470 ARG D 386 CG CD NE CZ NH1 NH2
REMARK 470 SER D 400 OG
REMARK 470 SER D 415 OG
REMARK 470 LYS E 246 CG CD CE NZ
REMARK 470 LYS E 248 CG CD CE NZ
REMARK 470 MET E 252 CG SD CE
REMARK 470 ILE E 253 CG1 CG2 CD1
REMARK 470 SER E 254 OG
REMARK 470 ARG E 255 CG CD NE CZ NH1 NH2
REMARK 470 SER E 267 OG
REMARK 470 GLU E 269 CG CD OE1 OE2
REMARK 470 ASP E 270 CG OD1 OD2
REMARK 470 GLU E 272 CG CD OE1 OE2
REMARK 470 VAL E 273 CG1 CG2
REMARK 470 LYS E 274 CG CD CE NZ
REMARK 470 ASN E 276 CG OD1 ND2
REMARK 470 VAL E 279 CG1 CG2
REMARK 470 ASP E 280 CG OD1 OD2
REMARK 470 VAL E 282 CG1 CG2
REMARK 470 VAL E 284 CG1 CG2
REMARK 470 ASN E 286 CG OD1 ND2
REMARK 470 LYS E 288 CG CD CE NZ
REMARK 470 LYS E 290 CG CD CE NZ
REMARK 470 GLU E 293 CG CD OE1 OE2
REMARK 470 SER E 298 OG
REMARK 470 VAL E 302 CG1 CG2
REMARK 470 VAL E 303 CG1 CG2
REMARK 470 SER E 304 OG
REMARK 470 LEU E 309 CG CD1 CD2
REMARK 470 LEU E 314 CG CD1 CD2
REMARK 470 LYS E 317 CG CD CE NZ
REMARK 470 GLU E 320 CG CD OE1 OE2
REMARK 470 LYS E 322 CG CD CE NZ
REMARK 470 VAL E 323 CG1 CG2
REMARK 470 SER E 324 OG
REMARK 470 ASN E 325 CG OD1 ND2
REMARK 470 LYS E 326 CG CD CE NZ
REMARK 470 LEU E 328 CG CD1 CD2
REMARK 470 ILE E 332 CG1 CG2 CD1
REMARK 470 GLU E 333 CG CD OE1 OE2
REMARK 470 LYS E 334 CG CD CE NZ
REMARK 470 ILE E 336 CG1 CG2 CD1
REMARK 470 LYS E 340 CG CD CE NZ
REMARK 470 ARG E 355 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 358 CG CD1 CD2
REMARK 470 LYS E 360 CG CD CE NZ
REMARK 470 ASN E 361 CG OD1 ND2
REMARK 470 VAL E 363 CG1 CG2
REMARK 470 GLU E 382 CD OE1 OE2
REMARK 470 ARG E 386 CG CD NE CZ NH1 NH2
REMARK 470 ASN E 389 CG OD1 ND2
REMARK 470 LYS E 414 CG CD CE NZ
REMARK 470 GLN E 418 CG CD OE1 NE2
REMARK 470 VAL F 240 CG1 CG2
REMARK 470 PHE F 241 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU F 242 CG CD1 CD2
REMARK 470 LYS F 246 CG CD CE NZ
REMARK 470 LEU F 251 CG CD1 CD2
REMARK 470 MET F 252 CG SD CE
REMARK 470 ILE F 253 CG1 CG2 CD1
REMARK 470 VAL F 259 CG1 CG2
REMARK 470 VAL F 262 CG1 CG2
REMARK 470 VAL F 263 CG1 CG2
REMARK 470 VAL F 264 CG1 CG2
REMARK 470 TYR F 278 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP F 280 CG OD1 OD2
REMARK 470 VAL F 282 CG1 CG2
REMARK 470 GLU F 283 CG CD OE1 OE2
REMARK 470 VAL F 284 CG1 CG2
REMARK 470 HIS F 285 CG ND1 CD2 CE1 NE2
REMARK 470 ASN F 286 CG OD1 ND2
REMARK 470 LYS F 288 CG CD CE NZ
REMARK 470 THR F 289 OG1 CG2
REMARK 470 LYS F 290 CG CD CE NZ
REMARK 470 ARG F 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 293 CG CD OE1 OE2
REMARK 470 ARG F 301 CG CD NE CZ NH1 NH2
REMARK 470 VAL F 302 CG1 CG2
REMARK 470 VAL F 303 CG1 CG2
REMARK 470 SER F 304 OG
REMARK 470 LEU F 306 CG CD1 CD2
REMARK 470 LEU F 309 CG CD1 CD2
REMARK 470 GLN F 311 CG CD OE1 NE2
REMARK 470 LEU F 314 CG CD1 CD2
REMARK 470 LYS F 317 CG CD CE NZ
REMARK 470 GLU F 318 CG CD OE1 OE2
REMARK 470 LYS F 322 CG CD CE NZ
REMARK 470 VAL F 323 CG1 CG2
REMARK 470 ILE F 332 CG1 CG2 CD1
REMARK 470 LYS F 334 CG CD CE NZ
REMARK 470 ILE F 336 CG1 CG2 CD1
REMARK 470 LYS F 340 CG CD CE NZ
REMARK 470 GLN F 342 CG CD OE1 NE2
REMARK 470 ARG F 344 NE CZ NH1 NH2
REMARK 470 ARG F 355 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 360 CG CD CE NZ
REMARK 470 ASN F 384 CG OD1 ND2
REMARK 470 ARG F 386 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 418 CG CD OE1 NE2
REMARK 470 VAL F 422 CG1 CG2
REMARK 470 ASN F 434 CG OD1 ND2
REMARK 470 LEU G 234 CG CD1 CD2
REMARK 470 LEU G 235 CG CD1 CD2
REMARK 470 LYS G 246 CG CD CE NZ
REMARK 470 ILE G 253 CG1 CG2 CD1
REMARK 470 ARG G 255 CG CD NE CZ NH1 NH2
REMARK 470 SER G 267 OG
REMARK 470 GLU G 269 CG CD OE1 OE2
REMARK 470 GLU G 272 CG CD OE1 OE2
REMARK 470 LYS G 274 CG CD CE NZ
REMARK 470 VAL G 279 CG1 CG2
REMARK 470 ASP G 280 CG OD1 OD2
REMARK 470 VAL G 282 CG1 CG2
REMARK 470 HIS G 285 CG ND1 CD2 CE1 NE2
REMARK 470 LYS G 288 CG CD CE NZ
REMARK 470 LYS G 290 CG CD CE NZ
REMARK 470 SER G 298 OG
REMARK 470 LYS G 317 CG CD CE NZ
REMARK 470 LYS G 326 CG CD CE NZ
REMARK 470 ILE G 332 CG1 CG2 CD1
REMARK 470 LYS G 338 CG CD CE NZ
REMARK 470 LYS G 340 CG CD CE NZ
REMARK 470 GLN G 342 CG CD OE1 NE2
REMARK 470 ARG G 344 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 355 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 357 CG CD OE1 OE2
REMARK 470 LEU G 358 CG CD1 CD2
REMARK 470 THR G 359 OG1 CG2
REMARK 470 LYS G 360 CG CD CE NZ
REMARK 470 ARG G 386 CG CD NE CZ NH1 NH2
REMARK 470 ASN G 390 CG OD1 ND2
REMARK 470 LYS G 414 CG CD CE NZ
REMARK 470 GLN G 418 CG CD OE1 NE2
REMARK 470 LYS G 439 CG CD CE NZ
REMARK 470 LEU G 443 CG CD1 CD2
REMARK 470 SER G 444 OG
REMARK 470 GLU H 233 CG CD OE1 OE2
REMARK 470 LEU H 234 CG CD1 CD2
REMARK 470 LYS H 246 CG CD CE NZ
REMARK 470 MET H 252 CG SD CE
REMARK 470 ARG H 255 CG CD NE CZ NH1 NH2
REMARK 470 SER H 267 OG
REMARK 470 HIS H 268 CG ND1 CD2 CE1 NE2
REMARK 470 GLU H 269 CG CD OE1 OE2
REMARK 470 ASP H 270 CG OD1 OD2
REMARK 470 LYS H 274 CG CD CE NZ
REMARK 470 ASP H 280 CG OD1 OD2
REMARK 470 VAL H 282 CG1 CG2
REMARK 470 LYS H 288 CG CD CE NZ
REMARK 470 THR H 289 OG1 CG2
REMARK 470 LYS H 290 CG CD CE NZ
REMARK 470 ARG H 292 CG CD NE CZ NH1 NH2
REMARK 470 SER H 298 OG
REMARK 470 THR H 299 OG1 CG2
REMARK 470 VAL H 302 CG1 CG2
REMARK 470 LEU H 309 CG CD1 CD2
REMARK 470 GLN H 311 CG CD OE1 NE2
REMARK 470 LEU H 314 CG CD1 CD2
REMARK 470 LYS H 317 CG CD CE NZ
REMARK 470 LYS H 322 CG CD CE NZ
REMARK 470 VAL H 323 CG1 CG2
REMARK 470 SER H 324 OG
REMARK 470 ASN H 325 CG OD1 ND2
REMARK 470 LYS H 326 CG CD CE NZ
REMARK 470 LEU H 328 CG CD1 CD2
REMARK 470 ILE H 332 CG1 CG2 CD1
REMARK 470 GLU H 333 CG CD OE1 OE2
REMARK 470 LYS H 334 CG CD CE NZ
REMARK 470 LYS H 338 CD CE NZ
REMARK 470 LYS H 340 CG CD CE NZ
REMARK 470 GLN H 342 CG CD OE1 NE2
REMARK 470 ARG H 344 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 355 CG CD NE CZ NH1 NH2
REMARK 470 THR H 359 OG1 CG2
REMARK 470 LYS H 360 CD CE NZ
REMARK 470 ASN H 361 CG OD1 ND2
REMARK 470 ASN H 384 CG OD1 ND2
REMARK 470 ARG H 386 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 414 CG CD CE NZ
REMARK 470 ARG H 416 CG CD NE CZ NH1 NH2
REMARK 470 GLN H 418 CG CD OE1 NE2
REMARK 470 VAL H 422 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 OD1 ASP G 249 O HOH G 601 1.97
REMARK 500 N LEU F 358 O HOH F 501 2.01
REMARK 500 O CYS E 367 O HOH E 601 2.08
REMARK 500 O SER A 354 O HOH A 601 2.09
REMARK 500 O VAL H 302 O HOH H 601 2.17
REMARK 500 N SER E 408 O HOH E 601 2.18
REMARK 500 O VAL H 302 O HOH H 602 2.19
REMARK 500 O LEU F 443 O HOH F 502 2.19
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 LYS C 288 -143.74 -99.43
REMARK 500 ASP D 265 74.05 57.81
REMARK 500 ASN F 286 42.70 -88.21
REMARK 500 ASN F 434 32.45 -141.86
REMARK 500 ASN G 434 19.95 59.76
REMARK 500 ASN H 297 30.05 -90.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 BMA J 1
REMARK 610 BMA K 1
REMARK 610 MAN B 501
REMARK 610 MAN B 502
REMARK 610 NAG B 503
DBREF 5V4E A 221 446 UNP P01857 IGHG1_HUMAN 104 329
DBREF 5V4E B 221 446 UNP P01857 IGHG1_HUMAN 104 329
DBREF 5V4E C 221 446 UNP P01857 IGHG1_HUMAN 104 329
DBREF 5V4E D 221 446 UNP P01857 IGHG1_HUMAN 104 329
DBREF 5V4E E 221 446 UNP P01857 IGHG1_HUMAN 104 329
DBREF 5V4E F 221 446 UNP P01857 IGHG1_HUMAN 104 329
DBREF 5V4E G 221 446 UNP P01857 IGHG1_HUMAN 104 329
DBREF 5V4E H 221 446 UNP P01857 IGHG1_HUMAN 104 329
SEQADV 5V4E GLU A 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG A 386 UNP P01857 GLN 269 CONFLICT
SEQADV 5V4E GLU B 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG B 386 UNP P01857 GLN 269 CONFLICT
SEQADV 5V4E GLU C 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG C 386 UNP P01857 GLN 269 CONFLICT
SEQADV 5V4E GLU D 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG D 386 UNP P01857 GLN 269 CONFLICT
SEQADV 5V4E GLU E 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG E 386 UNP P01857 GLN 269 CONFLICT
SEQADV 5V4E GLU F 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG F 386 UNP P01857 GLN 269 CONFLICT
SEQADV 5V4E GLU G 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG G 386 UNP P01857 GLN 269 CONFLICT
SEQADV 5V4E GLU H 320 UNP P01857 LYS 203 CONFLICT
SEQADV 5V4E ARG H 386 UNP P01857 GLN 269 CONFLICT
SEQRES 1 A 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 A 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 A 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 A 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 A 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 A 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 A 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 A 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 A 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 A 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 A 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 A 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 A 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 A 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 A 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 A 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 A 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 A 226 SER LEU SER PRO GLY
SEQRES 1 B 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 B 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 B 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 B 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 B 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 B 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 B 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 B 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 B 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 B 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 B 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 B 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 B 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 B 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 B 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 B 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 B 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 B 226 SER LEU SER PRO GLY
SEQRES 1 C 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 C 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 C 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 C 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 C 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 C 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 C 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 C 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 C 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 C 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 C 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 C 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 C 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 C 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 C 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 C 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 C 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 C 226 SER LEU SER PRO GLY
SEQRES 1 D 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 D 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 D 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 D 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 D 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 D 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 D 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 D 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 D 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 D 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 D 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 D 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 D 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 D 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 D 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 D 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 D 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 D 226 SER LEU SER PRO GLY
SEQRES 1 E 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 E 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 E 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 E 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 E 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 E 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 E 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 E 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 E 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 E 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 E 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 E 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 E 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 E 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 E 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 E 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 E 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 E 226 SER LEU SER PRO GLY
SEQRES 1 F 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 F 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 F 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 F 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 F 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 F 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 F 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 F 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 F 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 F 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 F 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 F 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 F 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 F 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 F 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 F 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 F 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 F 226 SER LEU SER PRO GLY
SEQRES 1 G 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 G 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 G 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 G 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 G 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 G 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 G 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 G 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 G 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 G 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 G 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 G 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 G 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 G 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 G 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 G 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 G 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 G 226 SER LEU SER PRO GLY
SEQRES 1 H 226 ASP LYS THR HIS THR CYS PRO PRO CYS PRO ALA PRO GLU
SEQRES 2 H 226 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 3 H 226 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 4 H 226 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 5 H 226 VAL LYS PHE ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 6 H 226 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 7 H 226 THR TYR ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 8 H 226 ASP TRP LEU ASN GLY LYS GLU TYR GLU CYS LYS VAL SER
SEQRES 9 H 226 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 10 H 226 LYS ALA LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 11 H 226 LEU PRO PRO SER ARG ASP GLU LEU THR LYS ASN GLN VAL
SEQRES 12 H 226 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 13 H 226 ILE ALA VAL GLU TRP GLU SER ASN GLY ARG PRO GLU ASN
SEQRES 14 H 226 ASN TYR LYS THR THR PRO PRO VAL LEU ASP SER ASP GLY
SEQRES 15 H 226 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 16 H 226 ARG TRP GLN GLN GLY ASN VAL PHE SER CYS SER VAL MET
SEQRES 17 H 226 HIS GLU ALA LEU HIS ASN HIS TYR THR GLN LYS SER LEU
SEQRES 18 H 226 SER LEU SER PRO GLY
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET MAN I 4 11
HET NAG I 5 14
HET MAN I 6 11
HET NAG I 7 14
HET FUC I 8 10
HET BMA J 1 11
HET MAN J 2 11
HET NAG J 3 14
HET BMA K 1 11
HET MAN K 2 11
HET NAG K 3 14
HET NAG L 1 14
HET NAG L 2 14
HET BMA L 3 11
HET MAN L 4 11
HET NAG L 5 14
HET MAN L 6 11
HET FUC L 7 10
HET NAG M 1 14
HET NAG M 2 14
HET BMA M 3 11
HET MAN M 4 11
HET NAG M 5 14
HET MAN M 6 11
HET NAG M 7 14
HET FUC M 8 10
HET NAG N 1 14
HET NAG N 2 14
HET BMA N 3 11
HET MAN N 4 11
HET NAG N 5 14
HET MAN N 6 11
HET NAG N 7 14
HET FUC N 8 10
HET K A 509 1
HET MAN B 501 11
HET MAN B 502 11
HET NAG B 503 14
HET K D 504 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM K POTASSIUM ION
FORMUL 9 NAG 18(C8 H15 N O6)
FORMUL 9 BMA 6(C6 H12 O6)
FORMUL 9 MAN 12(C6 H12 O6)
FORMUL 9 FUC 4(C6 H12 O5)
FORMUL 15 K 2(K 1+)
FORMUL 20 HOH *36(H2 O)
HELIX 1 AA1 LYS A 246 MET A 252 1 7
HELIX 2 AA2 LEU A 309 ASN A 315 1 7
HELIX 3 AA3 ASP A 356 LYS A 360 5 5
HELIX 4 AA4 LYS A 414 GLN A 419 1 6
HELIX 5 AA5 LEU A 432 TYR A 436 5 5
HELIX 6 AA6 LYS B 246 MET B 252 1 7
HELIX 7 AA7 LEU B 309 ASN B 315 1 7
HELIX 8 AA8 SER B 354 LYS B 360 5 7
HELIX 9 AA9 LYS B 414 GLN B 419 1 6
HELIX 10 AB1 LEU B 432 TYR B 436 5 5
HELIX 11 AB2 LYS C 246 MET C 252 1 7
HELIX 12 AB3 LEU C 309 ASN C 315 1 7
HELIX 13 AB4 SER C 354 LYS C 360 5 7
HELIX 14 AB5 LYS C 414 GLN C 419 1 6
HELIX 15 AB6 LEU C 432 TYR C 436 5 5
HELIX 16 AB7 LYS D 246 MET D 252 1 7
HELIX 17 AB8 LEU D 309 ASN D 315 1 7
HELIX 18 AB9 SER D 354 LYS D 360 5 7
HELIX 19 AC1 LYS D 414 GLY D 420 1 7
HELIX 20 AC2 LEU D 432 TYR D 436 5 5
HELIX 21 AC3 LYS E 246 MET E 252 1 7
HELIX 22 AC4 LEU E 309 ASN E 315 1 7
HELIX 23 AC5 ASP E 356 LYS E 360 5 5
HELIX 24 AC6 LYS E 414 GLN E 419 1 6
HELIX 25 AC7 LEU E 432 TYR E 436 5 5
HELIX 26 AC8 LYS F 246 MET F 252 1 7
HELIX 27 AC9 LEU F 309 ASN F 315 1 7
HELIX 28 AD1 LYS F 414 GLN F 419 1 6
HELIX 29 AD2 LYS G 246 MET G 252 1 7
HELIX 30 AD3 LEU G 309 ASN G 315 1 7
HELIX 31 AD4 ASP G 356 LYS G 360 5 5
HELIX 32 AD5 LYS G 414 GLN G 419 1 6
HELIX 33 AD6 LEU G 432 TYR G 436 5 5
HELIX 34 AD7 LYS H 246 MET H 252 1 7
HELIX 35 AD8 LEU H 309 ASN H 315 1 7
HELIX 36 AD9 SER H 354 LYS H 360 5 7
HELIX 37 AE1 LYS H 414 GLN H 419 1 6
HELIX 38 AE2 LEU H 432 TYR H 436 5 5
SHEET 1 AA1 4 SER A 239 PHE A 243 0
SHEET 2 AA1 4 GLU A 258 VAL A 266 -1 O VAL A 264 N SER A 239
SHEET 3 AA1 4 TYR A 300 THR A 307 -1 O SER A 304 N CYS A 261
SHEET 4 AA1 4 ALA A 287 THR A 289 -1 N LYS A 288 O VAL A 305
SHEET 1 AA2 4 VAL A 282 VAL A 284 0
SHEET 2 AA2 4 VAL A 273 VAL A 279 -1 N TRP A 277 O VAL A 284
SHEET 3 AA2 4 TYR A 319 ASN A 325 -1 O GLU A 320 N TYR A 278
SHEET 4 AA2 4 ILE A 332 ILE A 336 -1 O LYS A 334 N CYS A 321
SHEET 1 AA3 4 GLN A 347 LEU A 351 0
SHEET 2 AA3 4 GLN A 362 PHE A 372 -1 O THR A 366 N LEU A 351
SHEET 3 AA3 4 PHE A 404 ASP A 413 -1 O LEU A 410 N LEU A 365
SHEET 4 AA3 4 TYR A 391 THR A 393 -1 N LYS A 392 O LYS A 409
SHEET 1 AA4 4 GLN A 347 LEU A 351 0
SHEET 2 AA4 4 GLN A 362 PHE A 372 -1 O THR A 366 N LEU A 351
SHEET 3 AA4 4 PHE A 404 ASP A 413 -1 O LEU A 410 N LEU A 365
SHEET 4 AA4 4 VAL A 397 LEU A 398 -1 N VAL A 397 O PHE A 405
SHEET 1 AA5 4 ARG A 386 GLU A 388 0
SHEET 2 AA5 4 ALA A 378 SER A 383 -1 N SER A 383 O ARG A 386
SHEET 3 AA5 4 PHE A 423 MET A 428 -1 O SER A 424 N GLU A 382
SHEET 4 AA5 4 THR A 437 LEU A 441 -1 O LYS A 439 N CYS A 425
SHEET 1 AA6 3 GLU B 258 VAL B 263 0
SHEET 2 AA6 3 VAL B 302 THR B 307 -1 O SER B 304 N CYS B 261
SHEET 3 AA6 3 ALA B 287 LYS B 290 -1 N LYS B 288 O VAL B 305
SHEET 1 AA7 4 VAL B 282 VAL B 284 0
SHEET 2 AA7 4 ASN B 276 VAL B 279 -1 N TRP B 277 O VAL B 284
SHEET 3 AA7 4 TYR B 319 LYS B 322 -1 O GLU B 320 N TYR B 278
SHEET 4 AA7 4 LYS B 334 ILE B 336 -1 O LYS B 334 N CYS B 321
SHEET 1 AA8 4 GLN B 347 LEU B 351 0
SHEET 2 AA8 4 GLN B 362 PHE B 372 -1 O THR B 366 N LEU B 351
SHEET 3 AA8 4 PHE B 404 ASP B 413 -1 O LEU B 410 N LEU B 365
SHEET 4 AA8 4 TYR B 391 THR B 393 -1 N LYS B 392 O LYS B 409
SHEET 1 AA9 4 GLN B 347 LEU B 351 0
SHEET 2 AA9 4 GLN B 362 PHE B 372 -1 O THR B 366 N LEU B 351
SHEET 3 AA9 4 PHE B 404 ASP B 413 -1 O LEU B 410 N LEU B 365
SHEET 4 AA9 4 VAL B 397 LEU B 398 -1 N VAL B 397 O PHE B 405
SHEET 1 AB1 4 ARG B 386 PRO B 387 0
SHEET 2 AB1 4 ILE B 377 SER B 383 -1 N SER B 383 O ARG B 386
SHEET 3 AB1 4 VAL B 422 HIS B 429 -1 O SER B 426 N GLU B 380
SHEET 4 AB1 4 THR B 437 SER B 442 -1 O LEU B 441 N PHE B 423
SHEET 1 AB2 2 GLU C 258 THR C 260 0
SHEET 2 AB2 2 VAL C 305 THR C 307 -1 O LEU C 306 N VAL C 259
SHEET 1 AB3 3 VAL C 282 GLU C 283 0
SHEET 2 AB3 3 TYR C 278 VAL C 279 -1 N VAL C 279 O VAL C 282
SHEET 3 AB3 3 TYR C 319 GLU C 320 -1 O GLU C 320 N TYR C 278
SHEET 1 AB4 4 GLN C 347 LEU C 351 0
SHEET 2 AB4 4 GLN C 362 PHE C 372 -1 O LEU C 368 N TYR C 349
SHEET 3 AB4 4 PHE C 404 ASP C 413 -1 O LEU C 410 N LEU C 365
SHEET 4 AB4 4 TYR C 391 THR C 393 -1 N LYS C 392 O LYS C 409
SHEET 1 AB5 4 GLN C 347 LEU C 351 0
SHEET 2 AB5 4 GLN C 362 PHE C 372 -1 O LEU C 368 N TYR C 349
SHEET 3 AB5 4 PHE C 404 ASP C 413 -1 O LEU C 410 N LEU C 365
SHEET 4 AB5 4 VAL C 397 LEU C 398 -1 N VAL C 397 O PHE C 405
SHEET 1 AB6 4 ARG C 386 PRO C 387 0
SHEET 2 AB6 4 ALA C 378 SER C 383 -1 N SER C 383 O ARG C 386
SHEET 3 AB6 4 PHE C 423 MET C 428 -1 O SER C 424 N GLU C 382
SHEET 4 AB6 4 THR C 437 LEU C 441 -1 O LYS C 439 N CYS C 425
SHEET 1 AB7 4 VAL D 240 PHE D 243 0
SHEET 2 AB7 4 GLU D 258 VAL D 266 -1 O THR D 260 N PHE D 243
SHEET 3 AB7 4 TYR D 300 THR D 307 -1 O SER D 304 N CYS D 261
SHEET 4 AB7 4 ALA D 287 THR D 289 -1 N LYS D 288 O VAL D 305
SHEET 1 AB8 4 VAL D 282 VAL D 284 0
SHEET 2 AB8 4 LYS D 274 VAL D 279 -1 N VAL D 279 O VAL D 282
SHEET 3 AB8 4 TYR D 319 SER D 324 -1 O SER D 324 N LYS D 274
SHEET 4 AB8 4 ILE D 332 ILE D 336 -1 O ILE D 336 N TYR D 319
SHEET 1 AB9 4 GLN D 347 LEU D 351 0
SHEET 2 AB9 4 GLN D 362 PHE D 372 -1 O THR D 366 N LEU D 351
SHEET 3 AB9 4 PHE D 404 ASP D 413 -1 O LEU D 410 N LEU D 365
SHEET 4 AB9 4 TYR D 391 THR D 393 -1 N LYS D 392 O LYS D 409
SHEET 1 AC1 4 GLN D 347 LEU D 351 0
SHEET 2 AC1 4 GLN D 362 PHE D 372 -1 O THR D 366 N LEU D 351
SHEET 3 AC1 4 PHE D 404 ASP D 413 -1 O LEU D 410 N LEU D 365
SHEET 4 AC1 4 VAL D 397 LEU D 398 -1 N VAL D 397 O PHE D 405
SHEET 1 AC2 4 ARG D 386 PRO D 387 0
SHEET 2 AC2 4 ALA D 378 SER D 383 -1 N SER D 383 O ARG D 386
SHEET 3 AC2 4 PHE D 423 MET D 428 -1 O SER D 426 N GLU D 380
SHEET 4 AC2 4 THR D 437 LEU D 441 -1 O LYS D 439 N CYS D 425
SHEET 1 AC3 4 SER E 239 PHE E 243 0
SHEET 2 AC3 4 GLU E 258 VAL E 266 -1 O VAL E 262 N PHE E 241
SHEET 3 AC3 4 TYR E 300 THR E 307 -1 O SER E 304 N CYS E 261
SHEET 4 AC3 4 LYS E 288 THR E 289 -1 N LYS E 288 O VAL E 305
SHEET 1 AC4 4 SER E 239 PHE E 243 0
SHEET 2 AC4 4 GLU E 258 VAL E 266 -1 O VAL E 262 N PHE E 241
SHEET 3 AC4 4 TYR E 300 THR E 307 -1 O SER E 304 N CYS E 261
SHEET 4 AC4 4 GLU E 293 GLU E 294 -1 N GLU E 293 O ARG E 301
SHEET 1 AC5 4 VAL E 282 VAL E 284 0
SHEET 2 AC5 4 VAL E 273 VAL E 279 -1 N VAL E 279 O VAL E 282
SHEET 3 AC5 4 TYR E 319 ASN E 325 -1 O GLU E 320 N TYR E 278
SHEET 4 AC5 4 ILE E 332 ILE E 336 -1 O ILE E 336 N TYR E 319
SHEET 1 AC6 4 GLN E 347 LEU E 351 0
SHEET 2 AC6 4 GLN E 362 PHE E 372 -1 O LEU E 368 N TYR E 349
SHEET 3 AC6 4 PHE E 404 ASP E 413 -1 O LEU E 410 N LEU E 365
SHEET 4 AC6 4 TYR E 391 THR E 393 -1 N LYS E 392 O LYS E 409
SHEET 1 AC7 4 GLN E 347 LEU E 351 0
SHEET 2 AC7 4 GLN E 362 PHE E 372 -1 O LEU E 368 N TYR E 349
SHEET 3 AC7 4 PHE E 404 ASP E 413 -1 O LEU E 410 N LEU E 365
SHEET 4 AC7 4 VAL E 397 LEU E 398 -1 N VAL E 397 O PHE E 405
SHEET 1 AC8 4 ARG E 386 GLU E 388 0
SHEET 2 AC8 4 ALA E 378 SER E 383 -1 N SER E 383 O ARG E 386
SHEET 3 AC8 4 PHE E 423 MET E 428 -1 O MET E 428 N ALA E 378
SHEET 4 AC8 4 THR E 437 LEU E 441 -1 O LYS E 439 N CYS E 425
SHEET 1 AC9 4 VAL F 240 LEU F 242 0
SHEET 2 AC9 4 GLU F 258 VAL F 263 -1 O VAL F 262 N PHE F 241
SHEET 3 AC9 4 VAL F 302 THR F 307 -1 O VAL F 302 N VAL F 263
SHEET 4 AC9 4 ALA F 287 THR F 289 -1 N LYS F 288 O VAL F 305
SHEET 1 AD1 2 TYR F 319 CYS F 321 0
SHEET 2 AD1 2 LYS F 334 ILE F 336 -1 O ILE F 336 N TYR F 319
SHEET 1 AD2 4 GLN F 347 LEU F 351 0
SHEET 2 AD2 4 GLN F 362 PHE F 372 -1 O LYS F 370 N GLN F 347
SHEET 3 AD2 4 PHE F 404 ASP F 413 -1 O LEU F 410 N LEU F 365
SHEET 4 AD2 4 TYR F 391 THR F 393 -1 N LYS F 392 O LYS F 409
SHEET 1 AD3 4 GLN F 347 LEU F 351 0
SHEET 2 AD3 4 GLN F 362 PHE F 372 -1 O LYS F 370 N GLN F 347
SHEET 3 AD3 4 PHE F 404 ASP F 413 -1 O LEU F 410 N LEU F 365
SHEET 4 AD3 4 VAL F 397 LEU F 398 -1 N VAL F 397 O PHE F 405
SHEET 1 AD4 4 ARG F 386 PRO F 387 0
SHEET 2 AD4 4 ALA F 378 SER F 383 -1 N SER F 383 O ARG F 386
SHEET 3 AD4 4 PHE F 423 MET F 428 -1 O SER F 424 N GLU F 382
SHEET 4 AD4 4 THR F 437 LEU F 441 -1 O LYS F 439 N CYS F 425
SHEET 1 AD5 2 LEU G 234 LEU G 235 0
SHEET 2 AD5 2 GLU H 233 LEU H 234 1 O GLU H 233 N LEU G 235
SHEET 1 AD6 4 SER G 239 PHE G 243 0
SHEET 2 AD6 4 GLU G 258 VAL G 266 -1 O VAL G 262 N PHE G 241
SHEET 3 AD6 4 TYR G 300 THR G 307 -1 O SER G 304 N CYS G 261
SHEET 4 AD6 4 LYS G 288 THR G 289 -1 N LYS G 288 O VAL G 305
SHEET 1 AD7 4 VAL G 282 VAL G 284 0
SHEET 2 AD7 4 VAL G 273 VAL G 279 -1 N TRP G 277 O VAL G 284
SHEET 3 AD7 4 TYR G 319 ASN G 325 -1 O GLU G 320 N TYR G 278
SHEET 4 AD7 4 ILE G 332 ILE G 336 -1 O ILE G 336 N TYR G 319
SHEET 1 AD8 4 GLN G 347 LEU G 351 0
SHEET 2 AD8 4 GLN G 362 PHE G 372 -1 O LEU G 368 N TYR G 349
SHEET 3 AD8 4 PHE G 404 ASP G 413 -1 O LEU G 410 N LEU G 365
SHEET 4 AD8 4 TYR G 391 THR G 393 -1 N LYS G 392 O LYS G 409
SHEET 1 AD9 4 GLN G 347 LEU G 351 0
SHEET 2 AD9 4 GLN G 362 PHE G 372 -1 O LEU G 368 N TYR G 349
SHEET 3 AD9 4 PHE G 404 ASP G 413 -1 O LEU G 410 N LEU G 365
SHEET 4 AD9 4 VAL G 397 LEU G 398 -1 N VAL G 397 O PHE G 405
SHEET 1 AE1 4 ARG G 386 PRO G 387 0
SHEET 2 AE1 4 ALA G 378 SER G 383 -1 N SER G 383 O ARG G 386
SHEET 3 AE1 4 PHE G 423 MET G 428 -1 O MET G 428 N ALA G 378
SHEET 4 AE1 4 THR G 437 LEU G 441 -1 O THR G 437 N VAL G 427
SHEET 1 AE2 4 SER H 239 PHE H 243 0
SHEET 2 AE2 4 GLU H 258 VAL H 266 -1 O VAL H 262 N PHE H 241
SHEET 3 AE2 4 TYR H 300 THR H 307 -1 O SER H 304 N CYS H 261
SHEET 4 AE2 4 ALA H 287 THR H 289 -1 N LYS H 288 O VAL H 305
SHEET 1 AE3 4 SER H 239 PHE H 243 0
SHEET 2 AE3 4 GLU H 258 VAL H 266 -1 O VAL H 262 N PHE H 241
SHEET 3 AE3 4 TYR H 300 THR H 307 -1 O SER H 304 N CYS H 261
SHEET 4 AE3 4 GLU H 293 GLU H 294 -1 N GLU H 293 O ARG H 301
SHEET 1 AE4 4 VAL H 282 VAL H 284 0
SHEET 2 AE4 4 VAL H 273 VAL H 279 -1 N VAL H 279 O VAL H 282
SHEET 3 AE4 4 TYR H 319 ASN H 325 -1 O GLU H 320 N TYR H 278
SHEET 4 AE4 4 ILE H 332 ILE H 336 -1 O ILE H 336 N TYR H 319
SHEET 1 AE5 4 GLN H 347 LEU H 351 0
SHEET 2 AE5 4 GLN H 362 PHE H 372 -1 O LEU H 368 N TYR H 349
SHEET 3 AE5 4 PHE H 404 ASP H 413 -1 O LEU H 410 N LEU H 365
SHEET 4 AE5 4 TYR H 391 THR H 393 -1 N LYS H 392 O LYS H 409
SHEET 1 AE6 4 GLN H 347 LEU H 351 0
SHEET 2 AE6 4 GLN H 362 PHE H 372 -1 O LEU H 368 N TYR H 349
SHEET 3 AE6 4 PHE H 404 ASP H 413 -1 O LEU H 410 N LEU H 365
SHEET 4 AE6 4 VAL H 397 LEU H 398 -1 N VAL H 397 O PHE H 405
SHEET 1 AE7 4 ARG H 386 PRO H 387 0
SHEET 2 AE7 4 ILE H 377 SER H 383 -1 N SER H 383 O ARG H 386
SHEET 3 AE7 4 PHE H 423 HIS H 429 -1 O SER H 426 N GLU H 380
SHEET 4 AE7 4 THR H 437 LEU H 441 -1 O LYS H 439 N CYS H 425
SSBOND 1 CYS A 261 CYS A 321 1555 1555 2.03
SSBOND 2 CYS A 367 CYS A 425 1555 1555 2.03
SSBOND 3 CYS B 261 CYS B 321 1555 1555 2.04
SSBOND 4 CYS B 367 CYS B 425 1555 1555 2.03
SSBOND 5 CYS C 261 CYS C 321 1555 1555 2.04
SSBOND 6 CYS C 367 CYS C 425 1555 1555 2.03
SSBOND 7 CYS D 261 CYS D 321 1555 1555 2.03
SSBOND 8 CYS D 367 CYS D 425 1555 1555 2.03
SSBOND 9 CYS E 261 CYS E 321 1555 1555 2.03
SSBOND 10 CYS E 367 CYS E 425 1555 1555 2.03
SSBOND 11 CYS F 261 CYS F 321 1555 1555 2.03
SSBOND 12 CYS F 367 CYS F 425 1555 1555 2.03
SSBOND 13 CYS G 226 CYS H 226 1555 1555 2.03
SSBOND 14 CYS G 229 CYS H 229 1555 1555 2.03
SSBOND 15 CYS G 261 CYS G 321 1555 1555 2.03
SSBOND 16 CYS G 367 CYS G 425 1555 1555 2.03
SSBOND 17 CYS H 261 CYS H 321 1555 1555 2.03
SSBOND 18 CYS H 367 CYS H 425 1555 1555 2.03
LINK ND2 ASN A 297 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN E 297 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN G 297 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN H 297 C1 NAG N 1 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O6 NAG I 1 C1 FUC I 8 1555 1555 1.45
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44
LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.44
LINK O6 BMA I 3 C1 MAN I 6 1555 1555 1.44
LINK O2 MAN I 4 C1 NAG I 5 1555 1555 1.44
LINK O2 MAN I 6 C1 NAG I 7 1555 1555 1.44
LINK O3 BMA J 1 C1 MAN J 2 1555 1555 1.45
LINK O2 MAN J 2 C1 NAG J 3 1555 1555 1.44
LINK O6 BMA K 1 C1 MAN K 2 1555 1555 1.44
LINK O2 MAN K 2 C1 NAG K 3 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45
LINK O6 NAG L 1 C1 FUC L 7 1555 1555 1.43
LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.45
LINK O6 BMA L 3 C1 MAN L 4 1555 1555 1.45
LINK O3 BMA L 3 C1 MAN L 6 1555 1555 1.44
LINK O2 MAN L 4 C1 NAG L 5 1555 1555 1.45
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45
LINK O6 NAG M 1 C1 FUC M 8 1555 1555 1.44
LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44
LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.45
LINK O6 BMA M 3 C1 MAN M 6 1555 1555 1.45
LINK O2 MAN M 4 C1 NAG M 5 1555 1555 1.45
LINK O2 MAN M 6 C1 NAG M 7 1555 1555 1.44
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45
LINK O6 NAG N 1 C1 FUC N 8 1555 1555 1.44
LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.46
LINK O2 BMA N 3 C1 MAN N 4 1555 1555 1.46
LINK O6 BMA N 3 C1 MAN N 6 1555 1555 1.44
LINK O2 MAN N 4 C1 NAG N 5 1555 1555 1.45
LINK O2 MAN N 6 C1 NAG N 7 1555 1555 1.44
CISPEP 1 TYR A 373 PRO A 374 0 4.99
CISPEP 2 TYR B 373 PRO B 374 0 -0.59
CISPEP 3 TYR C 373 PRO C 374 0 -0.23
CISPEP 4 TYR D 373 PRO D 374 0 -0.50
CISPEP 5 TYR E 373 PRO E 374 0 4.03
CISPEP 6 TYR F 373 PRO F 374 0 0.67
CISPEP 7 TYR G 373 PRO G 374 0 4.30
CISPEP 8 TYR H 373 PRO H 374 0 -0.12
CRYST1 93.615 141.020 98.866 90.00 117.33 90.00 P 1 21 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010682 0.000000 0.005520 0.00000
SCALE2 0.000000 0.007091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011385 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
