HEADER IMMUNE SYSTEM 12-AUG-15 5D6D
TITLE CRYSTAL STRUCTURE OF GASDALIE IGG1 FC IN COMPLEX WITH FCGRIIIA
CAVEAT 5D6D NAG C 302 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IG GAMMA-1 CHAIN C REGION;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 109-329;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR III-A;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: UNP RESIDUES 14-205;
COMPND 11 SYNONYM: CD16A ANTIGEN,FC-GAMMA RIII-ALPHA,FCRIIIA,FCR-10,IGG FC
COMPND 12 RECEPTOR III-2;
COMPND 13 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_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: FCGR3A, CD16A, FCG3, FCGR3, IGFR3;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS ADCC, IMMUNE SYSTEM, IGG
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.AHMED,P.J.BJORKMAN
REVDAT 7 27-SEP-23 5D6D 1 HETSYN LINK
REVDAT 6 29-JUL-20 5D6D 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 11-DEC-19 5D6D 1 REMARK
REVDAT 4 27-SEP-17 5D6D 1 JRNL REMARK
REVDAT 3 02-MAR-16 5D6D 1 JRNL
REVDAT 2 24-FEB-16 5D6D 1 JRNL
REVDAT 1 10-FEB-16 5D6D 0
JRNL AUTH A.A.AHMED,S.R.KEREMANE,J.VIELMETTER,P.J.BJORKMAN
JRNL TITL STRUCTURAL CHARACTERIZATION OF GASDALIE FC BOUND TO THE
JRNL TITL 2 ACTIVATING FC RECEPTOR FC GAMMA RIIIA.
JRNL REF J.STRUCT.BIOL. V. 194 78 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 26850169
JRNL DOI 10.1016/J.JSB.2016.02.001
REMARK 2
REMARK 2 RESOLUTION. 3.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 3.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 13945
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.273
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1395
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 71.3272 - 6.7418 1.00 1359 148 0.2499 0.2753
REMARK 3 2 6.7418 - 5.3517 1.00 1286 145 0.2752 0.2764
REMARK 3 3 5.3517 - 4.6754 1.00 1274 141 0.2270 0.2909
REMARK 3 4 4.6754 - 4.2480 1.00 1255 141 0.2262 0.2509
REMARK 3 5 4.2480 - 3.9435 1.00 1242 138 0.2501 0.2585
REMARK 3 6 3.9435 - 3.7110 1.00 1254 140 0.2961 0.3131
REMARK 3 7 3.7110 - 3.5252 0.99 1221 134 0.3044 0.3002
REMARK 3 8 3.5252 - 3.3717 0.99 1224 137 0.3191 0.3819
REMARK 3 9 3.3717 - 3.2419 0.99 1228 135 0.3849 0.4085
REMARK 3 10 3.2419 - 3.1301 0.97 1207 136 0.4271 0.4226
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) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.970
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 : 0.015 4884
REMARK 3 ANGLE : 1.459 6656
REMARK 3 CHIRALITY : 0.070 783
REMARK 3 PLANARITY : 0.011 822
REMARK 3 DIHEDRAL : 16.883 1794
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 5D6D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212637.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-14
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 : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14045
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.130
REMARK 200 RESOLUTION RANGE LOW (A) : 71.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, PHENIX
REMARK 200 STARTING MODEL: 3SGK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: GROWN IN SITTING DROP VAPOR DIFFUSION
REMARK 280 BY MIXING EQUAL VOLUMES OF PROTEIN (10 MG/ML) WITH A SOLUTION
REMARK 280 CONTAINING 0.04 M POTASSIUM DIHYDROGEN PHOSPHATE AND 16% (W/V)
REMARK 280 PEG 8000 AT 293.15 K, VAPOR DIFFUSION, SITTING DROP
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 37.19000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.33500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.33500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.19000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 198
REMARK 465 GLU A 199
REMARK 465 PHE A 200
REMARK 465 GLY A 201
REMARK 465 LEU A 202
REMARK 465 SER A 203
REMARK 465 TRP A 204
REMARK 465 LEU A 205
REMARK 465 PHE A 206
REMARK 465 LEU A 207
REMARK 465 VAL A 208
REMARK 465 ALA A 209
REMARK 465 ILE A 210
REMARK 465 LEU A 211
REMARK 465 LYS A 212
REMARK 465 GLY A 213
REMARK 465 VAL A 214
REMARK 465 GLN A 215
REMARK 465 CYS A 216
REMARK 465 GLU A 217
REMARK 465 VAL A 218
REMARK 465 GLN A 219
REMARK 465 LEU A 220
REMARK 465 LEU A 221
REMARK 465 GLU A 222
REMARK 465 THR A 223
REMARK 465 SER A 224
REMARK 465 THR A 225
REMARK 465 CYS A 226
REMARK 465 PRO A 227
REMARK 465 PRO A 228
REMARK 465 CYS A 229
REMARK 465 PRO A 230
REMARK 465 ALA A 231
REMARK 465 PRO A 232
REMARK 465 GLU A 233
REMARK 465 LEU A 234
REMARK 465 LEU A 235
REMARK 465 PRO A 445
REMARK 465 GLY A 446
REMARK 465 MET B 198
REMARK 465 GLU B 199
REMARK 465 PHE B 200
REMARK 465 GLY B 201
REMARK 465 LEU B 202
REMARK 465 SER B 203
REMARK 465 TRP B 204
REMARK 465 LEU B 205
REMARK 465 PHE B 206
REMARK 465 LEU B 207
REMARK 465 VAL B 208
REMARK 465 ALA B 209
REMARK 465 ILE B 210
REMARK 465 LEU B 211
REMARK 465 LYS B 212
REMARK 465 GLY B 213
REMARK 465 VAL B 214
REMARK 465 GLN B 215
REMARK 465 CYS B 216
REMARK 465 GLU B 217
REMARK 465 VAL B 218
REMARK 465 GLN B 219
REMARK 465 LEU B 220
REMARK 465 LEU B 221
REMARK 465 GLU B 222
REMARK 465 THR B 223
REMARK 465 SER 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 SER B 444
REMARK 465 PRO B 445
REMARK 465 GLY B 446
REMARK 465 MET C -17
REMARK 465 TRP C -16
REMARK 465 GLN C -15
REMARK 465 LEU C -14
REMARK 465 LEU C -13
REMARK 465 LEU C -12
REMARK 465 PRO C -11
REMARK 465 THR C -10
REMARK 465 ALA C -9
REMARK 465 LEU C -8
REMARK 465 LEU C -7
REMARK 465 LEU C -6
REMARK 465 LEU C -5
REMARK 465 VAL C -4
REMARK 465 SER C -3
REMARK 465 ALA C -2
REMARK 465 GLY C -1
REMARK 465 MET C 0
REMARK 465 ARG C 1
REMARK 465 THR C 2
REMARK 465 GLU C 3
REMARK 465 ASP C 4
REMARK 465 LEU C 5
REMARK 465 PRO C 6
REMARK 465 LYS C 7
REMARK 465 TYR C 33
REMARK 465 SER C 34
REMARK 465 PRO C 35
REMARK 465 GLU C 36
REMARK 465 ASP C 37
REMARK 465 GLN C 38
REMARK 465 SER C 39
REMARK 465 SER C 76
REMARK 465 THR C 77
REMARK 465 LEU C 78
REMARK 465 GLY C 175
REMARK 465 LEU C 176
REMARK 465 ALA C 177
REMARK 465 VAL C 178
REMARK 465 SER C 179
REMARK 465 THR C 180
REMARK 465 ILE C 181
REMARK 465 SER C 182
REMARK 465 SER C 183
REMARK 465 PHE C 184
REMARK 465 PHE C 185
REMARK 465 PRO C 186
REMARK 465 PRO C 187
REMARK 465 SER C 188
REMARK 465 ARG C 189
REMARK 465 GLY C 190
REMARK 465 GLY C 191
REMARK 465 GLY C 192
REMARK 465 GLY C 193
REMARK 465 SER C 194
REMARK 465 GLY C 195
REMARK 465 GLY C 196
REMARK 465 GLY C 197
REMARK 465 GLY C 198
REMARK 465 HIS C 199
REMARK 465 VAL C 200
REMARK 465 LEU C 201
REMARK 465 ASN C 202
REMARK 465 ASP C 203
REMARK 465 ILE C 204
REMARK 465 PHE C 205
REMARK 465 GLU C 206
REMARK 465 ALA C 207
REMARK 465 GLN C 208
REMARK 465 LYS C 209
REMARK 465 ILE C 210
REMARK 465 GLU C 211
REMARK 465 TRP C 212
REMARK 465 HIS C 213
REMARK 465 GLU C 214
REMARK 465 THR C 215
REMARK 465 GLY C 216
REMARK 465 HIS C 217
REMARK 465 HIS C 218
REMARK 465 HIS C 219
REMARK 465 HIS C 220
REMARK 465 HIS C 221
REMARK 465 HIS C 222
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 LYS A 246 CG CD CE NZ
REMARK 470 LYS A 248 CG CD CE NZ
REMARK 470 GLU A 258 CG CD OE1 OE2
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 GLU A 294 CG CD OE1 OE2
REMARK 470 SER A 298 OG
REMARK 470 TYR A 300 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 ARG A 355 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 246 CG CD CE NZ
REMARK 470 GLN B 419 CG CD OE1 NE2
REMARK 470 SER B 442 OG
REMARK 470 PHE C 11 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 13 CG CD OE1 OE2
REMARK 470 GLN C 30 CG CD OE1 NE2
REMARK 470 PHE C 43 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 48 CG CD1 CD2
REMARK 470 ILE C 49 CG1 CG2 CD1
REMARK 470 GLU C 68 CG CD OE1 OE2
REMARK 470 GLN C 72 CG CD OE1 NE2
REMARK 470 LYS C 101 CG CD CE NZ
REMARK 470 GLU C 103 CG CD OE1 OE2
REMARK 470 THR C 116 OG1 CG2
REMARK 470 LYS C 128 CG CD CE NZ
REMARK 470 LYS C 143 CG CD CE NZ
REMARK 470 ARG C 155 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 174 CG CD OE1 NE2
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 O2 MAN D 7 O5 NAG D 8 1.66
REMARK 500 O6 NAG E 1 C1 FUC B 509 1.82
REMARK 500 ND2 ASN C 162 O5 NAG C 301 1.98
REMARK 500 OE2 GLU A 382 OG SER A 426 2.02
REMARK 500 OE1 GLU A 388 NH2 ARG A 416 2.09
REMARK 500 ND2 ASN A 297 O5 NAG D 1 2.11
REMARK 500 NH1 ARG C 18 O LEU C 93 2.12
REMARK 500 OE1 GLU A 388 NH1 ARG A 416 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 238 C - N - CD ANGL. DEV. = 15.6 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 A 286 24.44 -178.53
REMARK 500 SER A 298 16.95 80.61
REMARK 500 SER B 254 -39.86 -39.36
REMARK 500 PRO B 331 151.28 -44.80
REMARK 500 SER B 400 5.36 -68.99
REMARK 500 ASN B 434 14.48 58.39
REMARK 500 GLU C 13 96.58 -166.20
REMARK 500 TRP C 16 116.46 -32.00
REMARK 500 SER C 55 136.14 -172.95
REMARK 500 SER C 66 -173.84 -69.52
REMARK 500 PHE C 153 145.77 -172.87
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 FUC B 509
DBREF 5D6D A 225 446 UNP P01857 IGHG1_HUMAN 108 329
DBREF 5D6D B 225 446 UNP P01857 IGHG1_HUMAN 108 329
DBREF 5D6D C -4 187 UNP P08637 FCG3A_HUMAN 14 205
SEQADV 5D6D MET A 198 UNP P01857 INITIATING METHIONINE
SEQADV 5D6D GLU A 199 UNP P01857 EXPRESSION TAG
SEQADV 5D6D PHE A 200 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLY A 201 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU A 202 UNP P01857 EXPRESSION TAG
SEQADV 5D6D SER A 203 UNP P01857 EXPRESSION TAG
SEQADV 5D6D TRP A 204 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU A 205 UNP P01857 EXPRESSION TAG
SEQADV 5D6D PHE A 206 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU A 207 UNP P01857 EXPRESSION TAG
SEQADV 5D6D VAL A 208 UNP P01857 EXPRESSION TAG
SEQADV 5D6D ALA A 209 UNP P01857 EXPRESSION TAG
SEQADV 5D6D ILE A 210 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU A 211 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LYS A 212 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLY A 213 UNP P01857 EXPRESSION TAG
SEQADV 5D6D VAL A 214 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLN A 215 UNP P01857 EXPRESSION TAG
SEQADV 5D6D CYS A 216 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLU A 217 UNP P01857 EXPRESSION TAG
SEQADV 5D6D VAL A 218 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLN A 219 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU A 220 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU A 221 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLU A 222 UNP P01857 EXPRESSION TAG
SEQADV 5D6D THR A 223 UNP P01857 EXPRESSION TAG
SEQADV 5D6D SER A 224 UNP P01857 EXPRESSION TAG
SEQADV 5D6D ALA A 236 UNP P01857 GLY 119 ENGINEERED MUTATION
SEQADV 5D6D ASP A 239 UNP P01857 SER 122 ENGINEERED MUTATION
SEQADV 5D6D LEU A 330 UNP P01857 ALA 213 ENGINEERED MUTATION
SEQADV 5D6D GLU A 332 UNP P01857 ILE 215 ENGINEERED MUTATION
SEQADV 5D6D MET B 198 UNP P01857 INITIATING METHIONINE
SEQADV 5D6D GLU B 199 UNP P01857 EXPRESSION TAG
SEQADV 5D6D PHE B 200 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLY B 201 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU B 202 UNP P01857 EXPRESSION TAG
SEQADV 5D6D SER B 203 UNP P01857 EXPRESSION TAG
SEQADV 5D6D TRP B 204 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU B 205 UNP P01857 EXPRESSION TAG
SEQADV 5D6D PHE B 206 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU B 207 UNP P01857 EXPRESSION TAG
SEQADV 5D6D VAL B 208 UNP P01857 EXPRESSION TAG
SEQADV 5D6D ALA B 209 UNP P01857 EXPRESSION TAG
SEQADV 5D6D ILE B 210 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU B 211 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LYS B 212 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLY B 213 UNP P01857 EXPRESSION TAG
SEQADV 5D6D VAL B 214 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLN B 215 UNP P01857 EXPRESSION TAG
SEQADV 5D6D CYS B 216 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLU B 217 UNP P01857 EXPRESSION TAG
SEQADV 5D6D VAL B 218 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLN B 219 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU B 220 UNP P01857 EXPRESSION TAG
SEQADV 5D6D LEU B 221 UNP P01857 EXPRESSION TAG
SEQADV 5D6D GLU B 222 UNP P01857 EXPRESSION TAG
SEQADV 5D6D THR B 223 UNP P01857 EXPRESSION TAG
SEQADV 5D6D SER B 224 UNP P01857 EXPRESSION TAG
SEQADV 5D6D ALA B 236 UNP P01857 GLY 119 ENGINEERED MUTATION
SEQADV 5D6D ASP B 239 UNP P01857 SER 122 ENGINEERED MUTATION
SEQADV 5D6D LEU B 330 UNP P01857 ALA 213 ENGINEERED MUTATION
SEQADV 5D6D GLU B 332 UNP P01857 ILE 215 ENGINEERED MUTATION
SEQADV 5D6D MET C -17 UNP P08637 EXPRESSION TAG
SEQADV 5D6D TRP C -16 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLN C -15 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C -14 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C -13 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C -12 UNP P08637 EXPRESSION TAG
SEQADV 5D6D PRO C -11 UNP P08637 EXPRESSION TAG
SEQADV 5D6D THR C -10 UNP P08637 EXPRESSION TAG
SEQADV 5D6D ALA C -9 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C -8 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C -7 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C -6 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C -5 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLN C 38 UNP P08637 ASN 56 ENGINEERED MUTATION
SEQADV 5D6D GLN C 74 UNP P08637 ASN 92 ENGINEERED MUTATION
SEQADV 5D6D GLN C 169 UNP P08637 ASN 187 ENGINEERED MUTATION
SEQADV 5D6D SER C 188 UNP P08637 EXPRESSION TAG
SEQADV 5D6D ARG C 189 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 190 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 191 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 192 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 193 UNP P08637 EXPRESSION TAG
SEQADV 5D6D SER C 194 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 195 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 196 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 197 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 198 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 199 UNP P08637 EXPRESSION TAG
SEQADV 5D6D VAL C 200 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LEU C 201 UNP P08637 EXPRESSION TAG
SEQADV 5D6D ASN C 202 UNP P08637 EXPRESSION TAG
SEQADV 5D6D ASP C 203 UNP P08637 EXPRESSION TAG
SEQADV 5D6D ILE C 204 UNP P08637 EXPRESSION TAG
SEQADV 5D6D PHE C 205 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLU C 206 UNP P08637 EXPRESSION TAG
SEQADV 5D6D ALA C 207 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLN C 208 UNP P08637 EXPRESSION TAG
SEQADV 5D6D LYS C 209 UNP P08637 EXPRESSION TAG
SEQADV 5D6D ILE C 210 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLU C 211 UNP P08637 EXPRESSION TAG
SEQADV 5D6D TRP C 212 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 213 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLU C 214 UNP P08637 EXPRESSION TAG
SEQADV 5D6D THR C 215 UNP P08637 EXPRESSION TAG
SEQADV 5D6D GLY C 216 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 217 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 218 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 219 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 220 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 221 UNP P08637 EXPRESSION TAG
SEQADV 5D6D HIS C 222 UNP P08637 EXPRESSION TAG
SEQRES 1 A 249 MET GLU PHE GLY LEU SER TRP LEU PHE LEU VAL ALA ILE
SEQRES 2 A 249 LEU LYS GLY VAL GLN CYS GLU VAL GLN LEU LEU GLU THR
SEQRES 3 A 249 SER THR CYS PRO PRO CYS PRO ALA PRO GLU LEU LEU ALA
SEQRES 4 A 249 GLY PRO ASP VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP
SEQRES 5 A 249 THR LEU MET ILE SER ARG THR PRO GLU VAL THR CYS VAL
SEQRES 6 A 249 VAL VAL ASP VAL SER HIS GLU ASP PRO GLU VAL LYS PHE
SEQRES 7 A 249 ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA LYS
SEQRES 8 A 249 THR LYS PRO ARG GLU GLU GLN TYR ASN SER THR TYR ARG
SEQRES 9 A 249 VAL VAL SER VAL LEU THR VAL LEU HIS GLN ASP TRP LEU
SEQRES 10 A 249 ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA
SEQRES 11 A 249 LEU PRO LEU PRO GLU GLU LYS THR ILE SER LYS ALA LYS
SEQRES 12 A 249 GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU PRO PRO
SEQRES 13 A 249 SER ARG ASP GLU LEU THR LYS ASN GLN VAL SER LEU THR
SEQRES 14 A 249 CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE ALA VAL
SEQRES 15 A 249 GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN TYR LYS
SEQRES 16 A 249 THR THR PRO PRO VAL LEU ASP SER ASP GLY SER PHE PHE
SEQRES 17 A 249 LEU TYR SER LYS LEU THR VAL ASP LYS SER ARG TRP GLN
SEQRES 18 A 249 GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS GLU ALA
SEQRES 19 A 249 LEU HIS ASN HIS TYR THR GLN LYS SER LEU SER LEU SER
SEQRES 20 A 249 PRO GLY
SEQRES 1 B 249 MET GLU PHE GLY LEU SER TRP LEU PHE LEU VAL ALA ILE
SEQRES 2 B 249 LEU LYS GLY VAL GLN CYS GLU VAL GLN LEU LEU GLU THR
SEQRES 3 B 249 SER THR CYS PRO PRO CYS PRO ALA PRO GLU LEU LEU ALA
SEQRES 4 B 249 GLY PRO ASP VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP
SEQRES 5 B 249 THR LEU MET ILE SER ARG THR PRO GLU VAL THR CYS VAL
SEQRES 6 B 249 VAL VAL ASP VAL SER HIS GLU ASP PRO GLU VAL LYS PHE
SEQRES 7 B 249 ASN TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA LYS
SEQRES 8 B 249 THR LYS PRO ARG GLU GLU GLN TYR ASN SER THR TYR ARG
SEQRES 9 B 249 VAL VAL SER VAL LEU THR VAL LEU HIS GLN ASP TRP LEU
SEQRES 10 B 249 ASN GLY LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA
SEQRES 11 B 249 LEU PRO LEU PRO GLU GLU LYS THR ILE SER LYS ALA LYS
SEQRES 12 B 249 GLY GLN PRO ARG GLU PRO GLN VAL TYR THR LEU PRO PRO
SEQRES 13 B 249 SER ARG ASP GLU LEU THR LYS ASN GLN VAL SER LEU THR
SEQRES 14 B 249 CYS LEU VAL LYS GLY PHE TYR PRO SER ASP ILE ALA VAL
SEQRES 15 B 249 GLU TRP GLU SER ASN GLY GLN PRO GLU ASN ASN TYR LYS
SEQRES 16 B 249 THR THR PRO PRO VAL LEU ASP SER ASP GLY SER PHE PHE
SEQRES 17 B 249 LEU TYR SER LYS LEU THR VAL ASP LYS SER ARG TRP GLN
SEQRES 18 B 249 GLN GLY ASN VAL PHE SER CYS SER VAL MET HIS GLU ALA
SEQRES 19 B 249 LEU HIS ASN HIS TYR THR GLN LYS SER LEU SER LEU SER
SEQRES 20 B 249 PRO GLY
SEQRES 1 C 240 MET TRP GLN LEU LEU LEU PRO THR ALA LEU LEU LEU LEU
SEQRES 2 C 240 VAL SER ALA GLY MET ARG THR GLU ASP LEU PRO LYS ALA
SEQRES 3 C 240 VAL VAL PHE LEU GLU PRO GLN TRP TYR ARG VAL LEU GLU
SEQRES 4 C 240 LYS ASP SER VAL THR LEU LYS CYS GLN GLY ALA TYR SER
SEQRES 5 C 240 PRO GLU ASP GLN SER THR GLN TRP PHE HIS ASN GLU SER
SEQRES 6 C 240 LEU ILE SER SER GLN ALA SER SER TYR PHE ILE ASP ALA
SEQRES 7 C 240 ALA THR VAL ASP ASP SER GLY GLU TYR ARG CYS GLN THR
SEQRES 8 C 240 GLN LEU SER THR LEU SER ASP PRO VAL GLN LEU GLU VAL
SEQRES 9 C 240 HIS ILE GLY TRP LEU LEU LEU GLN ALA PRO ARG TRP VAL
SEQRES 10 C 240 PHE LYS GLU GLU ASP PRO ILE HIS LEU ARG CYS HIS SER
SEQRES 11 C 240 TRP LYS ASN THR ALA LEU HIS LYS VAL THR TYR LEU GLN
SEQRES 12 C 240 ASN GLY LYS GLY ARG LYS TYR PHE HIS HIS ASN SER ASP
SEQRES 13 C 240 PHE TYR ILE PRO LYS ALA THR LEU LYS ASP SER GLY SER
SEQRES 14 C 240 TYR PHE CYS ARG GLY LEU PHE GLY SER LYS ASN VAL SER
SEQRES 15 C 240 SER GLU THR VAL GLN ILE THR ILE THR GLN GLY LEU ALA
SEQRES 16 C 240 VAL SER THR ILE SER SER PHE PHE PRO PRO SER ARG GLY
SEQRES 17 C 240 GLY GLY GLY SER GLY GLY GLY GLY HIS VAL LEU ASN ASP
SEQRES 18 C 240 ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU THR GLY
SEQRES 19 C 240 HIS HIS HIS HIS HIS HIS
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET NAG D 5 14
HET GAL D 6 11
HET MAN D 7 11
HET NAG D 8 14
HET FUL D 9 10
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET NAG E 5 14
HET GAL E 6 11
HET MAN E 7 11
HET NAG E 8 14
HET FUC B 509 10
HET NAG C 301 14
HET NAG C 302 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUL FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 4 NAG 10(C8 H15 N O6)
FORMUL 4 BMA 2(C6 H12 O6)
FORMUL 4 MAN 4(C6 H12 O6)
FORMUL 4 GAL 2(C6 H12 O6)
FORMUL 4 FUL C6 H12 O5
FORMUL 6 FUC C6 H12 O5
HELIX 1 AA1 LYS A 246 MET A 252 1 7
HELIX 2 AA2 LEU A 309 LEU A 314 1 6
HELIX 3 AA3 SER A 354 LYS A 360 5 7
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 HIS B 310 ASN B 315 1 6
HELIX 8 AA8 ASP B 356 LYS B 360 5 5
HELIX 9 AA9 ASP B 413 GLN B 418 1 6
HELIX 10 AB1 LEU B 432 TYR B 436 5 5
HELIX 11 AB2 THR C 62 SER C 66 5 5
HELIX 12 AB3 LYS C 114 THR C 116 5 3
HELIX 13 AB4 THR C 145 SER C 149 5 5
SHEET 1 AA1 4 ASP A 239 PHE A 243 0
SHEET 2 AA1 4 GLU A 258 VAL A 266 -1 O VAL A 262 N PHE A 241
SHEET 3 AA1 4 TYR A 300 THR A 307 -1 O SER A 304 N CYS A 261
SHEET 4 AA1 4 LYS A 288 LYS A 290 -1 N LYS A 290 O VAL A 303
SHEET 1 AA2 4 VAL A 282 VAL A 284 0
SHEET 2 AA2 4 LYS A 274 VAL A 279 -1 N TRP A 277 O VAL A 284
SHEET 3 AA2 4 TYR A 319 SER A 324 -1 O LYS A 322 N ASN A 276
SHEET 4 AA2 4 GLU A 332 ILE A 336 -1 O ILE A 336 N TYR A 319
SHEET 1 AA3 4 GLN A 347 LEU A 351 0
SHEET 2 AA3 4 GLN A 362 PHE A 372 -1 O LEU A 368 N TYR A 349
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 LEU A 368 N TYR A 349
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 GLN A 386 PRO A 387 0
SHEET 2 AA5 4 ALA A 378 SER A 383 -1 N SER A 383 O GLN A 386
SHEET 3 AA5 4 PHE A 423 MET A 428 -1 O SER A 426 N GLU A 380
SHEET 4 AA5 4 THR A 437 LEU A 441 -1 O LEU A 441 N PHE A 423
SHEET 1 AA6 4 ASP B 239 PHE B 243 0
SHEET 2 AA6 4 GLU B 258 VAL B 266 -1 O THR B 260 N PHE B 243
SHEET 3 AA6 4 TYR B 300 THR B 307 -1 O TYR B 300 N VAL B 266
SHEET 4 AA6 4 LYS B 288 THR B 289 -1 N LYS B 288 O VAL B 305
SHEET 1 AA7 4 VAL B 282 VAL B 284 0
SHEET 2 AA7 4 LYS B 274 VAL B 279 -1 N VAL B 279 O VAL B 282
SHEET 3 AA7 4 TYR B 319 SER B 324 -1 O LYS B 322 N ASN B 276
SHEET 4 AA7 4 GLU B 332 ILE B 336 -1 O GLU B 332 N VAL B 323
SHEET 1 AA8 4 GLN B 347 LEU B 351 0
SHEET 2 AA8 4 SER B 364 PHE B 372 -1 O THR B 366 N LEU B 351
SHEET 3 AA8 4 PHE B 404 THR B 411 -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 SER B 364 PHE B 372 -1 O THR B 366 N LEU B 351
SHEET 3 AA9 4 PHE B 404 THR B 411 -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 GLN B 386 PRO B 387 0
SHEET 2 AB1 4 ALA B 378 SER B 383 -1 N SER B 383 O GLN B 386
SHEET 3 AB1 4 PHE B 423 MET B 428 -1 O SER B 426 N GLU B 380
SHEET 4 AB1 4 THR B 437 LEU B 441 -1 O LEU B 441 N PHE B 423
SHEET 1 AB2 3 VAL C 9 LEU C 12 0
SHEET 2 AB2 3 VAL C 25 GLN C 30 -1 O LYS C 28 N PHE C 11
SHEET 3 AB2 3 SER C 55 ILE C 58 -1 O ILE C 58 N VAL C 25
SHEET 1 AB3 2 ARG C 18 LEU C 20 0
SHEET 2 AB3 2 GLU C 85 HIS C 87 1 O GLU C 85 N VAL C 19
SHEET 1 AB4 2 GLN C 41 HIS C 44 0
SHEET 2 AB4 2 TYR C 69 GLN C 72 -1 O GLN C 72 N GLN C 41
SHEET 1 AB5 3 LEU C 91 GLN C 94 0
SHEET 2 AB5 3 ILE C 106 SER C 112 -1 O HIS C 111 N LEU C 92
SHEET 3 AB5 3 PHE C 139 ILE C 141 -1 O PHE C 139 N LEU C 108
SHEET 1 AB6 2 VAL C 99 PHE C 100 0
SHEET 2 AB6 2 THR C 171 ILE C 172 1 O THR C 171 N PHE C 100
SHEET 1 AB7 4 LYS C 128 HIS C 135 0
SHEET 2 AB7 4 HIS C 119 GLN C 125 -1 N VAL C 121 O PHE C 133
SHEET 3 AB7 4 SER C 151 PHE C 158 -1 O ARG C 155 N THR C 122
SHEET 4 AB7 4 LYS C 161 SER C 164 -1 O LYS C 161 N PHE C 158
SHEET 1 AB8 4 LYS C 128 HIS C 135 0
SHEET 2 AB8 4 HIS C 119 GLN C 125 -1 N VAL C 121 O PHE C 133
SHEET 3 AB8 4 SER C 151 PHE C 158 -1 O ARG C 155 N THR C 122
SHEET 4 AB8 4 VAL C 168 GLN C 169 -1 O VAL C 168 N TYR C 152
SSBOND 1 CYS A 261 CYS A 321 1555 1555 2.53
SSBOND 2 CYS A 367 CYS A 425 1555 1555 2.01
SSBOND 3 CYS B 261 CYS B 321 1555 1555 2.03
SSBOND 4 CYS B 367 CYS B 425 1555 1555 2.14
SSBOND 5 CYS C 29 CYS C 71 1555 1555 1.89
SSBOND 6 CYS C 110 CYS C 154 1555 1555 2.04
LINK ND2 ASN A 297 C1 NAG D 1 1555 1555 1.26
LINK ND2 ASN B 297 C1 NAG E 1 1555 1555 1.50
LINK ND2 ASN C 45 C1 NAG C 302 1555 1555 1.37
LINK ND2 ASN C 162 C1 NAG C 301 1555 1555 1.56
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
LINK O6 NAG D 1 C1 FUL D 9 1555 1555 1.29
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.39
LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.40
LINK O3 BMA D 3 C1 MAN D 7 1555 1555 1.40
LINK O2 MAN D 4 C1 NAG D 5 1555 1555 1.39
LINK O4 NAG D 5 C1 GAL D 6 1555 1555 1.39
LINK O2 MAN D 7 C1 NAG D 8 1555 1555 1.26
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.39
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.39
LINK O6 BMA E 3 C1 MAN E 4 1555 1555 1.40
LINK O3 BMA E 3 C1 MAN E 7 1555 1555 1.39
LINK O2 MAN E 4 C1 NAG E 5 1555 1555 1.39
LINK O4 NAG E 5 C1 GAL E 6 1555 1555 1.39
LINK O2 MAN E 7 C1 NAG E 8 1555 1555 1.42
CISPEP 1 GLY A 237 PRO A 238 0 -1.57
CISPEP 2 TYR A 373 PRO A 374 0 3.43
CISPEP 3 GLY B 237 PRO B 238 0 9.04
CISPEP 4 TYR B 373 PRO B 374 0 -1.95
CISPEP 5 GLN B 419 GLY B 420 0 -1.75
CISPEP 6 GLU C 13 PRO C 14 0 2.66
CRYST1 74.380 94.500 108.670 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013445 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010582 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009202 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
