HEADER IMMUNE SYSTEM 05-DEC-13 3WN5
TITLE CRYSTAL STRUCTURE OF ASYMMETRICALLY ENGINEERED FC VARIANT IN COMPLEX
TITLE 2 WITH FCGRIIIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IG GAMMA-1 CHAIN C REGION;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: UNP RESIDUES 99-328;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: IG GAMMA-1 CHAIN C REGION;
COMPND 9 CHAIN: B, E;
COMPND 10 FRAGMENT: UNP RESIDUES 99-328;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR III-A;
COMPND 15 CHAIN: C, F;
COMPND 16 FRAGMENT: UNP RESIDUES 18-208;
COMPND 17 SYNONYM: CD16A ANTIGEN, FC-GAMMA RIII-ALPHA, FC-GAMMA RIII, FC-GAMMA
COMPND 18 RIIIA, FCRIII, FCRIIIA, FCR-10, IGG FC RECEPTOR III-2;
COMPND 19 ENGINEERED: YES;
COMPND 20 MUTATION: 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: HEK293F;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: IGHG1;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: FCGR3A, CD16A, FCG3, FCGR3, IGFR3;
SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS RECEPTOR COMPLEX, FC RECEPTOR, ANTIBODY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KADONO,F.MIMOTO,H.KATADA,T.IGAWA,T.KAMIKAWA,K.HATTORI
REVDAT 2 29-JUL-20 3WN5 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE ATOM
REVDAT 1 19-NOV-14 3WN5 0
JRNL AUTH F.MIMOTO,S.KADONO,H.KATADA,T.IGAWA,T.KAMIKAWA,K.HATTORI
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL ASYMMETRICALLY ENGINEERED FC
JRNL TITL 2 VARIANT WITH IMPROVED AFFINITY FOR FC GAMMA RS.
JRNL REF MOL.IMMUNOL. V. 58 132 2014
JRNL REFN ISSN 0161-5890
JRNL PMID 24334029
JRNL DOI 10.1016/J.MOLIMM.2013.11.017
REMARK 2
REMARK 2 RESOLUTION. 2.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 41404
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2192
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2952
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.4000
REMARK 3 BIN FREE R VALUE SET COUNT : 141
REMARK 3 BIN FREE R VALUE : 0.4420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 576
REMARK 3 SOLVENT ATOMS : 41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.24000
REMARK 3 B22 (A**2) : 1.51000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.699
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.382
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.308
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.885
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10211 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14018 ; 0.947 ; 2.012
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1175 ; 4.631 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 427 ;33.265 ;24.801
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1518 ;14.183 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;15.813 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1669 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7501 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4724 ; 1.288 ; 5.503
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5891 ; 2.341 ; 8.248
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5487 ; 1.140 ; 5.589
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES
REMARK 4
REMARK 4 3WN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000096544.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 95.0
REMARK 200 PH : 6.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
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 : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43675
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.780
REMARK 200 RESOLUTION RANGE LOW (A) : 49.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.61900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.090
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 (%): 58.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.5% PEG 3350, 0.1M BIS-TRIS, 0.2M
REMARK 280 SODIUM IODIDE, STREAK SEEDING, PH 6.25, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, 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 36.24500
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, K, L, M
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 GLU A 216
REMARK 465 PRO A 217
REMARK 465 LYS A 218
REMARK 465 SER A 219
REMARK 465 SER A 220
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 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 PRO A 445
REMARK 465 GLU B 216
REMARK 465 PRO B 217
REMARK 465 LYS B 218
REMARK 465 SER B 219
REMARK 465 SER B 220
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 TYR B 234
REMARK 465 PRO B 445
REMARK 465 MET C -3
REMARK 465 ARG C -2
REMARK 465 THR C -1
REMARK 465 GLU C 0
REMARK 465 GLU C 33
REMARK 465 ASP C 34
REMARK 465 GLY C 172
REMARK 465 LEU C 173
REMARK 465 ALA C 174
REMARK 465 VAL C 175
REMARK 465 SER C 176
REMARK 465 THR C 177
REMARK 465 ILE C 178
REMARK 465 SER C 179
REMARK 465 SER C 180
REMARK 465 PHE C 181
REMARK 465 PHE C 182
REMARK 465 PRO C 183
REMARK 465 PRO C 184
REMARK 465 GLY C 185
REMARK 465 TYR C 186
REMARK 465 GLN C 187
REMARK 465 HIS C 188
REMARK 465 HIS C 189
REMARK 465 HIS C 190
REMARK 465 HIS C 191
REMARK 465 HIS C 192
REMARK 465 HIS C 193
REMARK 465 GLU D 216
REMARK 465 PRO D 217
REMARK 465 LYS D 218
REMARK 465 SER D 219
REMARK 465 SER D 220
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 PRO D 445
REMARK 465 GLU E 216
REMARK 465 PRO E 217
REMARK 465 LYS E 218
REMARK 465 SER E 219
REMARK 465 SER E 220
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 TYR E 234
REMARK 465 PRO E 445
REMARK 465 MET F -3
REMARK 465 ARG F -2
REMARK 465 THR F -1
REMARK 465 GLU F 0
REMARK 465 GLU F 33
REMARK 465 ASP F 34
REMARK 465 LEU F 173
REMARK 465 ALA F 174
REMARK 465 VAL F 175
REMARK 465 SER F 176
REMARK 465 THR F 177
REMARK 465 ILE F 178
REMARK 465 SER F 179
REMARK 465 SER F 180
REMARK 465 PHE F 181
REMARK 465 PHE F 182
REMARK 465 PRO F 183
REMARK 465 PRO F 184
REMARK 465 GLY F 185
REMARK 465 TYR F 186
REMARK 465 GLN F 187
REMARK 465 HIS F 188
REMARK 465 HIS F 189
REMARK 465 HIS F 190
REMARK 465 HIS F 191
REMARK 465 HIS F 192
REMARK 465 HIS F 193
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 CD CE NZ
REMARK 470 LYS A 248 CE NZ
REMARK 470 GLU A 272 CD OE1 OE2
REMARK 470 LYS A 288 CD CE NZ
REMARK 470 LYS A 290 CG CD CE NZ
REMARK 470 GLN A 311 CG CD OE1 NE2
REMARK 470 LYS A 340 CD CE NZ
REMARK 470 LYS B 274 CD CE NZ
REMARK 470 LYS B 288 CD CE NZ
REMARK 470 LYS B 290 CD CE NZ
REMARK 470 GLU B 293 CD OE1 OE2
REMARK 470 LYS B 322 CD CE NZ
REMARK 470 LYS B 326 CD CE NZ
REMARK 470 ARG B 344 CD NE CZ NH1 NH2
REMARK 470 ARG B 355 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 10 CG CD OE1 OE2
REMARK 470 LYS C 25 CD CE NZ
REMARK 470 LYS C 144 CD CE NZ
REMARK 470 GLU D 233 CG CD OE1 OE2
REMARK 470 GLU D 272 CG CD OE1 OE2
REMARK 470 LYS D 274 CG CD CE NZ
REMARK 470 LYS D 288 CD CE NZ
REMARK 470 LYS D 290 CG CD CE NZ
REMARK 470 GLU D 293 CG CD OE1 OE2
REMARK 470 LYS D 340 CG CD CE NZ
REMARK 470 GLN D 342 CG CD OE1 NE2
REMARK 470 ARG D 355 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 360 CD CE NZ
REMARK 470 GLU E 272 CG CD OE1 OE2
REMARK 470 LYS E 288 CG CD CE NZ
REMARK 470 LYS E 290 CD CE NZ
REMARK 470 GLU E 293 CD OE1 OE2
REMARK 470 LYS E 322 CE NZ
REMARK 470 LYS E 326 CG CD CE NZ
REMARK 470 LYS E 340 CE NZ
REMARK 470 ARG E 355 CG CD NE CZ NH1 NH2
REMARK 470 ASN E 361 CG OD1 ND2
REMARK 470 GLN E 386 CD OE1 NE2
REMARK 470 ASN E 389 CG OD1 ND2
REMARK 470 LYS E 392 CD CE NZ
REMARK 470 LYS E 414 CD CE NZ
REMARK 470 ASN E 421 CG OD1 ND2
REMARK 470 ASN E 434 CG OD1 ND2
REMARK 470 LYS F 25 CD CE NZ
REMARK 470 LYS F 98 CG CD CE NZ
REMARK 470 LYS F 125 CG CD CE NZ
REMARK 470 LYS F 128 CD CE NZ
REMARK 470 LYS F 144 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 234 71.51 -108.60
REMARK 500 ASN A 390 72.04 -102.95
REMARK 500 PRO B 271 -150.97 -78.54
REMARK 500 ASP B 327 56.17 -108.14
REMARK 500 THR B 359 48.04 -94.86
REMARK 500 HIS B 435 16.28 53.55
REMARK 500 LYS C 19 -13.41 88.40
REMARK 500 LEU C 72 30.48 -99.50
REMARK 500 LYS C 117 61.03 62.05
REMARK 500 GLU D 357 40.36 -85.17
REMARK 500 ASN D 390 74.02 -101.77
REMARK 500 HIS D 435 -6.02 59.45
REMARK 500 PRO E 271 -154.46 -73.88
REMARK 500 ASN E 286 60.37 -114.19
REMARK 500 ASP E 327 41.64 -90.33
REMARK 500 ASN E 390 71.49 67.01
REMARK 500 LYS F 19 -4.63 82.52
REMARK 500 ILE F 46 -51.46 -122.21
REMARK 500 GLN F 49 -52.36 -123.57
REMARK 500 GLU F 100 -3.97 75.19
REMARK 500 LYS F 111 17.16 58.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE CONFLICT VAL158 IS RELATED TO A NATURALLY OCCURRING
REMARK 999 VARIATION IN THE SEQUENCE OF HFCGIIIA
DBREF 3WN5 A 216 445 UNP P01857 IGHG1_HUMAN 99 328
DBREF 3WN5 B 216 445 UNP P01857 IGHG1_HUMAN 99 328
DBREF 3WN5 C -3 187 UNP P08637 FCG3A_HUMAN 18 208
DBREF 3WN5 D 216 445 UNP P01857 IGHG1_HUMAN 99 328
DBREF 3WN5 E 216 445 UNP P01857 IGHG1_HUMAN 99 328
DBREF 3WN5 F -3 187 UNP P08637 FCG3A_HUMAN 18 208
SEQADV 3WN5 SER A 220 UNP P01857 CYS 103 ENGINEERED MUTATION
SEQADV 3WN5 GLU A 270 UNP P01857 ASP 153 ENGINEERED MUTATION
SEQADV 3WN5 ASP A 326 UNP P01857 LYS 209 ENGINEERED MUTATION
SEQADV 3WN5 LYS A 330 UNP P01857 ALA 213 ENGINEERED MUTATION
SEQADV 3WN5 GLU A 334 UNP P01857 LYS 217 ENGINEERED MUTATION
SEQADV 3WN5 CYS A 356 UNP P01857 ASP 239 ENGINEERED MUTATION
SEQADV 3WN5 SER A 366 UNP P01857 THR 249 ENGINEERED MUTATION
SEQADV 3WN5 ALA A 368 UNP P01857 LEU 251 ENGINEERED MUTATION
SEQADV 3WN5 VAL A 407 UNP P01857 TYR 290 ENGINEERED MUTATION
SEQADV 3WN5 SER B 220 UNP P01857 CYS 103 ENGINEERED MUTATION
SEQADV 3WN5 TYR B 234 UNP P01857 LEU 117 ENGINEERED MUTATION
SEQADV 3WN5 TYR B 235 UNP P01857 LEU 118 ENGINEERED MUTATION
SEQADV 3WN5 TRP B 236 UNP P01857 GLY 119 ENGINEERED MUTATION
SEQADV 3WN5 MET B 239 UNP P01857 SER 122 ENGINEERED MUTATION
SEQADV 3WN5 ASP B 268 UNP P01857 HIS 151 ENGINEERED MUTATION
SEQADV 3WN5 ALA B 298 UNP P01857 SER 181 ENGINEERED MUTATION
SEQADV 3WN5 ASP B 327 UNP P01857 ALA 210 ENGINEERED MUTATION
SEQADV 3WN5 CYS B 349 UNP P01857 TYR 232 ENGINEERED MUTATION
SEQADV 3WN5 TRP B 366 UNP P01857 THR 249 ENGINEERED MUTATION
SEQADV 3WN5 GLN C 35 UNP P08637 ASN 56 ENGINEERED MUTATION
SEQADV 3WN5 GLN C 71 UNP P08637 ASN 92 ENGINEERED MUTATION
SEQADV 3WN5 VAL C 155 UNP P08637 PHE 176 SEE REMARK 999
SEQADV 3WN5 GLN C 166 UNP P08637 ASN 187 ENGINEERED MUTATION
SEQADV 3WN5 HIS C 188 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS C 189 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS C 190 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS C 191 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS C 192 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS C 193 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 SER D 220 UNP P01857 CYS 103 ENGINEERED MUTATION
SEQADV 3WN5 GLU D 270 UNP P01857 ASP 153 ENGINEERED MUTATION
SEQADV 3WN5 ASP D 326 UNP P01857 LYS 209 ENGINEERED MUTATION
SEQADV 3WN5 LYS D 330 UNP P01857 ALA 213 ENGINEERED MUTATION
SEQADV 3WN5 GLU D 334 UNP P01857 LYS 217 ENGINEERED MUTATION
SEQADV 3WN5 CYS D 356 UNP P01857 ASP 239 ENGINEERED MUTATION
SEQADV 3WN5 SER D 366 UNP P01857 THR 249 ENGINEERED MUTATION
SEQADV 3WN5 ALA D 368 UNP P01857 LEU 251 ENGINEERED MUTATION
SEQADV 3WN5 VAL D 407 UNP P01857 TYR 290 ENGINEERED MUTATION
SEQADV 3WN5 SER E 220 UNP P01857 CYS 103 ENGINEERED MUTATION
SEQADV 3WN5 TYR E 234 UNP P01857 LEU 117 ENGINEERED MUTATION
SEQADV 3WN5 TYR E 235 UNP P01857 LEU 118 ENGINEERED MUTATION
SEQADV 3WN5 TRP E 236 UNP P01857 GLY 119 ENGINEERED MUTATION
SEQADV 3WN5 MET E 239 UNP P01857 SER 122 ENGINEERED MUTATION
SEQADV 3WN5 ASP E 268 UNP P01857 HIS 151 ENGINEERED MUTATION
SEQADV 3WN5 ALA E 298 UNP P01857 SER 181 ENGINEERED MUTATION
SEQADV 3WN5 ASP E 327 UNP P01857 ALA 210 ENGINEERED MUTATION
SEQADV 3WN5 CYS E 349 UNP P01857 TYR 232 ENGINEERED MUTATION
SEQADV 3WN5 TRP E 366 UNP P01857 THR 249 ENGINEERED MUTATION
SEQADV 3WN5 GLN F 35 UNP P08637 ASN 56 ENGINEERED MUTATION
SEQADV 3WN5 GLN F 71 UNP P08637 ASN 92 ENGINEERED MUTATION
SEQADV 3WN5 VAL F 155 UNP P08637 PHE 176 SEE REMARK 999
SEQADV 3WN5 GLN F 166 UNP P08637 ASN 187 ENGINEERED MUTATION
SEQADV 3WN5 HIS F 188 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS F 189 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS F 190 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS F 191 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS F 192 UNP P08637 EXPRESSION TAG
SEQADV 3WN5 HIS F 193 UNP P08637 EXPRESSION TAG
SEQRES 1 A 230 GLU PRO LYS SER SER ASP LYS THR HIS THR CYS PRO PRO
SEQRES 2 A 230 CYS PRO ALA PRO GLU LEU LEU GLY GLY PRO SER VAL PHE
SEQRES 3 A 230 LEU PHE PRO PRO LYS PRO LYS ASP THR LEU MET ILE SER
SEQRES 4 A 230 ARG THR PRO GLU VAL THR CYS VAL VAL VAL ASP VAL SER
SEQRES 5 A 230 HIS GLU GLU PRO GLU VAL LYS PHE ASN TRP TYR VAL ASP
SEQRES 6 A 230 GLY VAL GLU VAL HIS ASN ALA LYS THR LYS PRO ARG GLU
SEQRES 7 A 230 GLU GLN TYR ASN SER THR TYR ARG VAL VAL SER VAL LEU
SEQRES 8 A 230 THR VAL LEU HIS GLN ASP TRP LEU ASN GLY LYS GLU TYR
SEQRES 9 A 230 LYS CYS LYS VAL SER ASN ASP ALA LEU PRO LYS PRO ILE
SEQRES 10 A 230 GLU GLU THR ILE SER LYS ALA LYS GLY GLN PRO ARG GLU
SEQRES 11 A 230 PRO GLN VAL TYR THR LEU PRO PRO SER ARG CYS GLU LEU
SEQRES 12 A 230 THR LYS ASN GLN VAL SER LEU SER CYS ALA VAL LYS GLY
SEQRES 13 A 230 PHE TYR PRO SER ASP ILE ALA VAL GLU TRP GLU SER ASN
SEQRES 14 A 230 GLY GLN PRO GLU ASN ASN TYR LYS THR THR PRO PRO VAL
SEQRES 15 A 230 LEU ASP SER ASP GLY SER PHE PHE LEU VAL SER LYS LEU
SEQRES 16 A 230 THR VAL ASP LYS SER ARG TRP GLN GLN GLY ASN VAL PHE
SEQRES 17 A 230 SER CYS SER VAL MET HIS GLU ALA LEU HIS ASN HIS TYR
SEQRES 18 A 230 THR GLN LYS SER LEU SER LEU SER PRO
SEQRES 1 B 230 GLU PRO LYS SER SER ASP LYS THR HIS THR CYS PRO PRO
SEQRES 2 B 230 CYS PRO ALA PRO GLU TYR TYR TRP GLY PRO MET VAL PHE
SEQRES 3 B 230 LEU PHE PRO PRO LYS PRO LYS ASP THR LEU MET ILE SER
SEQRES 4 B 230 ARG THR PRO GLU VAL THR CYS VAL VAL VAL ASP VAL SER
SEQRES 5 B 230 ASP GLU ASP PRO GLU VAL LYS PHE ASN TRP TYR VAL ASP
SEQRES 6 B 230 GLY VAL GLU VAL HIS ASN ALA LYS THR LYS PRO ARG GLU
SEQRES 7 B 230 GLU GLN TYR ASN ALA THR TYR ARG VAL VAL SER VAL LEU
SEQRES 8 B 230 THR VAL LEU HIS GLN ASP TRP LEU ASN GLY LYS GLU TYR
SEQRES 9 B 230 LYS CYS LYS VAL SER ASN LYS ASP LEU PRO ALA PRO ILE
SEQRES 10 B 230 GLU LYS THR ILE SER LYS ALA LYS GLY GLN PRO ARG GLU
SEQRES 11 B 230 PRO GLN VAL CYS THR LEU PRO PRO SER ARG ASP GLU LEU
SEQRES 12 B 230 THR LYS ASN GLN VAL SER LEU TRP CYS LEU VAL LYS GLY
SEQRES 13 B 230 PHE TYR PRO SER ASP ILE ALA VAL GLU TRP GLU SER ASN
SEQRES 14 B 230 GLY GLN PRO GLU ASN ASN TYR LYS THR THR PRO PRO VAL
SEQRES 15 B 230 LEU ASP SER ASP GLY SER PHE PHE LEU TYR SER LYS LEU
SEQRES 16 B 230 THR VAL ASP LYS SER ARG TRP GLN GLN GLY ASN VAL PHE
SEQRES 17 B 230 SER CYS SER VAL MET HIS GLU ALA LEU HIS ASN HIS TYR
SEQRES 18 B 230 THR GLN LYS SER LEU SER LEU SER PRO
SEQRES 1 C 197 MET ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU
SEQRES 2 C 197 GLU PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL
SEQRES 3 C 197 THR LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP GLN
SEQRES 4 C 197 SER THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER
SEQRES 5 C 197 GLN ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP
SEQRES 6 C 197 ASP SER GLY GLU TYR ARG CYS GLN THR GLN LEU SER THR
SEQRES 7 C 197 LEU SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP
SEQRES 8 C 197 LEU LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU
SEQRES 9 C 197 ASP PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR
SEQRES 10 C 197 ALA LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY
SEQRES 11 C 197 ARG LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO
SEQRES 12 C 197 LYS ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG
SEQRES 13 C 197 GLY LEU VAL GLY SER LYS ASN VAL SER SER GLU THR VAL
SEQRES 14 C 197 GLN ILE THR ILE THR GLN GLY LEU ALA VAL SER THR ILE
SEQRES 15 C 197 SER SER PHE PHE PRO PRO GLY TYR GLN HIS HIS HIS HIS
SEQRES 16 C 197 HIS HIS
SEQRES 1 D 230 GLU PRO LYS SER SER ASP LYS THR HIS THR CYS PRO PRO
SEQRES 2 D 230 CYS PRO ALA PRO GLU LEU LEU GLY GLY PRO SER VAL PHE
SEQRES 3 D 230 LEU PHE PRO PRO LYS PRO LYS ASP THR LEU MET ILE SER
SEQRES 4 D 230 ARG THR PRO GLU VAL THR CYS VAL VAL VAL ASP VAL SER
SEQRES 5 D 230 HIS GLU GLU PRO GLU VAL LYS PHE ASN TRP TYR VAL ASP
SEQRES 6 D 230 GLY VAL GLU VAL HIS ASN ALA LYS THR LYS PRO ARG GLU
SEQRES 7 D 230 GLU GLN TYR ASN SER THR TYR ARG VAL VAL SER VAL LEU
SEQRES 8 D 230 THR VAL LEU HIS GLN ASP TRP LEU ASN GLY LYS GLU TYR
SEQRES 9 D 230 LYS CYS LYS VAL SER ASN ASP ALA LEU PRO LYS PRO ILE
SEQRES 10 D 230 GLU GLU THR ILE SER LYS ALA LYS GLY GLN PRO ARG GLU
SEQRES 11 D 230 PRO GLN VAL TYR THR LEU PRO PRO SER ARG CYS GLU LEU
SEQRES 12 D 230 THR LYS ASN GLN VAL SER LEU SER CYS ALA VAL LYS GLY
SEQRES 13 D 230 PHE TYR PRO SER ASP ILE ALA VAL GLU TRP GLU SER ASN
SEQRES 14 D 230 GLY GLN PRO GLU ASN ASN TYR LYS THR THR PRO PRO VAL
SEQRES 15 D 230 LEU ASP SER ASP GLY SER PHE PHE LEU VAL SER LYS LEU
SEQRES 16 D 230 THR VAL ASP LYS SER ARG TRP GLN GLN GLY ASN VAL PHE
SEQRES 17 D 230 SER CYS SER VAL MET HIS GLU ALA LEU HIS ASN HIS TYR
SEQRES 18 D 230 THR GLN LYS SER LEU SER LEU SER PRO
SEQRES 1 E 230 GLU PRO LYS SER SER ASP LYS THR HIS THR CYS PRO PRO
SEQRES 2 E 230 CYS PRO ALA PRO GLU TYR TYR TRP GLY PRO MET VAL PHE
SEQRES 3 E 230 LEU PHE PRO PRO LYS PRO LYS ASP THR LEU MET ILE SER
SEQRES 4 E 230 ARG THR PRO GLU VAL THR CYS VAL VAL VAL ASP VAL SER
SEQRES 5 E 230 ASP GLU ASP PRO GLU VAL LYS PHE ASN TRP TYR VAL ASP
SEQRES 6 E 230 GLY VAL GLU VAL HIS ASN ALA LYS THR LYS PRO ARG GLU
SEQRES 7 E 230 GLU GLN TYR ASN ALA THR TYR ARG VAL VAL SER VAL LEU
SEQRES 8 E 230 THR VAL LEU HIS GLN ASP TRP LEU ASN GLY LYS GLU TYR
SEQRES 9 E 230 LYS CYS LYS VAL SER ASN LYS ASP LEU PRO ALA PRO ILE
SEQRES 10 E 230 GLU LYS THR ILE SER LYS ALA LYS GLY GLN PRO ARG GLU
SEQRES 11 E 230 PRO GLN VAL CYS THR LEU PRO PRO SER ARG ASP GLU LEU
SEQRES 12 E 230 THR LYS ASN GLN VAL SER LEU TRP CYS LEU VAL LYS GLY
SEQRES 13 E 230 PHE TYR PRO SER ASP ILE ALA VAL GLU TRP GLU SER ASN
SEQRES 14 E 230 GLY GLN PRO GLU ASN ASN TYR LYS THR THR PRO PRO VAL
SEQRES 15 E 230 LEU ASP SER ASP GLY SER PHE PHE LEU TYR SER LYS LEU
SEQRES 16 E 230 THR VAL ASP LYS SER ARG TRP GLN GLN GLY ASN VAL PHE
SEQRES 17 E 230 SER CYS SER VAL MET HIS GLU ALA LEU HIS ASN HIS TYR
SEQRES 18 E 230 THR GLN LYS SER LEU SER LEU SER PRO
SEQRES 1 F 197 MET ARG THR GLU ASP LEU PRO LYS ALA VAL VAL PHE LEU
SEQRES 2 F 197 GLU PRO GLN TRP TYR ARG VAL LEU GLU LYS ASP SER VAL
SEQRES 3 F 197 THR LEU LYS CYS GLN GLY ALA TYR SER PRO GLU ASP GLN
SEQRES 4 F 197 SER THR GLN TRP PHE HIS ASN GLU SER LEU ILE SER SER
SEQRES 5 F 197 GLN ALA SER SER TYR PHE ILE ASP ALA ALA THR VAL ASP
SEQRES 6 F 197 ASP SER GLY GLU TYR ARG CYS GLN THR GLN LEU SER THR
SEQRES 7 F 197 LEU SER ASP PRO VAL GLN LEU GLU VAL HIS ILE GLY TRP
SEQRES 8 F 197 LEU LEU LEU GLN ALA PRO ARG TRP VAL PHE LYS GLU GLU
SEQRES 9 F 197 ASP PRO ILE HIS LEU ARG CYS HIS SER TRP LYS ASN THR
SEQRES 10 F 197 ALA LEU HIS LYS VAL THR TYR LEU GLN ASN GLY LYS GLY
SEQRES 11 F 197 ARG LYS TYR PHE HIS HIS ASN SER ASP PHE TYR ILE PRO
SEQRES 12 F 197 LYS ALA THR LEU LYS ASP SER GLY SER TYR PHE CYS ARG
SEQRES 13 F 197 GLY LEU VAL GLY SER LYS ASN VAL SER SER GLU THR VAL
SEQRES 14 F 197 GLN ILE THR ILE THR GLN GLY LEU ALA VAL SER THR ILE
SEQRES 15 F 197 SER SER PHE PHE PRO PRO GLY TYR GLN HIS HIS HIS HIS
SEQRES 16 F 197 HIS HIS
MODRES 3WN5 ASN D 297 ASN GLYCOSYLATION SITE
MODRES 3WN5 ASN C 159 ASN GLYCOSYLATION SITE
MODRES 3WN5 ASN B 297 ASN GLYCOSYLATION SITE
MODRES 3WN5 ASN C 42 ASN GLYCOSYLATION SITE
MODRES 3WN5 ASN A 297 ASN GLYCOSYLATION SITE
MODRES 3WN5 ASN F 42 ASN GLYCOSYLATION SITE
MODRES 3WN5 ASN E 297 ASN GLYCOSYLATION SITE
MODRES 3WN5 ASN F 159 ASN GLYCOSYLATION SITE
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET NAG G 5 14
HET GAL G 6 11
HET MAN G 7 11
HET NAG G 8 14
HET FUL G 9 10
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET MAN H 4 11
HET NAG H 5 14
HET GAL H 6 11
HET MAN H 7 11
HET NAG H 8 14
HET FUL H 9 10
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET MAN I 4 11
HET MAN I 5 11
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET BMA K 3 11
HET MAN K 4 11
HET NAG K 5 14
HET MAN K 6 11
HET NAG K 7 14
HET FUL K 8 10
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 GAL L 6 11
HET MAN L 7 11
HET NAG L 8 14
HET FUL L 9 10
HET NAG M 1 14
HET NAG M 2 14
HET IOD A1010 1
HET IOD A1011 1
HET IOD B1010 1
HET IOD B1011 1
HET IOD B1012 1
HET IOD C 208 1
HET IOD C 209 1
HET IOD D1009 1
HET IOD E1010 1
HET IOD E1011 1
HET IOD E1012 1
HET IOD E1013 1
HET NAG F 201 14
HET IOD F 204 1
HET IOD F 205 1
HET IOD F 206 1
HET IOD F 207 1
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 IOD IODIDE ION
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 7 NAG 23(C8 H15 N O6)
FORMUL 7 BMA 5(C6 H12 O6)
FORMUL 7 MAN 10(C6 H12 O6)
FORMUL 7 GAL 3(C6 H12 O6)
FORMUL 7 FUL 4(C6 H12 O5)
FORMUL 14 IOD 16(I 1-)
FORMUL 31 HOH *41(H2 O)
HELIX 1 1 LYS A 246 MET A 252 1 7
HELIX 2 2 LEU A 309 ASN A 315 1 7
HELIX 3 3 SER A 354 LEU A 358 5 5
HELIX 4 4 LYS A 414 GLN A 419 1 6
HELIX 5 5 LEU A 432 TYR A 436 5 5
HELIX 6 6 LYS B 246 MET B 252 1 7
HELIX 7 7 LEU B 309 ASN B 315 1 7
HELIX 8 8 SER B 354 THR B 359 1 6
HELIX 9 9 LYS B 414 GLN B 419 1 6
HELIX 10 10 LEU B 432 ASN B 434 5 3
HELIX 11 11 THR C 59 SER C 63 5 5
HELIX 12 12 LYS C 111 THR C 113 5 3
HELIX 13 13 THR C 142 SER C 146 5 5
HELIX 14 14 LEU D 309 GLY D 316 1 8
HELIX 15 15 SER D 354 THR D 359 5 6
HELIX 16 16 LYS D 414 GLN D 419 1 6
HELIX 17 17 LEU D 432 ASN D 434 5 3
HELIX 18 18 LYS E 246 MET E 252 1 7
HELIX 19 19 LEU E 309 ASN E 315 1 7
HELIX 20 20 LYS E 414 GLN E 418 1 5
HELIX 21 21 LEU E 432 TYR E 436 5 5
HELIX 22 22 THR F 59 SER F 63 5 5
HELIX 23 23 LYS F 111 THR F 113 5 3
HELIX 24 24 THR F 142 SER F 146 5 5
SHEET 1 A 4 SER A 239 PHE A 243 0
SHEET 2 A 4 GLU A 258 VAL A 266 -1 O THR A 260 N PHE A 243
SHEET 3 A 4 TYR A 300 THR A 307 -1 O SER A 304 N CYS A 261
SHEET 4 A 4 LYS A 288 THR A 289 -1 N LYS A 288 O VAL A 305
SHEET 1 B 4 SER A 239 PHE A 243 0
SHEET 2 B 4 GLU A 258 VAL A 266 -1 O THR A 260 N PHE A 243
SHEET 3 B 4 TYR A 300 THR A 307 -1 O SER A 304 N CYS A 261
SHEET 4 B 4 GLU A 293 GLU A 294 -1 N GLU A 293 O ARG A 301
SHEET 1 C 4 VAL A 282 VAL A 284 0
SHEET 2 C 4 LYS A 274 VAL A 279 -1 N VAL A 279 O VAL A 282
SHEET 3 C 4 TYR A 319 SER A 324 -1 O LYS A 322 N ASN A 276
SHEET 4 C 4 ILE A 332 ILE A 336 -1 O ILE A 332 N VAL A 323
SHEET 1 D 4 GLN A 347 LEU A 351 0
SHEET 2 D 4 GLN A 362 PHE A 372 -1 O LYS A 370 N GLN A 347
SHEET 3 D 4 PHE A 404 ASP A 413 -1 O LEU A 410 N LEU A 365
SHEET 4 D 4 TYR A 391 THR A 393 -1 N LYS A 392 O LYS A 409
SHEET 1 E 4 GLN A 347 LEU A 351 0
SHEET 2 E 4 GLN A 362 PHE A 372 -1 O LYS A 370 N GLN A 347
SHEET 3 E 4 PHE A 404 ASP A 413 -1 O LEU A 410 N LEU A 365
SHEET 4 E 4 VAL A 397 LEU A 398 -1 N VAL A 397 O PHE A 405
SHEET 1 F 4 GLN A 386 PRO A 387 0
SHEET 2 F 4 ALA A 378 SER A 383 -1 N SER A 383 O GLN A 386
SHEET 3 F 4 PHE A 423 MET A 428 -1 O SER A 424 N GLU A 382
SHEET 4 F 4 THR A 437 LEU A 441 -1 O LYS A 439 N CYS A 425
SHEET 1 G 4 MET B 239 PHE B 243 0
SHEET 2 G 4 GLU B 258 VAL B 266 -1 O THR B 260 N PHE B 243
SHEET 3 G 4 TYR B 300 THR B 307 -1 O SER B 304 N CYS B 261
SHEET 4 G 4 LYS B 288 THR B 289 -1 N LYS B 288 O VAL B 305
SHEET 1 H 4 MET B 239 PHE B 243 0
SHEET 2 H 4 GLU B 258 VAL B 266 -1 O THR B 260 N PHE B 243
SHEET 3 H 4 TYR B 300 THR B 307 -1 O SER B 304 N CYS B 261
SHEET 4 H 4 GLU B 293 GLU B 294 -1 N GLU B 293 O ARG B 301
SHEET 1 I 4 VAL B 282 VAL B 284 0
SHEET 2 I 4 LYS B 274 VAL B 279 -1 N VAL B 279 O VAL B 282
SHEET 3 I 4 TYR B 319 SER B 324 -1 O LYS B 322 N ASN B 276
SHEET 4 I 4 ILE B 332 ILE B 336 -1 O ILE B 332 N VAL B 323
SHEET 1 J 4 GLN B 347 LEU B 351 0
SHEET 2 J 4 GLN B 362 PHE B 372 -1 O LEU B 368 N CYS B 349
SHEET 3 J 4 PHE B 404 ASP B 413 -1 O PHE B 404 N PHE B 372
SHEET 4 J 4 TYR B 391 THR B 393 -1 N LYS B 392 O LYS B 409
SHEET 1 K 4 GLN B 347 LEU B 351 0
SHEET 2 K 4 GLN B 362 PHE B 372 -1 O LEU B 368 N CYS B 349
SHEET 3 K 4 PHE B 404 ASP B 413 -1 O PHE B 404 N PHE B 372
SHEET 4 K 4 VAL B 397 LEU B 398 -1 N VAL B 397 O PHE B 405
SHEET 1 L 4 GLN B 386 GLU B 388 0
SHEET 2 L 4 ALA B 378 SER B 383 -1 N TRP B 381 O GLU B 388
SHEET 3 L 4 PHE B 423 MET B 428 -1 O SER B 426 N GLU B 380
SHEET 4 L 4 TYR B 436 LEU B 441 -1 O THR B 437 N VAL B 427
SHEET 1 M 3 VAL C 6 GLU C 10 0
SHEET 2 M 3 VAL C 22 GLN C 27 -1 O THR C 23 N GLU C 10
SHEET 3 M 3 SER C 52 ILE C 55 -1 O ILE C 55 N VAL C 22
SHEET 1 N 5 ARG C 15 LEU C 17 0
SHEET 2 N 5 VAL C 79 HIS C 84 1 O HIS C 84 N VAL C 16
SHEET 3 N 5 GLY C 64 THR C 70 -1 N GLY C 64 O LEU C 81
SHEET 4 N 5 THR C 37 HIS C 41 -1 N PHE C 40 O ARG C 67
SHEET 5 N 5 SER C 44 ILE C 46 -1 O ILE C 46 N TRP C 39
SHEET 1 O 3 LEU C 88 GLN C 91 0
SHEET 2 O 3 ILE C 103 SER C 109 -1 O HIS C 108 N LEU C 89
SHEET 3 O 3 PHE C 136 ILE C 138 -1 O PHE C 136 N LEU C 105
SHEET 1 P 5 VAL C 96 LYS C 98 0
SHEET 2 P 5 VAL C 165 THR C 170 1 O THR C 168 N PHE C 97
SHEET 3 P 5 GLY C 147 VAL C 155 -1 N GLY C 147 O ILE C 167
SHEET 4 P 5 HIS C 116 GLN C 122 -1 N HIS C 116 O LEU C 154
SHEET 5 P 5 LYS C 125 HIS C 132 -1 O ARG C 127 N TYR C 120
SHEET 1 Q 4 VAL C 96 LYS C 98 0
SHEET 2 Q 4 VAL C 165 THR C 170 1 O THR C 168 N PHE C 97
SHEET 3 Q 4 GLY C 147 VAL C 155 -1 N GLY C 147 O ILE C 167
SHEET 4 Q 4 LYS C 158 SER C 161 -1 O LYS C 158 N VAL C 155
SHEET 1 R 4 SER D 239 PHE D 243 0
SHEET 2 R 4 GLU D 258 VAL D 266 -1 O VAL D 262 N PHE D 241
SHEET 3 R 4 TYR D 300 THR D 307 -1 O SER D 304 N CYS D 261
SHEET 4 R 4 LYS D 288 THR D 289 -1 N LYS D 288 O VAL D 305
SHEET 1 S 4 SER D 239 PHE D 243 0
SHEET 2 S 4 GLU D 258 VAL D 266 -1 O VAL D 262 N PHE D 241
SHEET 3 S 4 TYR D 300 THR D 307 -1 O SER D 304 N CYS D 261
SHEET 4 S 4 GLU D 293 GLU D 294 -1 N GLU D 293 O ARG D 301
SHEET 1 T 4 VAL D 282 VAL D 284 0
SHEET 2 T 4 LYS D 274 VAL D 279 -1 N VAL D 279 O VAL D 282
SHEET 3 T 4 TYR D 319 SER D 324 -1 O LYS D 322 N ASN D 276
SHEET 4 T 4 ILE D 332 ILE D 336 -1 O ILE D 332 N VAL D 323
SHEET 1 U 4 GLN D 347 LEU D 351 0
SHEET 2 U 4 GLN D 362 PHE D 372 -1 O ALA D 368 N TYR D 349
SHEET 3 U 4 PHE D 404 ASP D 413 -1 O LEU D 410 N LEU D 365
SHEET 4 U 4 TYR D 391 THR D 393 -1 N LYS D 392 O LYS D 409
SHEET 1 V 4 GLN D 347 LEU D 351 0
SHEET 2 V 4 GLN D 362 PHE D 372 -1 O ALA D 368 N TYR D 349
SHEET 3 V 4 PHE D 404 ASP D 413 -1 O LEU D 410 N LEU D 365
SHEET 4 V 4 VAL D 397 LEU D 398 -1 N VAL D 397 O PHE D 405
SHEET 1 W 4 GLN D 386 PRO D 387 0
SHEET 2 W 4 ALA D 378 SER D 383 -1 N SER D 383 O GLN D 386
SHEET 3 W 4 PHE D 423 MET D 428 -1 O SER D 424 N GLU D 382
SHEET 4 W 4 TYR D 436 LEU D 441 -1 O LYS D 439 N CYS D 425
SHEET 1 X 4 MET E 239 PHE E 243 0
SHEET 2 X 4 GLU E 258 VAL E 266 -1 O VAL E 262 N PHE E 241
SHEET 3 X 4 TYR E 300 THR E 307 -1 O LEU E 306 N VAL E 259
SHEET 4 X 4 ALA E 287 THR E 289 -1 N LYS E 288 O VAL E 305
SHEET 1 Y 4 MET E 239 PHE E 243 0
SHEET 2 Y 4 GLU E 258 VAL E 266 -1 O VAL E 262 N PHE E 241
SHEET 3 Y 4 TYR E 300 THR E 307 -1 O LEU E 306 N VAL E 259
SHEET 4 Y 4 GLU E 293 GLU E 294 -1 N GLU E 293 O ARG E 301
SHEET 1 Z 4 VAL E 282 VAL E 284 0
SHEET 2 Z 4 LYS E 274 VAL E 279 -1 N VAL E 279 O VAL E 282
SHEET 3 Z 4 TYR E 319 SER E 324 -1 O SER E 324 N LYS E 274
SHEET 4 Z 4 ILE E 332 ILE E 336 -1 O ILE E 336 N TYR E 319
SHEET 1 AA 4 GLN E 347 LEU E 351 0
SHEET 2 AA 4 GLN E 362 PHE E 372 -1 O LEU E 368 N CYS E 349
SHEET 3 AA 4 PHE E 404 ASP E 413 -1 O LEU E 410 N LEU E 365
SHEET 4 AA 4 TYR E 391 THR E 393 -1 N LYS E 392 O LYS E 409
SHEET 1 AB 4 GLN E 347 LEU E 351 0
SHEET 2 AB 4 GLN E 362 PHE E 372 -1 O LEU E 368 N CYS E 349
SHEET 3 AB 4 PHE E 404 ASP E 413 -1 O LEU E 410 N LEU E 365
SHEET 4 AB 4 VAL E 397 LEU E 398 -1 N VAL E 397 O PHE E 405
SHEET 1 AC 4 GLN E 386 PRO E 387 0
SHEET 2 AC 4 ALA E 378 SER E 383 -1 N SER E 383 O GLN E 386
SHEET 3 AC 4 PHE E 423 MET E 428 -1 O MET E 428 N ALA E 378
SHEET 4 AC 4 THR E 437 LEU E 441 -1 O LYS E 439 N CYS E 425
SHEET 1 AD 3 VAL F 6 GLU F 10 0
SHEET 2 AD 3 VAL F 22 GLN F 27 -1 O LYS F 25 N PHE F 8
SHEET 3 AD 3 SER F 52 ILE F 55 -1 O ILE F 55 N VAL F 22
SHEET 1 AE 5 ARG F 15 LEU F 17 0
SHEET 2 AE 5 VAL F 79 HIS F 84 1 O HIS F 84 N VAL F 16
SHEET 3 AE 5 GLY F 64 THR F 70 -1 N GLY F 64 O LEU F 81
SHEET 4 AE 5 THR F 37 HIS F 41 -1 N PHE F 40 O ARG F 67
SHEET 5 AE 5 SER F 44 LEU F 45 -1 O SER F 44 N HIS F 41
SHEET 1 AF 3 LEU F 88 GLN F 91 0
SHEET 2 AF 3 ILE F 103 SER F 109 -1 O HIS F 108 N LEU F 89
SHEET 3 AF 3 PHE F 136 ILE F 138 -1 O PHE F 136 N LEU F 105
SHEET 1 AG 5 VAL F 96 LYS F 98 0
SHEET 2 AG 5 VAL F 165 THR F 170 1 O THR F 170 N PHE F 97
SHEET 3 AG 5 GLY F 147 VAL F 155 -1 N GLY F 147 O ILE F 167
SHEET 4 AG 5 HIS F 116 GLN F 122 -1 N HIS F 116 O LEU F 154
SHEET 5 AG 5 LYS F 125 HIS F 132 -1 O ARG F 127 N TYR F 120
SHEET 1 AH 4 VAL F 96 LYS F 98 0
SHEET 2 AH 4 VAL F 165 THR F 170 1 O THR F 170 N PHE F 97
SHEET 3 AH 4 GLY F 147 VAL F 155 -1 N GLY F 147 O ILE F 167
SHEET 4 AH 4 LYS F 158 SER F 161 -1 O LYS F 158 N VAL F 155
SSBOND 1 CYS A 261 CYS A 321 1555 1555 2.04
SSBOND 2 CYS A 356 CYS B 349 1555 1555 2.03
SSBOND 3 CYS A 367 CYS A 425 1555 1555 2.03
SSBOND 4 CYS B 261 CYS B 321 1555 1555 2.03
SSBOND 5 CYS B 367 CYS B 425 1555 1555 2.04
SSBOND 6 CYS C 26 CYS C 68 1555 1555 2.04
SSBOND 7 CYS C 107 CYS C 151 1555 1555 2.03
SSBOND 8 CYS D 261 CYS D 321 1555 1555 2.03
SSBOND 9 CYS D 356 CYS E 349 1555 1555 2.03
SSBOND 10 CYS D 367 CYS D 425 1555 1555 2.03
SSBOND 11 CYS E 261 CYS E 321 1555 1555 2.03
SSBOND 12 CYS E 367 CYS E 425 1555 1555 2.03
SSBOND 13 CYS F 26 CYS F 68 1555 1555 2.04
SSBOND 14 CYS F 107 CYS F 151 1555 1555 2.05
LINK ND2 ASN A 297 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN B 297 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN C 42 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN C 159 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN D 297 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN E 297 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN F 42 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN F 159 C1 NAG F 201 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O6 NAG G 1 C1 FUL G 9 1555 1555 1.44
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44
LINK O6 BMA G 3 C1 MAN G 4 1555 1555 1.44
LINK O3 BMA G 3 C1 MAN G 7 1555 1555 1.45
LINK O2 MAN G 4 C1 NAG G 5 1555 1555 1.44
LINK O4 NAG G 5 C1 GAL G 6 1555 1555 1.45
LINK O2 MAN G 7 C1 NAG G 8 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O6 NAG H 1 C1 FUL H 9 1555 1555 1.45
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44
LINK O6 BMA H 3 C1 MAN H 4 1555 1555 1.44
LINK O3 BMA H 3 C1 MAN H 7 1555 1555 1.46
LINK O2 MAN H 4 C1 NAG H 5 1555 1555 1.44
LINK O4 NAG H 5 C1 GAL H 6 1555 1555 1.45
LINK O2 MAN H 7 C1 NAG H 8 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.44
LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45
LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.45
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O6 NAG K 1 C1 FUL K 8 1555 1555 1.45
LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44
LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.45
LINK O6 BMA K 3 C1 MAN K 6 1555 1555 1.44
LINK O2 MAN K 4 C1 NAG K 5 1555 1555 1.44
LINK O2 MAN K 6 C1 NAG K 7 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O6 NAG L 1 C1 FUL L 9 1555 1555 1.45
LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.44
LINK O6 BMA L 3 C1 MAN L 4 1555 1555 1.44
LINK O3 BMA L 3 C1 MAN L 7 1555 1555 1.45
LINK O2 MAN L 4 C1 NAG L 5 1555 1555 1.44
LINK O4 NAG L 5 C1 GAL L 6 1555 1555 1.45
LINK O2 MAN L 7 C1 NAG L 8 1555 1555 1.45
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45
CISPEP 1 TYR A 373 PRO A 374 0 -1.58
CISPEP 2 TYR B 373 PRO B 374 0 0.43
CISPEP 3 GLU C 10 PRO C 11 0 -5.15
CISPEP 4 TYR D 373 PRO D 374 0 -3.17
CISPEP 5 TYR E 373 PRO E 374 0 -1.43
CISPEP 6 GLU F 10 PRO F 11 0 -1.63
CRYST1 75.030 72.490 163.480 90.00 91.15 90.00 P 1 21 1 4
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 0.013328 0.000000 0.000268 0.00000
SCALE2 0.000000 0.013795 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006118 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
