HEADER IMMUNE SYSTEM 11-DEC-14 4X98
TITLE IMMUNOGLOBULIN FC HETERODIMER VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IG GAMMA-1 CHAIN C REGION;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 108-327;
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;
COMPND 10 FRAGMENT: UNP RESIDUES 121-327;
COMPND 11 ENGINEERED: YES;
COMPND 12 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 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: IGHG1;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 18 EXPRESSION_SYSTEM_ORGAN: KIDNEY
KEYWDS BISPECIFIC ANTIBODY, IMMUNOGLOBULIN FC HETERODIMER, CH3 DOMAIN
KEYWDS 2 INTERFACE, ASYMMETRIC DISULFIDE BONDS, THERMAL STABILITY, FC
KEYWDS 3 ENGINEERING, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.SEOK,H.J.CHOI,Y.J.KIM,M.D.SEO,Y.S.KIM
REVDAT 3 08-NOV-23 4X98 1 HETSYN LINK
REVDAT 2 29-JUL-20 4X98 1 COMPND SOURCE JRNL REMARK
REVDAT 2 2 1 HETNAM LINK SITE ATOM
REVDAT 1 03-JUN-15 4X98 0
JRNL AUTH H.J.CHOI,S.H.SEOK,Y.J.KIM,M.D.SEO,Y.S.KIM
JRNL TITL CRYSTAL STRUCTURES OF IMMUNOGLOBULIN FC HETERODIMERS REVEAL
JRNL TITL 2 THE MOLECULAR BASIS FOR HETERODIMER FORMATION.
JRNL REF MOL.IMMUNOL. V. 65 377 2015
JRNL REFN ISSN 0161-5890
JRNL PMID 25743157
JRNL DOI 10.1016/J.MOLIMM.2015.02.017
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 26412
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.560
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 36.8441 - 6.0151 0.99 1904 156 0.2160 0.2524
REMARK 3 2 6.0151 - 4.7776 1.00 1794 147 0.1923 0.2309
REMARK 3 3 4.7776 - 4.1747 1.00 1768 143 0.1782 0.2332
REMARK 3 4 4.1747 - 3.7934 1.00 1757 144 0.2049 0.2566
REMARK 3 5 3.7934 - 3.5217 1.00 1741 143 0.2229 0.2779
REMARK 3 6 3.5217 - 3.3142 1.00 1727 142 0.2348 0.2795
REMARK 3 7 3.3142 - 3.1484 1.00 1730 142 0.2622 0.2946
REMARK 3 8 3.1484 - 3.0114 1.00 1732 141 0.2785 0.3377
REMARK 3 9 3.0114 - 2.8955 1.00 1717 141 0.2821 0.3041
REMARK 3 10 2.8955 - 2.7956 1.00 1719 140 0.2974 0.3671
REMARK 3 11 2.7956 - 2.7082 1.00 1723 141 0.2886 0.3496
REMARK 3 12 2.7082 - 2.6308 1.00 1702 139 0.2914 0.3960
REMARK 3 13 2.6308 - 2.5616 1.00 1709 141 0.2964 0.3237
REMARK 3 14 2.5616 - 2.4991 0.99 1691 138 0.3058 0.3726
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 3566
REMARK 3 ANGLE : 1.429 4873
REMARK 3 CHIRALITY : 0.055 585
REMARK 3 PLANARITY : 0.008 594
REMARK 3 DIHEDRAL : 15.575 1355
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 4X98 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205273.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26500
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.499
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 16.20
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 59.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
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 : NULL
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: 3AVE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M NACL, 0.1M SODIUM ACETATE, PH 4.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.32800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 72.65600
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 54.49200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 90.82000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 18.16400
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.32800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 72.65600
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 90.82000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 54.49200
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 18.16400
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 647 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR 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 GLY A 236
REMARK 465 SER B 298
REMARK 465 THR B 299
REMARK 465 TYR B 300
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 TYR B 278 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 294 CG CD OE1 OE2
REMARK 470 GLN B 295 CG CD OE1 NE2
REMARK 470 TYR B 296 CG CD1 CD2 CE1 CE2 CZ OH
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 O6 MAN C 4 N2 NAG C 5 2.00
REMARK 500 O4 NAG C 1 O5 NAG C 2 2.14
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 390 60.82 -110.18
REMARK 500 PRO B 271 23.26 -77.31
REMARK 500 PRO B 291 97.69 -66.76
REMARK 500 ASN B 390 59.95 -98.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X99 RELATED DB: PDB
DBREF 4X98 A 225 444 UNP P01857 IGHG1_HUMAN 108 327
DBREF 4X98 B 238 444 UNP P01857 IGHG1_HUMAN 121 327
SEQADV 4X98 GLU A 360 UNP P01857 LYS 243 ENGINEERED MUTATION
SEQADV 4X98 TRP A 409 UNP P01857 LYS 292 ENGINEERED MUTATION
SEQADV 4X98 ARG B 347 UNP P01857 GLN 230 ENGINEERED MUTATION
SEQADV 4X98 VAL B 399 UNP P01857 ASP 282 ENGINEERED MUTATION
SEQADV 4X98 THR B 405 UNP P01857 PHE 288 ENGINEERED MUTATION
SEQRES 1 A 220 THR CYS PRO PRO CYS PRO ALA PRO GLU LEU LEU GLY GLY
SEQRES 2 A 220 PRO SER VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP THR
SEQRES 3 A 220 LEU MET ILE SER ARG THR PRO GLU VAL THR CYS VAL VAL
SEQRES 4 A 220 VAL ASP VAL SER HIS GLU ASP PRO GLU VAL LYS PHE ASN
SEQRES 5 A 220 TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA LYS THR
SEQRES 6 A 220 LYS PRO ARG GLU GLU GLN TYR ASN SER THR TYR ARG VAL
SEQRES 7 A 220 VAL SER VAL LEU THR VAL LEU HIS GLN ASP TRP LEU ASN
SEQRES 8 A 220 GLY LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA LEU
SEQRES 9 A 220 PRO ALA PRO ILE GLU LYS THR ILE SER LYS ALA LYS GLY
SEQRES 10 A 220 GLN PRO ARG GLU PRO GLN VAL TYR THR LEU PRO PRO SER
SEQRES 11 A 220 ARG ASP GLU LEU THR GLU ASN GLN VAL SER LEU THR CYS
SEQRES 12 A 220 LEU VAL LYS GLY PHE TYR PRO SER ASP ILE ALA VAL GLU
SEQRES 13 A 220 TRP GLU SER ASN GLY GLN PRO GLU ASN ASN TYR LYS THR
SEQRES 14 A 220 THR PRO PRO VAL LEU ASP SER ASP GLY SER PHE PHE LEU
SEQRES 15 A 220 TYR SER TRP LEU THR VAL ASP LYS SER ARG TRP GLN GLN
SEQRES 16 A 220 GLY ASN VAL PHE SER CYS SER VAL MET HIS GLU ALA LEU
SEQRES 17 A 220 HIS ASN HIS TYR THR GLN LYS SER LEU SER LEU SER
SEQRES 1 B 207 PRO SER VAL PHE LEU PHE PRO PRO LYS PRO LYS ASP THR
SEQRES 2 B 207 LEU MET ILE SER ARG THR PRO GLU VAL THR CYS VAL VAL
SEQRES 3 B 207 VAL ASP VAL SER HIS GLU ASP PRO GLU VAL LYS PHE ASN
SEQRES 4 B 207 TRP TYR VAL ASP GLY VAL GLU VAL HIS ASN ALA LYS THR
SEQRES 5 B 207 LYS PRO ARG GLU GLU GLN TYR ASN SER THR TYR ARG VAL
SEQRES 6 B 207 VAL SER VAL LEU THR VAL LEU HIS GLN ASP TRP LEU ASN
SEQRES 7 B 207 GLY LYS GLU TYR LYS CYS LYS VAL SER ASN LYS ALA LEU
SEQRES 8 B 207 PRO ALA PRO ILE GLU LYS THR ILE SER LYS ALA LYS GLY
SEQRES 9 B 207 GLN PRO ARG GLU PRO ARG VAL TYR THR LEU PRO PRO SER
SEQRES 10 B 207 ARG ASP GLU LEU THR LYS ASN GLN VAL SER LEU THR CYS
SEQRES 11 B 207 LEU VAL LYS GLY PHE TYR PRO SER ASP ILE ALA VAL GLU
SEQRES 12 B 207 TRP GLU SER ASN GLY GLN PRO GLU ASN ASN TYR LYS THR
SEQRES 13 B 207 THR PRO PRO VAL LEU VAL SER ASP GLY SER PHE THR LEU
SEQRES 14 B 207 TYR SER LYS LEU THR VAL ASP LYS SER ARG TRP GLN GLN
SEQRES 15 B 207 GLY ASN VAL PHE SER CYS SER VAL MET HIS GLU ALA LEU
SEQRES 16 B 207 HIS ASN HIS TYR THR GLN LYS SER LEU SER LEU SER
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET NAG C 5 14
HET MAN C 6 11
HET NAG C 7 14
HET FUC C 8 10
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 MAN D 6 11
HET NAG D 7 14
HET FUC D 8 10
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 3 BMA 2(C6 H12 O6)
FORMUL 3 MAN 4(C6 H12 O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 HOH *71(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 SER A 354 LEU A 358 5 5
HELIX 4 AA4 LYS A 414 GLN A 419 1 6
HELIX 5 AA5 LEU A 432 ASN A 434 5 3
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 GLY B 420 1 7
HELIX 10 AB1 LEU B 432 TYR B 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 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 THR A 289 -1 N LYS A 288 O VAL A 305
SHEET 1 AA2 4 SER A 239 PHE A 243 0
SHEET 2 AA2 4 GLU A 258 VAL A 266 -1 O VAL A 262 N PHE A 241
SHEET 3 AA2 4 TYR A 300 THR A 307 -1 O SER A 304 N CYS A 261
SHEET 4 AA2 4 GLU A 293 GLU A 294 -1 N GLU A 293 O ARG A 301
SHEET 1 AA3 4 VAL A 282 VAL A 284 0
SHEET 2 AA3 4 LYS A 274 VAL A 279 -1 N VAL A 279 O VAL A 282
SHEET 3 AA3 4 TYR A 319 SER A 324 -1 O LYS A 322 N ASN A 276
SHEET 4 AA3 4 ILE A 332 ILE A 336 -1 O ILE A 336 N TYR A 319
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 TYR A 391 THR A 393 -1 N LYS A 392 O TRP A 409
SHEET 1 AA5 4 GLN A 347 LEU A 351 0
SHEET 2 AA5 4 GLN A 362 PHE A 372 -1 O THR A 366 N LEU A 351
SHEET 3 AA5 4 PHE A 404 ASP A 413 -1 O LEU A 410 N LEU A 365
SHEET 4 AA5 4 VAL A 397 LEU A 398 -1 N VAL A 397 O PHE A 405
SHEET 1 AA6 4 GLN A 386 GLU A 388 0
SHEET 2 AA6 4 ALA A 378 SER A 383 -1 N SER A 383 O GLN A 386
SHEET 3 AA6 4 VAL A 422 MET A 428 -1 O SER A 426 N GLU A 380
SHEET 4 AA6 4 TYR A 436 SER A 442 -1 O THR A 437 N VAL A 427
SHEET 1 AA7 4 VAL B 240 PHE B 243 0
SHEET 2 AA7 4 GLU B 258 VAL B 263 -1 O VAL B 262 N PHE B 241
SHEET 3 AA7 4 VAL B 302 THR B 307 -1 O SER B 304 N CYS B 261
SHEET 4 AA7 4 LYS B 288 THR B 289 -1 N LYS B 288 O VAL B 305
SHEET 1 AA8 4 VAL B 282 VAL B 284 0
SHEET 2 AA8 4 LYS B 274 VAL B 279 -1 N VAL B 279 O VAL B 282
SHEET 3 AA8 4 TYR B 319 SER B 324 -1 O LYS B 320 N TYR B 278
SHEET 4 AA8 4 ILE B 332 ILE B 336 -1 O ILE B 332 N VAL B 323
SHEET 1 AA9 4 ARG 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 VAL B 412 N VAL B 363
SHEET 4 AA9 4 TYR B 391 THR B 393 -1 N LYS B 392 O LYS B 409
SHEET 1 AB1 4 ARG B 347 LEU B 351 0
SHEET 2 AB1 4 GLN B 362 PHE B 372 -1 O THR B 366 N LEU B 351
SHEET 3 AB1 4 PHE B 404 ASP B 413 -1 O VAL B 412 N VAL B 363
SHEET 4 AB1 4 VAL B 397 LEU B 398 -1 N VAL B 397 O THR B 405
SHEET 1 AB2 4 GLN B 386 GLU B 388 0
SHEET 2 AB2 4 ALA B 378 SER B 383 -1 N SER B 383 O GLN B 386
SHEET 3 AB2 4 PHE B 423 MET B 428 -1 O SER B 426 N GLU B 380
SHEET 4 AB2 4 THR B 437 LEU B 441 -1 O LEU B 441 N PHE B 423
SSBOND 1 CYS A 261 CYS A 321 1555 1555 2.03
SSBOND 2 CYS A 367 CYS A 425 1555 1555 2.05
SSBOND 3 CYS B 261 CYS B 321 1555 1555 2.02
SSBOND 4 CYS B 367 CYS B 425 1555 1555 2.05
LINK ND2 ASN A 297 C1 NAG C 1 1555 1555 1.32
LINK ND2 ASN B 297 C1 NAG D 1 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.36
LINK O6 NAG C 1 C1 FUC C 8 1555 1555 1.40
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.37
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.39
LINK O6 BMA C 3 C1 MAN C 6 1555 1555 1.37
LINK O2 MAN C 4 C1 NAG C 5 1555 1555 1.44
LINK O2 MAN C 6 C1 NAG C 7 1555 1555 1.39
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O6 NAG D 1 C1 FUC D 8 1555 1555 1.41
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.42
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.40
LINK O6 BMA D 3 C1 MAN D 6 1555 1555 1.42
LINK O2 MAN D 4 C1 NAG D 5 1555 1555 1.40
LINK O2 MAN D 6 C1 NAG D 7 1555 1555 1.42
CISPEP 1 TYR A 373 PRO A 374 0 -1.69
CISPEP 2 TYR B 373 PRO B 374 0 -1.99
CRYST1 152.744 152.744 108.984 90.00 90.00 120.00 P 61 2 2 12
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 0.006547 0.003780 0.000000 0.00000
SCALE2 0.000000 0.007560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
