HEADER IMMUNE SYSTEM 19-APR-18 6D58
TITLE CRYSTAL STRUCTURE OF A FC FRAGMENT OF HUMAN IGG3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN HEAVY CONSTANT GAMMA 3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HDC,HEAVY CHAIN DISEASE PROTEIN,IG GAMMA-3 CHAIN C REGION;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IGHG3;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS IMMUNOGLOBULIN, IGG3, IMMUNE SYSTEM, IMMUNOGLOBULIN-LIKE BETA
KEYWDS 2 SANDWICH, FC FRAGMENT
EXPDTA X-RAY DIFFRACTION
AUTHOR N.GOHAIN,W.D.TOLBERT,M.PAZGIER
REVDAT 4 04-OCT-23 6D58 1 HETSYN LINK
REVDAT 3 29-JUL-20 6D58 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 18-DEC-19 6D58 1 REMARK
REVDAT 1 15-MAY-19 6D58 0
JRNL AUTH N.GOHAIN,W.D.TOLBERT,M.PAZGIER
JRNL TITL CRYSTAL STRUCTURE OF A FC FRAGMENT OF HUMAN IGG3.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 68.1
REMARK 3 NUMBER OF REFLECTIONS : 15194
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 759
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 35.8916 - 4.0857 0.74 3281 149 0.1963 0.2389
REMARK 3 2 4.0857 - 3.2436 0.76 3208 175 0.2426 0.2917
REMARK 3 3 3.2436 - 2.8338 0.72 2994 189 0.2777 0.3242
REMARK 3 4 2.8338 - 2.5748 0.64 2696 135 0.3163 0.3975
REMARK 3 5 2.5748 - 2.3903 0.54 2256 111 0.3244 0.4007
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) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.380
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 : 0.012 3628
REMARK 3 ANGLE : 1.470 4966
REMARK 3 CHIRALITY : 0.075 590
REMARK 3 PLANARITY : 0.009 608
REMARK 3 DIHEDRAL : 8.461 2200
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 237 THROUGH 443)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4401 9.7812 41.6332
REMARK 3 T TENSOR
REMARK 3 T11: 0.2435 T22: 0.2134
REMARK 3 T33: 0.4644 T12: 0.0226
REMARK 3 T13: 0.0480 T23: 0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 1.9768 L22: 1.6466
REMARK 3 L33: 4.9474 L12: 1.1368
REMARK 3 L13: 1.9855 L23: 1.3043
REMARK 3 S TENSOR
REMARK 3 S11: -0.2012 S12: 0.1348 S13: 0.2000
REMARK 3 S21: -0.1176 S22: 0.0535 S23: -0.0240
REMARK 3 S31: -0.1538 S32: -0.0461 S33: 0.1228
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 237 THROUGH 443)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9241 -10.3225 44.5400
REMARK 3 T TENSOR
REMARK 3 T11: 0.6003 T22: 0.2521
REMARK 3 T33: 0.5148 T12: 0.0172
REMARK 3 T13: -0.0861 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 2.1568 L22: 3.8116
REMARK 3 L33: 4.7620 L12: 0.0042
REMARK 3 L13: -0.3162 L23: -0.0911
REMARK 3 S TENSOR
REMARK 3 S11: -0.1706 S12: -0.2420 S13: -0.3102
REMARK 3 S21: 1.0786 S22: 0.1273 S23: -0.4077
REMARK 3 S31: 0.1236 S32: 0.2914 S33: 0.0706
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 6D58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000234017.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JAN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : RH COATED MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15232
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 68.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.26000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 42.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.48100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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 (%): 56.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 5,000 0.1 M BIS-TRIS PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 24.79500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.01450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.33900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.01450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.79500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.33900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 58.0 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 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 LEU A 234
REMARK 465 LEU A 235
REMARK 465 GLY A 236
REMARK 465 SER A 444
REMARK 465 PRO A 445
REMARK 465 GLY A 446
REMARK 465 LYS A 447
REMARK 465 LEU B 234
REMARK 465 LEU B 235
REMARK 465 GLY B 236
REMARK 465 SER B 444
REMARK 465 PRO B 445
REMARK 465 GLY B 446
REMARK 465 LYS B 447
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 CG ASN A 297 C1 NAG C 1 2.07
REMARK 500 OD1 ASN A 297 C1 NAG C 1 2.09
REMARK 500 O LYS B 340 OH TYR B 373 2.17
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 ASN A 297 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 LEU B 242 CB - CG - CD2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 PRO B 291 C - N - CA ANGL. DEV. = -9.8 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 ASP A 270 97.07 -166.73
REMARK 500 HIS A 285 12.72 -143.48
REMARK 500 SER A 298 38.22 101.95
REMARK 500 ASN A 390 78.51 -104.59
REMARK 500 VAL B 273 104.25 36.37
REMARK 500 VAL B 282 -146.52 -68.55
REMARK 500 ASN B 286 40.35 -85.15
REMARK 500 LYS B 288 95.07 -165.35
REMARK 500 GLU B 293 -156.10 -146.99
REMARK 500 TYR B 296 15.75 -62.61
REMARK 500 SER B 298 6.94 58.10
REMARK 500 PRO B 331 96.04 -63.55
REMARK 500 PRO B 374 -179.12 -68.23
REMARK 500 ASN B 390 65.69 -101.13
REMARK 500 ASP B 399 -128.95 -81.47
REMARK 500 LYS B 414 -82.00 7.07
REMARK 500 TRP B 417 -80.38 -45.43
REMARK 500 LEU B 441 110.79 -165.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 297 11.47
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6D58 A 234 447 UNP P01860 IGHG3_HUMAN 164 377
DBREF 6D58 B 234 447 UNP P01860 IGHG3_HUMAN 164 377
SEQADV 6D58 HIS A 435 UNP P01860 ARG 365 ENGINEERED MUTATION
SEQADV 6D58 HIS B 435 UNP P01860 ARG 365 ENGINEERED MUTATION
SEQRES 1 A 214 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 2 A 214 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 3 A 214 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 4 A 214 VAL GLN PHE LYS TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 5 A 214 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 6 A 214 THR PHE ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 7 A 214 ASP TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER
SEQRES 8 A 214 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 9 A 214 LYS THR LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 10 A 214 LEU PRO PRO SER ARG GLU GLU MET THR LYS ASN GLN VAL
SEQRES 11 A 214 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 12 A 214 ILE ALA VAL GLU TRP GLU SER SER GLY GLN PRO GLU ASN
SEQRES 13 A 214 ASN TYR ASN THR THR PRO PRO MET LEU ASP SER ASP GLY
SEQRES 14 A 214 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 15 A 214 ARG TRP GLN GLN GLY ASN ILE PHE SER CYS SER VAL MET
SEQRES 16 A 214 HIS GLU ALA LEU HIS ASN HIS PHE THR GLN LYS SER LEU
SEQRES 17 A 214 SER LEU SER PRO GLY LYS
SEQRES 1 B 214 LEU LEU GLY GLY PRO SER VAL PHE LEU PHE PRO PRO LYS
SEQRES 2 B 214 PRO LYS ASP THR LEU MET ILE SER ARG THR PRO GLU VAL
SEQRES 3 B 214 THR CYS VAL VAL VAL ASP VAL SER HIS GLU ASP PRO GLU
SEQRES 4 B 214 VAL GLN PHE LYS TRP TYR VAL ASP GLY VAL GLU VAL HIS
SEQRES 5 B 214 ASN ALA LYS THR LYS PRO ARG GLU GLU GLN TYR ASN SER
SEQRES 6 B 214 THR PHE ARG VAL VAL SER VAL LEU THR VAL LEU HIS GLN
SEQRES 7 B 214 ASP TRP LEU ASN GLY LYS GLU TYR LYS CYS LYS VAL SER
SEQRES 8 B 214 ASN LYS ALA LEU PRO ALA PRO ILE GLU LYS THR ILE SER
SEQRES 9 B 214 LYS THR LYS GLY GLN PRO ARG GLU PRO GLN VAL TYR THR
SEQRES 10 B 214 LEU PRO PRO SER ARG GLU GLU MET THR LYS ASN GLN VAL
SEQRES 11 B 214 SER LEU THR CYS LEU VAL LYS GLY PHE TYR PRO SER ASP
SEQRES 12 B 214 ILE ALA VAL GLU TRP GLU SER SER GLY GLN PRO GLU ASN
SEQRES 13 B 214 ASN TYR ASN THR THR PRO PRO MET LEU ASP SER ASP GLY
SEQRES 14 B 214 SER PHE PHE LEU TYR SER LYS LEU THR VAL ASP LYS SER
SEQRES 15 B 214 ARG TRP GLN GLN GLY ASN ILE PHE SER CYS SER VAL MET
SEQRES 16 B 214 HIS GLU ALA LEU HIS ASN HIS PHE THR GLN LYS SER LEU
SEQRES 17 B 214 SER LEU SER PRO GLY LYS
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 *22(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 LYS A 360 5 7
HELIX 4 AA4 LYS A 414 GLY A 420 1 7
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 LEU B 314 1 6
HELIX 8 AA8 SER B 354 LYS B 360 5 7
HELIX 9 AA9 LYS B 414 ASN B 421 1 8
HELIX 10 AB1 LEU B 432 ASN B 434 5 3
SHEET 1 AA1 4 SER A 239 PHE A 243 0
SHEET 2 AA1 4 GLU A 258 VAL A 266 -1 O THR A 260 N PHE A 243
SHEET 3 AA1 4 PHE A 300 THR A 307 -1 O PHE A 300 N VAL A 266
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 THR A 260 N PHE A 243
SHEET 3 AA2 4 PHE A 300 THR A 307 -1 O PHE A 300 N VAL A 266
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 GLN 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 320 N TYR A 278
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 LEU A 368 N TYR A 349
SHEET 3 AA4 4 PHE A 404 ASP A 413 -1 O LEU A 406 N VAL A 369
SHEET 4 AA4 4 TYR A 391 THR A 393 -1 N ASN A 392 O LYS 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 LEU A 368 N TYR A 349
SHEET 3 AA5 4 PHE A 404 ASP A 413 -1 O LEU A 406 N VAL A 369
SHEET 4 AA5 4 MET A 397 LEU A 398 -1 N MET A 397 O PHE A 405
SHEET 1 AA6 3 ALA A 378 GLU A 382 0
SHEET 2 AA6 3 PHE A 423 MET A 428 -1 O SER A 426 N GLU A 380
SHEET 3 AA6 3 PHE A 436 LEU A 441 -1 O LYS A 439 N CYS A 425
SHEET 1 AA7 4 SER B 239 PHE B 243 0
SHEET 2 AA7 4 GLU B 258 VAL B 264 -1 O VAL B 262 N PHE B 241
SHEET 3 AA7 4 VAL B 303 THR B 307 -1 O LEU B 306 N VAL B 259
SHEET 4 AA7 4 ALA B 287 THR B 289 -1 N LYS B 288 O VAL B 305
SHEET 1 AA8 3 LYS B 276 VAL B 279 0
SHEET 2 AA8 3 TYR B 319 LYS B 322 -1 O LYS B 322 N LYS B 276
SHEET 3 AA8 3 THR B 335 ILE B 336 -1 O ILE B 336 N TYR B 319
SHEET 1 AA9 4 GLN B 347 LEU B 351 0
SHEET 2 AA9 4 GLN B 362 PHE B 372 -1 O LYS B 370 N GLN B 347
SHEET 3 AA9 4 PHE B 404 ASP B 413 -1 O LEU B 410 N LEU B 365
SHEET 4 AA9 4 TYR B 391 THR B 393 -1 N ASN B 392 O LYS B 409
SHEET 1 AB1 4 GLN B 347 LEU B 351 0
SHEET 2 AB1 4 GLN B 362 PHE B 372 -1 O LYS B 370 N GLN B 347
SHEET 3 AB1 4 PHE B 404 ASP B 413 -1 O LEU B 410 N LEU B 365
SHEET 4 AB1 4 MET B 397 LEU B 398 -1 N MET B 397 O PHE B 405
SHEET 1 AB2 4 GLN B 386 PRO B 387 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 PHE B 436 LEU B 441 -1 O LYS B 439 N CYS B 425
SSBOND 1 CYS A 261 CYS A 321 1555 1555 2.03
SSBOND 2 CYS A 367 CYS A 425 1555 1555 2.07
SSBOND 3 CYS B 261 CYS B 321 1555 1555 2.04
SSBOND 4 CYS B 367 CYS B 425 1555 1555 2.06
LINK ND2 ASN A 297 C1 NAG C 1 1555 1555 1.50
LINK ND2 ASN B 297 C1 NAG D 1 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.42
LINK O6 NAG C 1 C1 FUC C 8 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.46
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.46
LINK O6 BMA C 3 C1 MAN C 6 1555 1555 1.45
LINK O2 MAN C 4 C1 NAG C 5 1555 1555 1.43
LINK O2 MAN C 6 C1 NAG C 7 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43
LINK O6 NAG D 1 C1 FUC D 8 1555 1555 1.46
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.43
LINK O6 BMA D 3 C1 MAN D 6 1555 1555 1.44
LINK O2 MAN D 4 C1 NAG D 5 1555 1555 1.43
LINK O2 MAN D 6 C1 NAG D 7 1555 1555 1.45
CISPEP 1 TYR A 373 PRO A 374 0 -1.29
CISPEP 2 TYR B 373 PRO B 374 0 -4.01
CRYST1 49.590 80.678 136.029 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 0.020165 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012395 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
