HEADER SIGNALING PROTEIN 17-OCT-13 4CC1
TITLE NOTCH LIGAND, JAGGED-1, CONTAINS AN N-TERMINAL C2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN JAGGED-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 32-335;
COMPND 5 SYNONYM: JAGGED1, HJ1, CD339;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: NAG LINKAGE AT N217 IN BOTH A, B CHAINS, FUC LINKAGE
COMPND 8 AT T311 IN A CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S
KEYWDS SIGNALING PROTEIN, GLYCOPROTEIN, EXTRACELLULAR, DEVELOPMENTAL
KEYWDS 2 PROTEIN, NOTCH SIGNALING PATHWAY, EGF, DSL, LIPID, NOTCH, MEMBRANE,
KEYWDS 3 PROTEIN-BINDING, TRANSMEMBRANE, EGF-LIKE DOMAIN, DISEASE MUTATION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.CHILAKURI,D.SHEPPARD,M.X.G.ILAGAN,L.R.HOLT,F.ABBOTT,S.LIANG,
AUTHOR 2 R.KOPAN,P.A.HANDFORD,S.M.LEA
REVDAT 5 20-DEC-23 4CC1 1 HETSYN
REVDAT 4 29-JUL-20 4CC1 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 25-DEC-13 4CC1 1 HETATM
REVDAT 2 11-DEC-13 4CC1 1 JRNL
REVDAT 1 27-NOV-13 4CC1 0
JRNL AUTH C.R.CHILAKURI,D.SHEPPARD,M.X.G.ILAGAN,L.R.HOLT,F.ABBOTT,
JRNL AUTH 2 S.LIANG,R.KOPAN,P.A.HANDFORD,S.M.LEA
JRNL TITL STRUCTURAL ANALYSIS UNCOVERS LIPID-BINDING PROPERTIES OF
JRNL TITL 2 NOTCH LIGANDS
JRNL REF CELL REP. V. 5 861 2013
JRNL REFN ESSN 2211-1247
JRNL PMID 24239355
JRNL DOI 10.1016/J.CELREP.2013.10.029
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 17666
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.590
REMARK 3 FREE R VALUE TEST SET COUNT : 988
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.01
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.22
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2801
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2773
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2639
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE : 0.3468
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.78
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 162
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4726
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 91.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.84150
REMARK 3 B22 (A**2) : -10.61960
REMARK 3 B33 (A**2) : 4.77810
REMARK 3 B12 (A**2) : -8.16110
REMARK 3 B13 (A**2) : -11.27760
REMARK 3 B23 (A**2) : 1.92170
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.400
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.354
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4939 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6715 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1671 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 142 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 722 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4939 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 607 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5064 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.20
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.55
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4CC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1290058752.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17793
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.840
REMARK 200 RESOLUTION RANGE LOW (A) : 60.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 2.450
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2VJ2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 HIS A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 HIS B 338
REMARK 465 HIS B 339
REMARK 465 HIS B 340
REMARK 465 HIS B 341
REMARK 465 HIS B 342
REMARK 465 HIS B 343
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 ARG A 130 -51.18 75.81
REMARK 500 ASP A 204 58.05 -150.58
REMARK 500 GLN A 304 71.15 51.42
REMARK 500 CYS B 66 -74.18 -72.85
REMARK 500 THR B 67 -148.65 54.82
REMARK 500 ARG B 68 -116.76 41.57
REMARK 500 ARG B 130 -50.36 75.57
REMARK 500 SER B 142 63.59 -117.28
REMARK 500 GLN B 304 71.27 52.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1340 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 72 OD2
REMARK 620 2 ASP A 140 OD1 93.0
REMARK 620 3 SER A 141 O 77.9 73.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1339 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 72 OD2
REMARK 620 2 ASP B 140 OD1 89.7
REMARK 620 3 SER B 141 O 80.2 85.1
REMARK 620 4 HOH B2001 O 82.3 66.2 146.3
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CBZ RELATED DB: PDB
REMARK 900 NOTCH LIGAND, JAGGED-1, CONTAINS AN N-TERMINAL C2 DOMAIN
REMARK 900 RELATED ID: 4CC0 RELATED DB: PDB
REMARK 900 NOTCH LIGAND, JAGGED-1, CONTAINS AN N-TERMINAL C2 DOMAIN
DBREF 4CC1 A 32 335 UNP P78504 JAG1_HUMAN 32 335
DBREF 4CC1 B 32 335 UNP P78504 JAG1_HUMAN 32 335
SEQADV 4CC1 VAL A 336 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 ASP A 337 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS A 338 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS A 339 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS A 340 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS A 341 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS A 342 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS A 343 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 VAL B 336 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 ASP B 337 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS B 338 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS B 339 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS B 340 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS B 341 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS B 342 UNP P78504 EXPRESSION TAG
SEQADV 4CC1 HIS B 343 UNP P78504 EXPRESSION TAG
SEQRES 1 A 312 SER GLY GLN PHE GLU LEU GLU ILE LEU SER MET GLN ASN
SEQRES 2 A 312 VAL ASN GLY GLU LEU GLN ASN GLY ASN CYS CYS GLY GLY
SEQRES 3 A 312 ALA ARG ASN PRO GLY ASP ARG LYS CYS THR ARG ASP GLU
SEQRES 4 A 312 CYS ASP THR TYR PHE LYS VAL CYS LEU LYS GLU TYR GLN
SEQRES 5 A 312 SER ARG VAL THR ALA GLY GLY PRO CYS SER PHE GLY SER
SEQRES 6 A 312 GLY SER THR PRO VAL ILE GLY GLY ASN THR PHE ASN LEU
SEQRES 7 A 312 LYS ALA SER ARG GLY ASN ASP ARG ASN ARG ILE VAL LEU
SEQRES 8 A 312 PRO PHE SER PHE ALA TRP PRO ARG SER TYR THR LEU LEU
SEQRES 9 A 312 VAL GLU ALA TRP ASP SER SER ASN ASP THR VAL GLN PRO
SEQRES 10 A 312 ASP SER ILE ILE GLU LYS ALA SER HIS SER GLY MET ILE
SEQRES 11 A 312 ASN PRO SER ARG GLN TRP GLN THR LEU LYS GLN ASN THR
SEQRES 12 A 312 GLY VAL ALA HIS PHE GLU TYR GLN ILE ARG VAL THR CYS
SEQRES 13 A 312 ASP ASP TYR TYR TYR GLY PHE GLY CYS ASN LYS PHE CYS
SEQRES 14 A 312 ARG PRO ARG ASP ASP PHE PHE GLY HIS TYR ALA CYS ASP
SEQRES 15 A 312 GLN ASN GLY ASN LYS THR CYS MET GLU GLY TRP MET GLY
SEQRES 16 A 312 PRO GLU CYS ASN ARG ALA ILE CYS ARG GLN GLY CYS SER
SEQRES 17 A 312 PRO LYS HIS GLY SER CYS LYS LEU PRO GLY ASP CYS ARG
SEQRES 18 A 312 CYS GLN TYR GLY TRP GLN GLY LEU TYR CYS ASP LYS CYS
SEQRES 19 A 312 ILE PRO HIS PRO GLY CYS VAL HIS GLY ILE CYS ASN GLU
SEQRES 20 A 312 PRO TRP GLN CYS LEU CYS GLU THR ASN TRP GLY GLY GLN
SEQRES 21 A 312 LEU CYS ASP LYS ASP LEU ASN TYR CYS GLY THR HIS GLN
SEQRES 22 A 312 PRO CYS LEU ASN GLY GLY THR CYS SER ASN THR GLY PRO
SEQRES 23 A 312 ASP LYS TYR GLN CYS SER CYS PRO GLU GLY TYR SER GLY
SEQRES 24 A 312 PRO ASN CYS GLU ILE VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 312 SER GLY GLN PHE GLU LEU GLU ILE LEU SER MET GLN ASN
SEQRES 2 B 312 VAL ASN GLY GLU LEU GLN ASN GLY ASN CYS CYS GLY GLY
SEQRES 3 B 312 ALA ARG ASN PRO GLY ASP ARG LYS CYS THR ARG ASP GLU
SEQRES 4 B 312 CYS ASP THR TYR PHE LYS VAL CYS LEU LYS GLU TYR GLN
SEQRES 5 B 312 SER ARG VAL THR ALA GLY GLY PRO CYS SER PHE GLY SER
SEQRES 6 B 312 GLY SER THR PRO VAL ILE GLY GLY ASN THR PHE ASN LEU
SEQRES 7 B 312 LYS ALA SER ARG GLY ASN ASP ARG ASN ARG ILE VAL LEU
SEQRES 8 B 312 PRO PHE SER PHE ALA TRP PRO ARG SER TYR THR LEU LEU
SEQRES 9 B 312 VAL GLU ALA TRP ASP SER SER ASN ASP THR VAL GLN PRO
SEQRES 10 B 312 ASP SER ILE ILE GLU LYS ALA SER HIS SER GLY MET ILE
SEQRES 11 B 312 ASN PRO SER ARG GLN TRP GLN THR LEU LYS GLN ASN THR
SEQRES 12 B 312 GLY VAL ALA HIS PHE GLU TYR GLN ILE ARG VAL THR CYS
SEQRES 13 B 312 ASP ASP TYR TYR TYR GLY PHE GLY CYS ASN LYS PHE CYS
SEQRES 14 B 312 ARG PRO ARG ASP ASP PHE PHE GLY HIS TYR ALA CYS ASP
SEQRES 15 B 312 GLN ASN GLY ASN LYS THR CYS MET GLU GLY TRP MET GLY
SEQRES 16 B 312 PRO GLU CYS ASN ARG ALA ILE CYS ARG GLN GLY CYS SER
SEQRES 17 B 312 PRO LYS HIS GLY SER CYS LYS LEU PRO GLY ASP CYS ARG
SEQRES 18 B 312 CYS GLN TYR GLY TRP GLN GLY LEU TYR CYS ASP LYS CYS
SEQRES 19 B 312 ILE PRO HIS PRO GLY CYS VAL HIS GLY ILE CYS ASN GLU
SEQRES 20 B 312 PRO TRP GLN CYS LEU CYS GLU THR ASN TRP GLY GLY GLN
SEQRES 21 B 312 LEU CYS ASP LYS ASP LEU ASN TYR CYS GLY THR HIS GLN
SEQRES 22 B 312 PRO CYS LEU ASN GLY GLY THR CYS SER ASN THR GLY PRO
SEQRES 23 B 312 ASP LYS TYR GLN CYS SER CYS PRO GLU GLY TYR SER GLY
SEQRES 24 B 312 PRO ASN CYS GLU ILE VAL ASP HIS HIS HIS HIS HIS HIS
MODRES 4CC1 ASN A 217 ASN GLYCOSYLATION SITE
MODRES 4CC1 THR A 311 THR GLYCOSYLATION SITE
MODRES 4CC1 ASN B 217 ASN GLYCOSYLATION SITE
HET NAG A1338 14
HET FUC A1339 10
HET CA A1340 1
HET CL A1341 1
HET CL A1342 1
HET CL A1343 1
HET CL A1344 1
HET NAG B1338 14
HET CA B1339 1
HET CL B1340 1
HET EDO B1341 10
HET EDO B1342 10
HET CL B1343 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 FUC C6 H12 O5
FORMUL 5 CA 2(CA 2+)
FORMUL 6 CL 6(CL 1-)
FORMUL 13 EDO 2(C2 H6 O2)
FORMUL 16 HOH *6(H2 O)
HELIX 1 1 ASN A 298 GLN A 304 1 7
HELIX 2 2 ASN B 298 GLN B 304 1 7
SHEET 1 AA 2 PHE A 107 ASN A 108 0
SHEET 2 AA 2 GLY A 33 GLN A 43 -1 O MET A 42 N PHE A 107
SHEET 1 AB 2 ARG A 119 PHE A 124 0
SHEET 2 AB 2 GLY A 33 GLN A 43 -1 O GLY A 33 N PHE A 124
SHEET 1 AC 4 SER A 164 GLN A 172 0
SHEET 2 AC 4 HIS A 178 CYS A 187 -1 O PHE A 179 N GLN A 172
SHEET 3 AC 4 GLY A 33 GLN A 43 -1 O GLN A 34 N THR A 186
SHEET 4 AC 4 PHE A 107 ASN A 108 -1 O PHE A 107 N MET A 42
SHEET 1 AD 4 SER A 164 GLN A 172 0
SHEET 2 AD 4 HIS A 178 CYS A 187 -1 O PHE A 179 N GLN A 172
SHEET 3 AD 4 GLY A 33 GLN A 43 -1 O GLN A 34 N THR A 186
SHEET 4 AD 4 ARG A 119 PHE A 124 -1 O ILE A 120 N LEU A 37
SHEET 1 AE 4 GLY A 95 SER A 98 0
SHEET 2 AE 4 THR A 73 LYS A 80 -1 O VAL A 77 N GLY A 97
SHEET 3 AE 4 SER A 131 ASP A 140 -1 O THR A 133 N LYS A 80
SHEET 4 AE 4 SER A 150 MET A 160 -1 O SER A 150 N ASP A 140
SHEET 1 AF 2 TYR A 191 TYR A 192 0
SHEET 2 AF 2 LYS A 198 PHE A 199 -1 O LYS A 198 N TYR A 192
SHEET 1 AG 3 ARG A 203 ASP A 205 0
SHEET 2 AG 3 GLY A 208 CYS A 212 -1 O GLY A 208 N ASP A 205
SHEET 3 AG 3 LYS A 218 CYS A 220 -1 O THR A 219 N ALA A 211
SHEET 1 AH 2 TRP A 224 MET A 225 0
SHEET 2 AH 2 ARG A 231 ALA A 232 -1 O ARG A 231 N MET A 225
SHEET 1 AI 2 GLY A 243 SER A 244 0
SHEET 2 AI 2 ARG A 252 CYS A 253 -1 O ARG A 252 N SER A 244
SHEET 1 AJ 2 TRP A 257 GLN A 258 0
SHEET 2 AJ 2 LYS A 264 CYS A 265 -1 O LYS A 264 N GLN A 258
SHEET 1 AK 2 GLY A 274 ILE A 275 0
SHEET 2 AK 2 LEU A 283 CYS A 284 -1 O LEU A 283 N ILE A 275
SHEET 1 AL 2 TRP A 288 GLY A 289 0
SHEET 2 AL 2 LYS A 295 ASP A 296 -1 O LYS A 295 N GLY A 289
SHEET 1 AM 2 THR A 311 GLY A 316 0
SHEET 2 AM 2 LYS A 319 SER A 323 -1 O LYS A 319 N THR A 315
SHEET 1 BA 2 PHE B 107 ASN B 108 0
SHEET 2 BA 2 GLY B 33 GLN B 43 -1 O MET B 42 N PHE B 107
SHEET 1 BB 2 ARG B 119 PHE B 124 0
SHEET 2 BB 2 GLY B 33 GLN B 43 -1 O GLY B 33 N PHE B 124
SHEET 1 BC 4 SER B 164 GLN B 172 0
SHEET 2 BC 4 HIS B 178 CYS B 187 -1 O PHE B 179 N GLN B 172
SHEET 3 BC 4 GLY B 33 GLN B 43 -1 O GLN B 34 N THR B 186
SHEET 4 BC 4 PHE B 107 ASN B 108 -1 O PHE B 107 N MET B 42
SHEET 1 BD 4 SER B 164 GLN B 172 0
SHEET 2 BD 4 HIS B 178 CYS B 187 -1 O PHE B 179 N GLN B 172
SHEET 3 BD 4 GLY B 33 GLN B 43 -1 O GLN B 34 N THR B 186
SHEET 4 BD 4 ARG B 119 PHE B 124 -1 O ILE B 120 N LEU B 37
SHEET 1 BE 4 GLY B 95 SER B 98 0
SHEET 2 BE 4 THR B 73 GLU B 81 -1 O VAL B 77 N GLY B 97
SHEET 3 BE 4 SER B 131 ASP B 140 -1 O THR B 133 N LYS B 80
SHEET 4 BE 4 SER B 150 MET B 160 -1 O SER B 150 N ASP B 140
SHEET 1 BF 2 TYR B 191 TYR B 192 0
SHEET 2 BF 2 LYS B 198 PHE B 199 -1 O LYS B 198 N TYR B 192
SHEET 1 BG 3 ARG B 203 ASP B 205 0
SHEET 2 BG 3 GLY B 208 CYS B 212 -1 O GLY B 208 N ASP B 205
SHEET 3 BG 3 LYS B 218 CYS B 220 -1 O THR B 219 N ALA B 211
SHEET 1 BH 2 TRP B 224 MET B 225 0
SHEET 2 BH 2 ARG B 231 ALA B 232 -1 O ARG B 231 N MET B 225
SHEET 1 BI 2 GLY B 243 SER B 244 0
SHEET 2 BI 2 ARG B 252 CYS B 253 -1 O ARG B 252 N SER B 244
SHEET 1 BJ 2 TRP B 257 GLN B 258 0
SHEET 2 BJ 2 LYS B 264 CYS B 265 -1 O LYS B 264 N GLN B 258
SHEET 1 BK 2 GLY B 274 ILE B 275 0
SHEET 2 BK 2 LEU B 283 CYS B 284 -1 O LEU B 283 N ILE B 275
SHEET 1 BL 2 TRP B 288 GLY B 289 0
SHEET 2 BL 2 LYS B 295 ASP B 296 -1 O LYS B 295 N GLY B 289
SHEET 1 BM 2 THR B 311 GLY B 316 0
SHEET 2 BM 2 LYS B 319 SER B 323 -1 O LYS B 319 N THR B 315
SSBOND 1 CYS A 54 CYS A 66 1555 1555 2.05
SSBOND 2 CYS A 55 CYS A 71 1555 1555 2.05
SSBOND 3 CYS A 78 CYS A 92 1555 1555 2.06
SSBOND 4 CYS A 187 CYS A 196 1555 1555 2.07
SSBOND 5 CYS A 200 CYS A 212 1555 1555 2.07
SSBOND 6 CYS A 220 CYS A 229 1555 1555 2.07
SSBOND 7 CYS A 234 CYS A 245 1555 1555 2.05
SSBOND 8 CYS A 238 CYS A 251 1555 1555 2.06
SSBOND 9 CYS A 253 CYS A 262 1555 1555 2.04
SSBOND 10 CYS A 265 CYS A 276 1555 1555 2.08
SSBOND 11 CYS A 271 CYS A 282 1555 1555 2.04
SSBOND 12 CYS A 284 CYS A 293 1555 1555 2.07
SSBOND 13 CYS A 300 CYS A 312 1555 1555 2.04
SSBOND 14 CYS A 306 CYS A 322 1555 1555 2.04
SSBOND 15 CYS A 324 CYS A 333 1555 1555 2.05
SSBOND 16 CYS B 54 CYS B 66 1555 1555 2.05
SSBOND 17 CYS B 55 CYS B 71 1555 1555 2.04
SSBOND 18 CYS B 78 CYS B 92 1555 1555 2.05
SSBOND 19 CYS B 187 CYS B 196 1555 1555 2.08
SSBOND 20 CYS B 200 CYS B 212 1555 1555 2.05
SSBOND 21 CYS B 220 CYS B 229 1555 1555 2.06
SSBOND 22 CYS B 234 CYS B 245 1555 1555 2.04
SSBOND 23 CYS B 238 CYS B 251 1555 1555 2.05
SSBOND 24 CYS B 253 CYS B 262 1555 1555 2.04
SSBOND 25 CYS B 265 CYS B 276 1555 1555 2.08
SSBOND 26 CYS B 271 CYS B 282 1555 1555 2.05
SSBOND 27 CYS B 284 CYS B 293 1555 1555 2.05
SSBOND 28 CYS B 300 CYS B 312 1555 1555 2.04
SSBOND 29 CYS B 306 CYS B 322 1555 1555 2.03
SSBOND 30 CYS B 324 CYS B 333 1555 1555 2.04
LINK ND2 ASN A 217 C1 NAG A1338 1555 1555 1.44
LINK OG1 THR A 311 C1 FUC A1339 1555 1555 1.42
LINK ND2 ASN B 217 C1 NAG B1338 1555 1555 1.45
LINK OD2 ASP A 72 CA CA A1340 1555 1555 2.84
LINK OD1 ASP A 140 CA CA A1340 1555 1555 2.63
LINK O SER A 141 CA CA A1340 1555 1555 3.00
LINK OD2 ASP B 72 CA CA B1339 1555 1555 2.74
LINK OD1 ASP B 140 CA CA B1339 1555 1555 2.76
LINK O SER B 141 CA CA B1339 1555 1555 2.56
LINK CA CA B1339 O HOH B2001 1555 1555 2.06
CRYST1 55.950 60.560 63.030 92.89 104.95 105.92 P 1 2
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 0.017873 0.005098 0.005484 0.00000
SCALE2 0.000000 0.017171 0.002259 0.00000
SCALE3 0.000000 0.000000 0.016563 0.00000
MTRIX1 1 -0.300000 -0.597000 0.744000 -28.36608 1
MTRIX2 1 -0.591000 -0.496000 -0.636000 11.95355 1
MTRIX3 1 0.749000 -0.631000 -0.204000 -15.59484 1
(ATOM LINES ARE NOT SHOWN.)
END
