HEADER CELL ADHESION 19-JAN-14 4OI9
TITLE CRYSTAL STRUCTURE OF ICAM-5 D1-D4 ECTODOMAIN FRAGMENT, SPACE GROUP P21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERCELLULAR ADHESION MOLECULE 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: D1-D4;
COMPND 5 SYNONYM: ICAM-5, TELENCEPHALIN;
COMPND 6 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: ICAM5, TLCN, TLN;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS CELL ADHESION, CELL SURFACE, NEURONS, IMMUNOGLOBULIN SUPERFAMILY,
KEYWDS 2 INTERCELLULAR ADHESION MOLECULES, ICAM-5, TELENCEPHALIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.RECACHA,D.JIMENEZ,L.TIAN,R.BARREDO,C.GHAMBERG,J.M.CASASNOVAS
REVDAT 2 29-JUL-20 4OI9 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 16-JUL-14 4OI9 0
JRNL AUTH R.RECACHA,D.JIMENEZ,L.TIAN,R.BARREDO,C.G.GAHMBERG,
JRNL AUTH 2 J.M.CASASNOVAS
JRNL TITL CRYSTAL STRUCTURES OF AN ICAM-5 ECTODOMAIN FRAGMENT SHOW
JRNL TITL 2 ELECTROSTATIC-BASED HOMOPHILIC ADHESIONS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 1934 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25004970
JRNL DOI 10.1107/S1399004714009468
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.250
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 20738
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.740
REMARK 3 FREE R VALUE TEST SET COUNT : 2325
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 19.5835 - 6.7005 0.84 1873 229 0.2067 0.1993
REMARK 3 2 6.7005 - 5.3542 0.90 2001 226 0.2061 0.2360
REMARK 3 3 5.3542 - 4.6880 0.91 2022 193 0.1726 0.1838
REMARK 3 4 4.6880 - 4.2642 0.89 1970 240 0.1765 0.1931
REMARK 3 5 4.2642 - 3.9613 0.90 2015 230 0.2121 0.2175
REMARK 3 6 3.9613 - 3.7294 0.91 2064 201 0.2119 0.2400
REMARK 3 7 3.7294 - 3.5438 0.90 1957 222 0.2296 0.2589
REMARK 3 8 3.5438 - 3.3903 0.91 2053 209 0.2581 0.2896
REMARK 3 9 3.3903 - 3.2604 0.90 1987 223 0.2815 0.2697
REMARK 3 10 3.2604 - 3.1484 0.90 2009 218 0.2818 0.3236
REMARK 3 11 3.1484 - 3.0503 0.90 2008 222 0.3153 0.3252
REMARK 3 12 3.0503 - 2.9634 0.89 1971 224 0.3308 0.3542
REMARK 3 13 2.9634 - 2.8857 0.90 1992 217 0.3556 0.4127
REMARK 3 14 2.8857 - 2.8155 0.90 2012 225 0.3681 0.4056
REMARK 3 15 2.8155 - 2.7517 0.89 1984 249 0.3711 0.4087
REMARK 3 16 2.7517 - 2.6932 0.91 2047 205 0.3834 0.3508
REMARK 3 17 2.6932 - 2.6395 0.89 1952 232 0.4108 0.4615
REMARK 3 18 2.6395 - 2.5898 0.89 1987 234 0.4231 0.4249
REMARK 3 19 2.5898 - 2.5437 0.90 2006 235 0.4224 0.4832
REMARK 3 20 2.5437 - 2.5006 0.89 2000 242 0.4279 0.4624
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.490
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: 0.0300
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3272
REMARK 3 ANGLE : 0.931 4401
REMARK 3 CHIRALITY : 0.058 522
REMARK 3 PLANARITY : 0.005 559
REMARK 3 DIHEDRAL : 23.282 1287
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 1:85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2423 -3.2420 91.0249
REMARK 3 T TENSOR
REMARK 3 T11: 0.3751 T22: 0.5895
REMARK 3 T33: 0.4639 T12: 0.0584
REMARK 3 T13: 0.0979 T23: 0.0804
REMARK 3 L TENSOR
REMARK 3 L11: 9.1897 L22: 3.1669
REMARK 3 L33: 4.5353 L12: 1.9183
REMARK 3 L13: -3.3509 L23: -1.3209
REMARK 3 S TENSOR
REMARK 3 S11: -0.0851 S12: 0.1793 S13: 0.0553
REMARK 3 S21: 0.1179 S22: 0.3028 S23: 0.5006
REMARK 3 S31: -0.1766 S32: -1.1629 S33: -0.2147
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 86:194 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5467 15.4228 62.9451
REMARK 3 T TENSOR
REMARK 3 T11: 0.4982 T22: 0.4809
REMARK 3 T33: 0.4168 T12: 0.0221
REMARK 3 T13: 0.0448 T23: 0.1493
REMARK 3 L TENSOR
REMARK 3 L11: 7.3825 L22: 2.5376
REMARK 3 L33: 9.6057 L12: 2.1461
REMARK 3 L13: -5.4778 L23: -3.4281
REMARK 3 S TENSOR
REMARK 3 S11: -0.1664 S12: 0.6666 S13: 0.4893
REMARK 3 S21: -0.2520 S22: -0.0203 S23: -0.2088
REMARK 3 S31: -0.4237 S32: 0.0133 S33: 0.1532
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 195:289 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.0088 20.0692 31.5361
REMARK 3 T TENSOR
REMARK 3 T11: 0.7258 T22: 1.6318
REMARK 3 T33: 0.6804 T12: -0.2637
REMARK 3 T13: 0.0849 T23: 0.4143
REMARK 3 L TENSOR
REMARK 3 L11: 2.5944 L22: 3.2679
REMARK 3 L33: 2.6951 L12: 0.2706
REMARK 3 L13: -0.6029 L23: 0.0719
REMARK 3 S TENSOR
REMARK 3 S11: -0.2519 S12: 0.6442 S13: 0.0532
REMARK 3 S21: 0.1491 S22: 0.4877 S23: 0.0976
REMARK 3 S31: 0.2280 S32: -0.0172 S33: -0.1609
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 290:378 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.9849 22.8915 5.2396
REMARK 3 T TENSOR
REMARK 3 T11: 0.6360 T22: 1.0766
REMARK 3 T33: 0.5662 T12: -0.3033
REMARK 3 T13: 0.1065 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 2.2487 L22: 2.5307
REMARK 3 L33: 0.5323 L12: 0.5489
REMARK 3 L13: -0.3334 L23: -0.5125
REMARK 3 S TENSOR
REMARK 3 S11: -0.1796 S12: 0.8483 S13: -0.6604
REMARK 3 S21: -0.2460 S22: 0.1540 S23: 0.1879
REMARK 3 S31: 0.4571 S32: -1.0938 S33: 0.0339
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 4OI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM16
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23117
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 22.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 44431.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL 8.5, 10% PEG4000, PH
REMARK 280 5.6, VAPOR DIFFUSION, TEMPERATURE 294K
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 23.45500
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLN A 263 CG CD OE1 NE2
REMARK 470 GLU A 264 CG CD OE1 OE2
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 CB CYS A 24 SG CYS A 68 1.65
REMARK 500 SG CYS A 28 CB CYS A 72 1.69
REMARK 500 CB CYS A 28 SG CYS A 72 1.71
REMARK 500 CB CYS A 313 SG CYS A 352 1.73
REMARK 500 ND2 ASN A 106 C2 NAG A 2304 1.75
REMARK 500 SG CYS A 313 CB CYS A 352 1.93
REMARK 500 ND2 ASN A 183 C2 NAG C 1 2.16
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 43 -74.22 -114.81
REMARK 500 PRO A 89 68.68 -69.91
REMARK 500 SER A 241 77.03 -118.67
REMARK 500 ALA A 261 -2.88 86.34
REMARK 500 GLN A 263 -140.59 58.93
REMARK 500 GLN A 318 -65.62 -95.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OIA RELATED DB: PDB
REMARK 900 RELATED ID: 4OIB RELATED DB: PDB
DBREF 4OI9 A 1 378 UNP Q9UMF0 ICAM5_HUMAN 32 409
SEQRES 1 A 378 GLU PRO PHE TRP ALA ASP LEU GLN PRO ARG VAL ALA PHE
SEQRES 2 A 378 VAL GLU ARG GLY GLY SER LEU TRP LEU ASN CYS SER THR
SEQRES 3 A 378 ASN CYS PRO ARG PRO GLU ARG GLY GLY LEU GLU THR SER
SEQRES 4 A 378 LEU ARG ARG ASN GLY THR GLN ARG GLY LEU ARG TRP LEU
SEQRES 5 A 378 ALA ARG GLN LEU VAL ASP ILE ARG GLU PRO GLU THR GLN
SEQRES 6 A 378 PRO VAL CYS PHE PHE ARG CYS ALA ARG ARG THR LEU GLN
SEQRES 7 A 378 ALA ARG GLY LEU ILE ARG THR PHE GLN ARG PRO ASP ARG
SEQRES 8 A 378 VAL GLU LEU MET PRO LEU PRO PRO TRP GLN PRO VAL GLY
SEQRES 9 A 378 GLU ASN PHE THR LEU SER CYS ARG VAL PRO GLY ALA GLY
SEQRES 10 A 378 PRO ARG ALA SER LEU THR LEU THR LEU LEU ARG GLY ALA
SEQRES 11 A 378 GLN GLU LEU ILE ARG ARG SER PHE ALA GLY GLU PRO PRO
SEQRES 12 A 378 ARG ALA ARG GLY ALA VAL LEU THR ALA THR VAL LEU ALA
SEQRES 13 A 378 ARG ARG GLU ASP HIS GLY ALA ASN PHE SER CYS ARG ALA
SEQRES 14 A 378 GLU LEU ASP LEU ARG PRO HIS GLY LEU GLY LEU PHE GLU
SEQRES 15 A 378 ASN SER SER ALA PRO ARG GLU LEU ARG THR PHE SER LEU
SEQRES 16 A 378 SER PRO ASP ALA PRO ARG LEU ALA ALA PRO ARG LEU LEU
SEQRES 17 A 378 GLU VAL GLY SER GLU ARG PRO VAL SER CYS THR LEU ASP
SEQRES 18 A 378 GLY LEU PHE PRO ALA SER GLU ALA ARG VAL TYR LEU ALA
SEQRES 19 A 378 LEU GLY ASP GLN ASN LEU SER PRO ASP VAL THR LEU GLU
SEQRES 20 A 378 GLY ASP ALA PHE VAL ALA THR ALA THR ALA THR ALA SER
SEQRES 21 A 378 ALA GLU GLN GLU GLY ALA ARG GLN LEU VAL CYS ASN VAL
SEQRES 22 A 378 THR LEU GLY GLY GLU ASN ARG GLU THR ARG GLU ASN VAL
SEQRES 23 A 378 THR ILE TYR SER PHE PRO ALA PRO LEU LEU THR LEU SER
SEQRES 24 A 378 GLU PRO SER VAL SER GLU GLY GLN MET VAL THR VAL THR
SEQRES 25 A 378 CYS ALA ALA GLY ALA GLN ALA LEU VAL THR LEU GLU GLY
SEQRES 26 A 378 VAL PRO ALA ALA VAL PRO GLY GLN PRO ALA GLN LEU GLN
SEQRES 27 A 378 LEU ASN ALA THR GLU ASN ASP ASP ARG ARG SER PHE PHE
SEQRES 28 A 378 CYS ASP ALA THR LEU ASP VAL ASP GLY GLU THR LEU ILE
SEQRES 29 A 378 LYS ASN ARG SER ALA GLU LEU ARG VAL LEU TYR ALA PRO
SEQRES 30 A 378 ARG
MODRES 4OI9 ASN A 43 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 106 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 285 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 164 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 340 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 23 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 183 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 272 ASN GLYCOSYLATION SITE
MODRES 4OI9 ASN A 366 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET NAG E 1 14
HET NAG E 2 14
HET NAG A2303 14
HET NAG A2304 14
HET NAG A2305 14
HET NAG A2312 14
HET NAG A2315 14
HET EDO A2316 4
HET EDO A2317 4
HET EDO A2318 4
HET EDO A2319 4
HET EDO A2320 4
HET EDO A2321 4
HET EDO A2322 4
HET EDO A2323 4
HET EDO A2324 4
HET EDO A2325 4
HET EDO A2326 4
HET EDO A2327 4
HET EDO A2328 4
HET EDO A2329 4
HET EDO A2330 4
HET EDO A2331 4
HET EDO A2332 4
HET EDO A2333 4
HET EDO A2334 4
HET EDO A2335 4
HET EDO A2336 4
HET EDO A2337 4
HET EDO A2338 4
HET EDO A2339 4
HET EDO A2340 4
HET EDO A2341 4
HET EDO A2342 4
HET EDO A2343 4
HET EDO A2344 4
HET EDO A2345 4
HET EDO A2346 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG 13(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN C6 H12 O6
FORMUL 11 EDO 31(C2 H6 O2)
FORMUL 42 HOH *97(H2 O)
HELIX 1 1 PRO A 118 ALA A 120 5 3
HELIX 2 2 ARG A 157 HIS A 161 5 5
HELIX 3 3 ARG A 174 GLY A 177 5 4
HELIX 4 4 PRO A 225 ALA A 229 5 5
HELIX 5 5 THR A 342 ASP A 346 5 5
SHEET 1 A 4 ALA A 5 GLN A 8 0
SHEET 2 A 4 GLY A 18 THR A 26 -1 O ASN A 23 N GLN A 8
SHEET 3 A 4 TRP A 51 ILE A 59 -1 O ARG A 54 N LEU A 22
SHEET 4 A 4 ARG A 41 ARG A 47 -1 N GLN A 46 O ALA A 53
SHEET 1 B 3 VAL A 11 GLU A 15 0
SHEET 2 B 3 LEU A 82 PHE A 86 1 O ARG A 84 N ALA A 12
SHEET 3 B 3 GLU A 63 THR A 64 -1 N THR A 64 O ILE A 83
SHEET 1 C 3 PRO A 31 GLU A 37 0
SHEET 2 C 3 VAL A 67 CYS A 72 -1 O ARG A 71 N GLU A 32
SHEET 3 C 3 ARG A 75 ARG A 80 -1 O LEU A 77 N PHE A 70
SHEET 1 D 3 GLU A 93 LEU A 94 0
SHEET 2 D 3 ASN A 106 VAL A 113 -1 O ARG A 112 N GLU A 93
SHEET 3 D 3 ALA A 148 LEU A 155 -1 O LEU A 150 N CYS A 111
SHEET 1 E 3 GLN A 101 PRO A 102 0
SHEET 2 E 3 THR A 192 LEU A 195 1 O PHE A 193 N GLN A 101
SHEET 3 E 3 LEU A 223 PHE A 224 -1 O PHE A 224 N SER A 194
SHEET 1 F 4 GLN A 131 SER A 137 0
SHEET 2 F 4 LEU A 122 ARG A 128 -1 N LEU A 124 O ARG A 136
SHEET 3 F 4 PHE A 165 ASP A 172 -1 O SER A 166 N LEU A 127
SHEET 4 F 4 LEU A 180 SER A 184 -1 O PHE A 181 N LEU A 171
SHEET 1 G 4 ARG A 201 ALA A 203 0
SHEET 2 G 4 ARG A 214 LEU A 220 -1 O SER A 217 N ALA A 203
SHEET 3 G 4 ALA A 250 ALA A 257 -1 O ALA A 253 N CYS A 218
SHEET 4 G 4 ASP A 243 GLU A 247 -1 N GLU A 247 O ALA A 250
SHEET 1 H 5 LEU A 207 GLU A 209 0
SHEET 2 H 5 GLU A 278 TYR A 289 1 O THR A 287 N LEU A 208
SHEET 3 H 5 GLY A 265 LEU A 275 -1 N GLY A 265 O ILE A 288
SHEET 4 H 5 ARG A 230 LEU A 235 -1 N TYR A 232 O ASN A 272
SHEET 5 H 5 ASN A 239 LEU A 240 -1 O LEU A 240 N LEU A 233
SHEET 1 I 3 LEU A 295 LEU A 298 0
SHEET 2 I 3 MET A 308 ALA A 314 -1 O ALA A 314 N LEU A 295
SHEET 3 I 3 ALA A 335 ASN A 340 -1 O LEU A 339 N VAL A 309
SHEET 1 J 5 SER A 302 SER A 304 0
SHEET 2 J 5 GLU A 361 LEU A 374 1 O ARG A 372 N VAL A 303
SHEET 3 J 5 ARG A 348 VAL A 358 -1 N LEU A 356 O LEU A 363
SHEET 4 J 5 LEU A 320 LEU A 323 -1 N THR A 322 O ASP A 353
SHEET 5 J 5 VAL A 326 PRO A 327 -1 O VAL A 326 N LEU A 323
SSBOND 1 CYS A 24 CYS A 68 1555 1555 2.02
SSBOND 2 CYS A 28 CYS A 72 1555 1555 2.02
SSBOND 3 CYS A 111 CYS A 167 1555 1555 2.03
SSBOND 4 CYS A 218 CYS A 271 1555 1555 2.04
SSBOND 5 CYS A 313 CYS A 352 1555 1555 2.00
LINK ND2 ASN A 23 C1 NAG B 1 1555 1555 1.44
LINK ND2 ASN A 43 C1 NAG A2303 1555 1555 1.43
LINK ND2 ASN A 106 C1 NAG A2304 1555 1555 1.44
LINK ND2 ASN A 164 C1 NAG A2305 1555 1555 1.44
LINK ND2 ASN A 183 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 272 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 285 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 340 C1 NAG A2312 1555 1555 1.44
LINK ND2 ASN A 366 C1 NAG A2315 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
CISPEP 1 GLN A 8 PRO A 9 0 -6.56
CISPEP 2 GLY A 117 PRO A 118 0 -2.69
CISPEP 3 PHE A 224 PRO A 225 0 -19.56
CISPEP 4 GLN A 263 GLU A 264 0 -5.49
CISPEP 5 ALA A 329 VAL A 330 0 0.05
CRYST1 76.590 46.910 95.790 90.00 104.34 90.00 P 1 21 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 0.013057 0.000000 0.003338 0.00000
SCALE2 0.000000 0.021317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010775 0.00000
(ATOM LINES ARE NOT SHOWN.)
END