HEADER MEMBRANE PROTEIN 31-JAN-08 3C5J
TITLE CRYSTAL STRUCTURE OF HLA DR52C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 25-206;
COMPND 5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MHC CLASS II ANTIGEN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 30-219;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: ELONGATION FACTOR 1-ALPHA 2;
COMPND 14 CHAIN: C;
COMPND 15 FRAGMENT: UNP RESIDUES 343-355;
COMPND 16 SYNONYM: EF-1-ALPHA-2, ELONGATION FACTOR 1 A-2, EEF1A-2, STATIN S1;
COMPND 17 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: HLA-DRA, HLA-DRA1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HLA-DRB3;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: EEF1A2, EEF1AL, STN;
SOURCE 26 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 27 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 29 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HLA, MHC CLASS II, GLYCOPROTEIN, IMMUNE RESPONSE, MEMBRANE, MHC II,
KEYWDS 2 TRANSMEMBRANE, ELONGATION FACTOR, GTP-BINDING, METHYLATION,
KEYWDS 3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, PROTEIN BIOSYNTHESIS,
KEYWDS 4 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DAI,J.W.KAPPLER
REVDAT 7 29-JUL-20 3C5J 1 COMPND REMARK HETNAM LINK
REVDAT 7 2 1 SITE
REVDAT 6 25-OCT-17 3C5J 1 REMARK
REVDAT 5 13-JUL-11 3C5J 1 VERSN
REVDAT 4 09-JUN-09 3C5J 1 REVDAT
REVDAT 3 24-FEB-09 3C5J 1 VERSN
REVDAT 2 02-DEC-08 3C5J 1 JRNL
REVDAT 1 05-AUG-08 3C5J 0
JRNL AUTH S.DAI,F.CRAWFORD,P.MARRACK,J.W.KAPPLER
JRNL TITL THE STRUCTURE OF HLA-DR52C: COMPARISON TO OTHER HLA-DRB3
JRNL TITL 2 ALLELES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 11893 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18697946
JRNL DOI 10.1073/PNAS.0805810105
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2282868.250
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 42672
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 SET) : 0.202
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2141
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6084
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 351
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.37000
REMARK 3 B22 (A**2) : 1.37000
REMARK 3 B33 (A**2) : -2.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 66.17
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : &_1_TOPOLOGY_INFILE_1
REMARK 3 TOPOLOGY FILE 2 : &_1_TOPOLOGY_INFILE_2
REMARK 3 TOPOLOGY FILE 3 : &_1_TOPOLOGY_INFILE_3
REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3C5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
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 : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42787
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.45500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 99.68250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.22750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.45500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.22750
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 99.68250
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: 7400 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17090 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 BIOMT1 2 0.000000 -1.000000 0.000000 83.38000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 83.38000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 99.68250
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 ILE A 1
REMARK 465 LYS A 2
REMARK 465 ASP A 181
REMARK 465 GLY B 1
REMARK 465 ASP B 2
REMARK 465 THR B 3
REMARK 465 THR B 106
REMARK 465 GLN B 107
REMARK 465 PRO B 108
REMARK 465 LEU B 109
REMARK 465 GLN B 110
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 GLU A 4 -41.75 -131.58
REMARK 500 TYR A 79 29.50 47.96
REMARK 500 THR A 113 146.50 -171.68
REMARK 500 GLN B 34 -5.86 76.98
REMARK 500 THR B 90 -71.61 -130.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN C AND CHAIN B ARE FUSED TOGETHER
REMARK 999 THROUGH A LINKER ( GGGGSLVPRGSGGGGS ). HOWEVER THIS LINKER IS
REMARK 999 DISORDERED
DBREF 3C5J A 1 181 UNP P01903 2DRA_HUMAN 26 206
DBREF 3C5J B 1 190 UNP Q6YJU6 Q6YJU6_HUMAN 30 219
DBREF 3C5J C 1 13 UNP Q05639 EF1A2_HUMAN 343 355
SEQRES 1 A 181 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 181 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 181 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 181 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 181 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 181 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 181 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 181 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 181 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 181 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 181 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 181 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 181 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 181 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES 1 B 190 GLY ASP THR ARG PRO ARG PHE LEU GLU LEU LEU LYS SER
SEQRES 2 B 190 GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE
SEQRES 3 B 190 LEU GLU ARG TYR PHE HIS ASN GLN GLU GLU PHE VAL ARG
SEQRES 4 B 190 PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES 5 B 190 LEU GLY ARG PRO VAL ALA GLU SER TRP ASN SER GLN LYS
SEQRES 6 B 190 ASP LEU LEU GLU GLN LYS ARG GLY GLN VAL ASP ASN TYR
SEQRES 7 B 190 CYS ARG HIS ASN TYR GLY VAL VAL GLU SER PHE THR VAL
SEQRES 8 B 190 GLN ARG ARG VAL HIS PRO GLN VAL THR VAL TYR PRO ALA
SEQRES 9 B 190 LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES 10 B 190 SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES 11 B 190 TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY VAL VAL
SEQRES 12 B 190 SER THR GLY LEU ILE HIS ASN GLY ASP TRP THR PHE GLN
SEQRES 13 B 190 THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES 14 B 190 VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES 15 B 190 PRO LEU THR VAL GLU TRP ARG ALA
SEQRES 1 C 13 GLN VAL ILE ILE LEU ASN HIS PRO GLY GLN ILE SER ALA
MODRES 3C5J ASN A 118 ASN GLYCOSYLATION SITE
MODRES 3C5J ASN B 19 ASN GLYCOSYLATION SITE
HET NAG A 182 14
HET NAG B 191 14
HET SO4 B 192 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 6 SO4 O4 S 2-
FORMUL 7 HOH *454(H2 O)
HELIX 1 1 LEU A 45 PHE A 51 5 7
HELIX 2 2 GLU A 55 SER A 77 1 23
HELIX 3 3 THR B 51 LEU B 53 5 3
HELIX 4 4 GLY B 54 SER B 63 1 10
HELIX 5 5 GLN B 64 ARG B 72 1 9
HELIX 6 6 GLY B 73 TYR B 78 1 6
HELIX 7 7 TYR B 78 GLU B 87 1 10
HELIX 8 8 SER B 88 THR B 90 5 3
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 N HIS A 33 O VAL A 42
SHEET 3 A 8 SER A 19 PHE A 26 -1 N PHE A 26 O ASP A 29
SHEET 4 A 8 HIS A 5 ASN A 15 -1 N ILE A 8 O ASP A 25
SHEET 5 A 8 PHE B 7 PHE B 18 -1 O PHE B 17 N HIS A 5
SHEET 6 A 8 ARG B 23 HIS B 32 -1 O LEU B 27 N GLU B 14
SHEET 7 A 8 GLU B 35 ASP B 41 -1 O PHE B 40 N GLU B 28
SHEET 8 A 8 TYR B 47 ALA B 49 -1 O ARG B 48 N ARG B 39
SHEET 1 B 4 GLU A 88 THR A 93 0
SHEET 2 B 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 B 4 PHE A 145 PHE A 153 -1 O LYS A 147 N ILE A 109
SHEET 4 B 4 SER A 133 GLU A 134 -1 N SER A 133 O TYR A 150
SHEET 1 C 4 GLU A 88 THR A 93 0
SHEET 2 C 4 ASN A 103 PHE A 112 -1 O ILE A 106 N LEU A 92
SHEET 3 C 4 PHE A 145 PHE A 153 -1 O LYS A 147 N ILE A 109
SHEET 4 C 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 D 4 LYS A 126 VAL A 128 0
SHEET 2 D 4 ASN A 118 ARG A 123 -1 N TRP A 121 O VAL A 128
SHEET 3 D 4 VAL A 160 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 D 4 LEU A 174 GLU A 179 -1 O LEU A 174 N VAL A 165
SHEET 1 E 4 GLN B 98 ALA B 104 0
SHEET 2 E 4 LEU B 114 PHE B 122 -1 O SER B 118 N THR B 100
SHEET 3 E 4 PHE B 155 LEU B 161 -1 O VAL B 159 N CYS B 117
SHEET 4 E 4 VAL B 142 SER B 144 -1 N VAL B 143 O MET B 160
SHEET 1 F 4 GLN B 98 ALA B 104 0
SHEET 2 F 4 LEU B 114 PHE B 122 -1 O SER B 118 N THR B 100
SHEET 3 F 4 PHE B 155 LEU B 161 -1 O VAL B 159 N CYS B 117
SHEET 4 F 4 ILE B 148 HIS B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 G 4 GLN B 136 GLU B 137 0
SHEET 2 G 4 GLU B 128 ARG B 133 -1 N ARG B 133 O GLN B 136
SHEET 3 G 4 VAL B 170 GLU B 176 -1 O GLN B 174 N ARG B 130
SHEET 4 G 4 LEU B 184 ARG B 189 -1 O TRP B 188 N TYR B 171
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.67
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.02
LINK ND2 ASN A 118 C1 NAG A 182 1555 1555 1.45
LINK ND2 ASN B 19 C1 NAG B 191 1555 1555 1.45
CISPEP 1 ASN A 15 PRO A 16 0 -0.17
CISPEP 2 THR A 113 PRO A 114 0 0.04
CISPEP 3 TYR B 123 PRO B 124 0 0.29
CRYST1 83.380 83.380 132.910 90.00 90.00 90.00 P 43 2 2 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 0.011993 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007524 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
