HEADER IMMUNE SYSTEM 24-OCT-01 1K8I
TITLE CRYSTAL STRUCTURE OF MOUSE H2-DM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS II H2-M ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MHC CLASS II H2-M BETA 2 CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: H2-DM;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HIGH-FIVE;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: H2-DM;
SOURCE 16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HIGH-FIVE;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS MHC, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.FREMONT,F.CRAWFORD,P.MARRACK,W.HENDRICKSON,J.KAPPLER
REVDAT 5 29-JUL-20 1K8I 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 13-JUL-11 1K8I 1 VERSN
REVDAT 3 24-FEB-09 1K8I 1 VERSN
REVDAT 2 01-APR-03 1K8I 1 JRNL
REVDAT 1 05-DEC-01 1K8I 0
JRNL AUTH D.H.FREMONT,F.CRAWFORD,P.MARRACK,W.A.HENDRICKSON,J.KAPPLER
JRNL TITL CRYSTAL STRUCTURE OF MOUSE H2-M.
JRNL REF IMMUNITY V. 9 385 1998
JRNL REFN ISSN 1074-7613
JRNL PMID 9768758
JRNL DOI 10.1016/S1074-7613(00)80621-4
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0100
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 13711
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) : 0.205
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 690
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1225
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 78
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.038
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2934
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 74.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.46000
REMARK 3 B22 (A**2) : -1.46000
REMARK 3 B33 (A**2) : 2.92000
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) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.67
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) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.79
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.260
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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM3_MOD.CHO
REMARK 3 PARAMETER FILE 3 : PARAMCSDX.MISC
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH3.CHO
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014692.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-98
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13711
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 4.560
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09100
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) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.710
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR,MIR
REMARK 200 SOFTWARE USED: AMORE, X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LITHIUM SULFATE, 0.1M MES, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 71.35000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.35000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 38.45000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 71.35000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.35000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.45000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 71.35000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 71.35000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 38.45000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 71.35000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 71.35000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 38.45000
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: 5700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ALA A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 VAL A 5
REMARK 465 PHE A 6
REMARK 465 TRP A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 PRO A 10
REMARK 465 GLY B 191
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 PRO A 167 C - N - CA ANGL. DEV. = 9.7 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 ILE A 25 -107.71 36.02
REMARK 500 GLU A 36 -19.53 75.95
REMARK 500 ALA A 57 -68.71 11.01
REMARK 500 GLN A 63 -32.91 69.67
REMARK 500 PRO A 126 77.14 -69.48
REMARK 500 SER A 136 -21.12 70.64
REMARK 500 PRO A 167 -30.98 -34.52
REMARK 500 LEU A 170 89.70 -162.51
REMARK 500 GLU A 178 59.34 38.04
REMARK 500 ILE A 179 -72.58 65.87
REMARK 500 TYR A 182 115.66 89.97
REMARK 500 PRO A 190 99.89 -66.63
REMARK 500 ALA B 15 -62.35 76.45
REMARK 500 ASN B 28 -156.75 57.36
REMARK 500 LEU B 32 -76.20 -96.67
REMARK 500 CYS B 45 -139.73 -133.95
REMARK 500 GLU B 46 84.01 -11.26
REMARK 500 GLU B 63 45.15 -77.99
REMARK 500 GLN B 83 -64.25 -29.80
REMARK 500 PHE B 106 -115.76 -82.20
REMARK 500 THR B 108 160.31 99.25
REMARK 500 PRO B 123 -169.59 -72.75
REMARK 500 HIS B 140 100.26 -163.44
REMARK 500 GLU B 144 -104.61 -104.41
REMARK 500 LYS B 145 -151.49 173.80
REMARK 500 ALA B 147 100.35 9.79
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K8I A 1 191 UNP P28078 2DMA_MOUSE 30 220
DBREF 1K8I B 1 191 UNP Q31099 Q31099_MOUSE 20 210
SEQRES 1 A 191 ALA SER THR PRO VAL PHE TRP ASP ASP PRO GLN ASN HIS
SEQRES 2 A 191 THR PHE ARG HIS THR LEU PHE CYS GLN ASP GLY ILE PRO
SEQRES 3 A 191 ASN ILE GLY LEU SER GLU THR TYR ASP GLU ASP GLU LEU
SEQRES 4 A 191 PHE SER PHE ASP PHE SER GLN ASN THR ARG VAL PRO ARG
SEQRES 5 A 191 LEU PRO ASP PHE ALA GLU TRP ALA GLN GLY GLN GLY ASP
SEQRES 6 A 191 ALA SER ALA ILE ALA PHE ASP LYS SER PHE CYS GLU MET
SEQRES 7 A 191 LEU MET ARG GLU VAL SER PRO LYS LEU GLU GLY GLN ILE
SEQRES 8 A 191 PRO VAL SER ARG GLY LEU PRO VAL ALA GLU VAL PHE THR
SEQRES 9 A 191 LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN THR LEU VAL
SEQRES 10 A 191 CYS PHE ILE SER ASN LEU PHE PRO PRO THR LEU THR VAL
SEQRES 11 A 191 ASN TRP GLN LEU HIS SER ALA PRO VAL GLU GLY ALA SER
SEQRES 12 A 191 PRO THR SER ILE SER ALA VAL ASP GLY LEU THR PHE GLN
SEQRES 13 A 191 ALA PHE SER TYR LEU ASN PHE THR PRO GLU PRO PHE ASP
SEQRES 14 A 191 LEU TYR SER CYS THR VAL THR HIS GLU ILE ASP ARG TYR
SEQRES 15 A 191 THR ALA ILE ALA TYR TRP VAL PRO GLN
SEQRES 1 B 191 GLY PHE VAL ALA HIS VAL GLU SER THR CYS VAL LEU ASN
SEQRES 2 B 191 ASP ALA GLY THR PRO GLN ASP PHE THR TYR CYS VAL SER
SEQRES 3 B 191 PHE ASN LYS ASP LEU LEU ALA CYS TRP ASP PRO ASP VAL
SEQRES 4 B 191 GLY LYS ILE VAL PRO CYS GLU PHE GLY VAL LEU SER ARG
SEQRES 5 B 191 LEU ALA GLU ILE ILE SER ASN ILE LEU ASN GLU GLN GLU
SEQRES 6 B 191 SER LEU ILE HIS ARG LEU GLN ASN GLY LEU GLN ASP CYS
SEQRES 7 B 191 ALA THR HIS THR GLN PRO PHE TRP ASP VAL LEU THR HIS
SEQRES 8 B 191 ARG THR ARG ALA PRO SER VAL ARG VAL ALA GLN THR THR
SEQRES 9 B 191 PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS TYR
SEQRES 10 B 191 VAL TRP GLY PHE TYR PRO ALA ASP VAL THR ILE THR TRP
SEQRES 11 B 191 MET LYS ASN GLY GLN LEU VAL PRO SER HIS SER ASN LYS
SEQRES 12 B 191 GLU LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR GLN
SEQRES 13 B 191 THR VAL SER TYR LEU ALA LEU THR PRO SER TYR GLY ASP
SEQRES 14 B 191 VAL TYR THR CYS VAL VAL GLN HIS SER GLY THR SER GLU
SEQRES 15 B 191 PRO ILE ARG GLY ASP TRP THR PRO GLY
MODRES 1K8I ASN A 12 ASN GLYCOSYLATION SITE
MODRES 1K8I ASN A 162 ASN GLYCOSYLATION SITE
HET NAG A 192 14
HET NAG A 193 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 3 NAG 2(C8 H15 N O6)
HELIX 1 1 ALA A 57 GLY A 62 1 6
HELIX 2 2 ASP A 65 GLU A 82 1 18
HELIX 3 3 GLU A 82 GLU A 88 1 7
HELIX 4 4 LEU B 50 GLU B 63 1 14
HELIX 5 5 GLN B 64 GLY B 74 1 11
HELIX 6 6 GLY B 74 HIS B 91 1 18
SHEET 1 A 6 THR A 48 PRO A 51 0
SHEET 2 A 6 ASP A 37 ASP A 43 -1 N ASP A 43 O THR A 48
SHEET 3 A 6 ILE A 28 TYR A 34 -1 N GLU A 32 O LEU A 39
SHEET 4 A 6 ASN A 12 GLN A 22 -1 N PHE A 20 O GLY A 29
SHEET 5 A 6 VAL B 3 ASN B 13 -1 O CYS B 10 N PHE A 15
SHEET 6 A 6 PRO B 18 PHE B 21 -1 O GLN B 19 N VAL B 11
SHEET 1 B 8 THR A 48 PRO A 51 0
SHEET 2 B 8 ASP A 37 ASP A 43 -1 N ASP A 43 O THR A 48
SHEET 3 B 8 ILE A 28 TYR A 34 -1 N GLU A 32 O LEU A 39
SHEET 4 B 8 ASN A 12 GLN A 22 -1 N PHE A 20 O GLY A 29
SHEET 5 B 8 VAL B 3 ASN B 13 -1 O CYS B 10 N PHE A 15
SHEET 6 B 8 CYS B 24 PHE B 27 -1 O CYS B 24 N GLU B 7
SHEET 7 B 8 ALA B 33 ASP B 36 -1 O ALA B 33 N VAL B 25
SHEET 8 B 8 LYS B 41 PRO B 44 -1 O VAL B 43 N CYS B 34
SHEET 1 C 4 VAL A 99 THR A 104 0
SHEET 2 C 4 ASN A 114 LEU A 123 -1 O SER A 121 N VAL A 99
SHEET 3 C 4 THR A 154 PHE A 163 -1 O LEU A 161 N LEU A 116
SHEET 4 C 4 SER A 146 VAL A 150 -1 N VAL A 150 O THR A 154
SHEET 1 D 4 ALA A 137 VAL A 139 0
SHEET 2 D 4 LEU A 128 LEU A 134 -1 N LEU A 134 O ALA A 137
SHEET 3 D 4 TYR A 171 HIS A 177 -1 O THR A 174 N ASN A 131
SHEET 4 D 4 THR A 183 TRP A 188 -1 O ALA A 184 N VAL A 175
SHEET 1 E 4 SER B 97 THR B 103 0
SHEET 2 E 4 VAL B 112 PHE B 121 -1 O ALA B 115 N ALA B 101
SHEET 3 E 4 TYR B 155 LEU B 163 -1 O LEU B 161 N LEU B 114
SHEET 4 E 4 GLN B 148 PRO B 149 -1 N GLN B 148 O GLN B 156
SHEET 1 F 4 GLN B 135 LEU B 136 0
SHEET 2 F 4 VAL B 126 LYS B 132 -1 N LYS B 132 O GLN B 135
SHEET 3 F 4 TYR B 171 HIS B 177 -1 O VAL B 174 N THR B 129
SHEET 4 F 4 THR B 180 TRP B 188 -1 O TRP B 188 N TYR B 171
SSBOND 1 CYS A 21 CYS A 76 1555 1555 2.03
SSBOND 2 CYS A 118 CYS A 173 1555 1555 2.01
SSBOND 3 CYS B 10 CYS B 78 1555 1555 2.03
SSBOND 4 CYS B 24 CYS B 34 1555 1555 2.04
SSBOND 5 CYS B 116 CYS B 173 1555 1555 2.03
LINK ND2 ASN A 12 C1 NAG A 192 1555 1555 1.46
LINK ND2 ASN A 162 C1 NAG A 193 1555 1555 1.46
CISPEP 1 PHE A 124 PRO A 125 0 0.10
CISPEP 2 TYR B 122 PRO B 123 0 -0.07
CRYST1 142.700 142.700 76.900 90.00 90.00 90.00 I 4 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 0.007008 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013004 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
