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1MHC.pdb
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HEADER HISTOCOMPATIBILITY ANTIGEN/PEPTIDE 23-AUG-95 1MHC
TITLE MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT
TITLE 2 2.3 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS I ANTIGEN H2-M3;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: MAJOR HISTOCOMPATIBILITY COMPLEX;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MHC CLASS I ANTIGEN H2-M3;
COMPND 9 CHAIN: B, E;
COMPND 10 SYNONYM: MAJOR HISTOCOMPATIBILITY COMPLEX;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: NONAPEPTIDE FROM RAT NADH DEHYDROGENASE;
COMPND 15 CHAIN: C, F;
COMPND 16 SYNONYM: ND1;
COMPND 17 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-M3 B2M;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM_GENE: H2-M3 B2M;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 GENE: H2-M3 B2M;
SOURCE 15 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 18 EXPRESSION_SYSTEM_GENE: H2-M3 B2M;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: RATTUS RATTUS;
SOURCE 21 ORGANISM_COMMON: BLACK RAT;
SOURCE 22 ORGANISM_TAXID: 10117
KEYWDS HISTOCOMPATIBILITY ANTIGEN/PEPTIDE, HISTOCOMPATIBILITY ANTIGEN-
KEYWDS 2 PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-R.WANG,K.FISCHER LINDAHL,J.DEISENHOFER
REVDAT 4 13-JUL-11 1MHC 1 VERSN
REVDAT 3 24-FEB-09 1MHC 1 VERSN
REVDAT 2 01-APR-03 1MHC 1 JRNL
REVDAT 1 29-JAN-96 1MHC 0
JRNL AUTH C.R.WANG,A.R.CASTANO,P.A.PETERSON,C.SLAUGHTER,K.F.LINDAHL,
JRNL AUTH 2 J.DEISENHOFER
JRNL TITL NONCLASSICAL BINDING OF FORMYLATED PEPTIDE IN CRYSTAL
JRNL TITL 2 STRUCTURE OF THE MHC CLASS IB MOLECULE H2-M3
JRNL REF CELL(CAMBRIDGE,MASS.) V. 82 655 1995
JRNL REFN ISSN 0092-8674
JRNL PMID 7664344
JRNL DOI 10.1016/0092-8674(95)90037-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.-R.WANG,B.E.LOVELAND,K.FISCHER LINDAHL
REMARK 1 TITL H-2M3 ENCODES THE MHC CLASS I MOLECULE PRESENTING THE
REMARK 1 TITL 2 MATERNALLY TRANSMITTED ANTIGEN OF THE MOUSE
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 66 335 1991
REMARK 1 REFN ISSN 0092-8674
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 70.0
REMARK 3 NUMBER OF REFLECTIONS : 33706
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 6282
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 372
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.88
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MHC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33706
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 70.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07900
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
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, 3
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 300 REMARK: MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX RESIDUES RESIDUES RMSD
REMARK 300 M1 D 2 .. D 182 A 2 .. A 182 0.288
REMARK 300 M2 D 183 .. D 275 A 183 .. A 275 0.292
REMARK 300 M3 E 1 .. E 99 B 1 .. B 99 0.312
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: 4330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -36.40172
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -46.88616
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -52.70407
REMARK 410
REMARK 410 IMGT/3Dstructure-DB annotations
REMARK 410 (http://www.imgt.org)
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 H2-M3
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1mhc_A,1mhc_B
REMARK 410
REMARK 410 ligand(s)
REMARK 410 NADH deshydrogenase peptide
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Rattus norvegicus (Norway rat)
REMARK 410 Chain ID
REMARK 410 1mhc_F
REMARK 410
REMARK 410 ligand(s)
REMARK 410 NADH deshydrogenase peptide
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Rattus norvegicus (Norway rat)
REMARK 410 Chain ID
REMARK 410 1mhc_C
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 H2-M3
REMARK 410 IMGT receptor type
REMARK 410 MH
REMARK 410 IMGT receptor description
REMARK 410 MH1-ALPHA_B2M
REMARK 410 Species
REMARK 410 Mus musculus (house mouse)
REMARK 410 Chain ID
REMARK 410 1mhc_D,1mhc_E
REMARK 410
REMARK 410
REMARK 410 Chain ID 1mhc_A (1MHCA)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GSHSLRYFHTAVSRPGRGEPQYISVGYVDDVQFQRCDSIEEIPRMEPRAPWMEKERPEYWKELKLK
REMARK 410 ][ G-ALPHA
REMARK 410 VKNIAQSARANLRTLLRYYNQSEGGSHILQWMVSCEVGPDMRLLGAHYQAAYDGSDYITLNEDLSS
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAVDMVSQITKSRLESAGTAEYFRAYVEGECLELLHRFLRNGKEILQRADPPKAHVAHHPRPKGD
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQKDEEDLTQDMELVETRPSGDGTFQKWAAVVVPSGEEQRYTCYVHHE
REMARK 410 ]
REMARK 410 GLTEPLALKWRSHHHHHH
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-M3 (100%)
REMARK 410 G-DOMAIN ..........GSHSLRY.FHTAVSRPGRGEPQYISVGYVDDVQFQRCDSIEE
REMARK 410 G-DOMAIN IPRMEPRA.......PWMEKERPEYWKELKLKVKNIAQSARANLRTLLRYYN
REMARK 410 G-DOMAIN QSEG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-M3 (100%)
REMARK 410 G-DOMAIN ..........GSHILQWMVSCEVGPDMRLLGAHYQAAYDGSDYITLNED..L
REMARK 410 G-DOMAIN SSWTAVD.......MVSQITKSRLESA.GTAEYFRAYVEGECLELLHRFLRN
REMARK 410 G-DOMAIN GKEILQRA.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus H2-M3 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DPPKAHVAHHPRPK......GDVTLRCWALGFYP..ADITLTWQK
REMARK 410 C-LIKE-DOMAIN DEEDLTQ..DMELVETRPSGD......GTFQKWAAVVVPSG.....EEQRYT
REMARK 410 C-LIKE-DOMAIN CYVHHEG..LTEPLALKW
REMARK 410
REMARK 410 Chain ID 1mhc_B (1MHCB)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
REMARK 410
REMARK 410 Chain ID 1mhc_D (1MHCD)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GSHSLRYFHTAVSRPGRGEPQYISVGYVDDVQFQRCDSIEEIPRMEPRAPWMEKERPEYWKELKLK
REMARK 410 ][ G-ALPHA
REMARK 410 VKNIAQSARANLRTLLRYYNQSEGGSHILQWMVSCEVGPDMRLLGAHYQAAYDGSDYITLNEDLSS
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAVDMVSQITKSRLESAGTAEYFRAYVEGECLELLHRFLRNGKEILQRADPPKAHVAHHPRPKGD
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQKDEEDLTQDMELVETRPSGDGTFQKWAAVVVPSGEEQRYTCYVHHE
REMARK 410 ]
REMARK 410 GLTEPLALKWRSHHHHHH
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-M3 (100%)
REMARK 410 G-DOMAIN ..........GSHSLRY.FHTAVSRPGRGEPQYISVGYVDDVQFQRCDSIEE
REMARK 410 G-DOMAIN IPRMEPRA.......PWMEKERPEYWKELKLKVKNIAQSARANLRTLLRYYN
REMARK 410 G-DOMAIN QSEG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus H2-M3 (100%)
REMARK 410 G-DOMAIN ..........GSHILQWMVSCEVGPDMRLLGAHYQAAYDGSDYITLNED..L
REMARK 410 G-DOMAIN SSWTAVD.......MVSQITKSRLESA.GTAEYFRAYVEGECLELLHRFLRN
REMARK 410 G-DOMAIN GKEILQRA.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus H2-M3 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DPPKAHVAHHPRPK......GDVTLRCWALGFYP..ADITLTWQK
REMARK 410 C-LIKE-DOMAIN DEEDLTQ..DMELVETRPSGD......GTFQKWAAVVVPSG.....EEQRYT
REMARK 410 C-LIKE-DOMAIN CYVHHEG..LTEPLALKW
REMARK 410
REMARK 410 Chain ID 1mhc_E (1MHCE)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (1-99) [D1]
REMARK 410 IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILA
REMARK 410 ]
REMARK 410 HTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus B2M*01 (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .....IQKTPQIQVYSRHPPEN....GKPNILNCYVTQFHP..PHIEIQMLK
REMARK 410 C-LIKE-DOMAIN NGKKIP...KVEMSDMSFSKD......WSFYILAHTEFTPTE.....TDTYA
REMARK 410 C-LIKE-DOMAIN CRVKHDS..MAEPKTVYWDRDM
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 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS D 277
REMARK 465 HIS D 278
REMARK 465 HIS D 279
REMARK 465 HIS D 280
REMARK 465 HIS D 281
REMARK 465 HIS D 282
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 SER A 2 112.19 80.07
REMARK 500 ASP A 29 -124.51 61.11
REMARK 500 SER A 38 95.63 -167.27
REMARK 500 GLU A 41 8.10 88.35
REMARK 500 TRP A 51 -2.75 -53.95
REMARK 500 PRO A 57 -13.37 -44.32
REMARK 500 MET A 107 18.82 57.82
REMARK 500 ASP A 122 153.33 -45.80
REMARK 500 TYR A 123 -56.53 -136.31
REMARK 500 SER A 131 -22.92 -147.92
REMARK 500 ASP A 137 -177.06 -172.52
REMARK 500 LYS A 176 -64.25 -26.71
REMARK 500 GLN A 180 41.44 -101.82
REMARK 500 ALA A 182 96.39 -164.26
REMARK 500 PRO A 210 -179.97 -65.88
REMARK 500 ASP A 220 -86.40 64.26
REMARK 500 GLU A 221 20.46 -147.04
REMARK 500 HIS B 31 132.52 -173.28
REMARK 500 TRP B 60 -5.06 68.34
REMARK 500 ASN C 5 97.51 -65.86
REMARK 500 THR C 8 19.49 51.45
REMARK 500 ASP D 29 -120.17 58.81
REMARK 500 SER D 38 107.70 -166.91
REMARK 500 TRP D 51 -5.63 -56.29
REMARK 500 TYR D 123 -61.88 -125.98
REMARK 500 GLN D 180 43.10 -99.96
REMARK 500 ASP D 220 -116.09 62.69
REMARK 500 GLU D 221 50.58 -117.18
REMARK 500 PRO E 20 157.73 -46.13
REMARK 500 ASN E 21 -178.87 -170.27
REMARK 500 TRP E 60 -1.54 72.75
REMARK 500 THR E 75 -70.38 -92.85
REMARK 500 ASP E 76 137.99 -29.77
REMARK 500 LEU F 7 -52.72 78.28
REMARK 500 THR F 8 -76.07 178.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 209 0.08 SIDE CHAIN
REMARK 500 TYR D 7 0.07 SIDE CHAIN
REMARK 500 TYR F 2 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 89 24.5 L L OUTSIDE RANGE
REMARK 500 GLU D 41 22.4 L L OUTSIDE RANGE
REMARK 500 ASN F 5 23.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 335 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH A 356 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B 100 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH D 501 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH D 526 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH D 553 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH D 582 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH D 593 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH D 621 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH D 624 DISTANCE = 5.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 500
DBREF 1MHC A 1 276 UNP Q31093 Q31093_MOUSE 25 298
DBREF 1MHC B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1MHC C 1 9 UNP P03889 NU1M_RAT 1 9
DBREF 1MHC D 1 276 UNP Q31093 Q31093_MOUSE 25 298
DBREF 1MHC E 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1MHC F 1 9 UNP P03889 NU1M_RAT 1 9
SEQADV 1MHC A UNP Q31093 GLY 299 DELETION
SEQADV 1MHC D UNP Q31093 GLY 299 DELETION
SEQRES 1 A 282 GLY SER HIS SER LEU ARG TYR PHE HIS THR ALA VAL SER
SEQRES 2 A 282 ARG PRO GLY ARG GLY GLU PRO GLN TYR ILE SER VAL GLY
SEQRES 3 A 282 TYR VAL ASP ASP VAL GLN PHE GLN ARG CYS ASP SER ILE
SEQRES 4 A 282 GLU GLU ILE PRO ARG MET GLU PRO ARG ALA PRO TRP MET
SEQRES 5 A 282 GLU LYS GLU ARG PRO GLU TYR TRP LYS GLU LEU LYS LEU
SEQRES 6 A 282 LYS VAL LYS ASN ILE ALA GLN SER ALA ARG ALA ASN LEU
SEQRES 7 A 282 ARG THR LEU LEU ARG TYR TYR ASN GLN SER GLU GLY GLY
SEQRES 8 A 282 SER HIS ILE LEU GLN TRP MET VAL SER CYS GLU VAL GLY
SEQRES 9 A 282 PRO ASP MET ARG LEU LEU GLY ALA HIS TYR GLN ALA ALA
SEQRES 10 A 282 TYR ASP GLY SER ASP TYR ILE THR LEU ASN GLU ASP LEU
SEQRES 11 A 282 SER SER TRP THR ALA VAL ASP MET VAL SER GLN ILE THR
SEQRES 12 A 282 LYS SER ARG LEU GLU SER ALA GLY THR ALA GLU TYR PHE
SEQRES 13 A 282 ARG ALA TYR VAL GLU GLY GLU CYS LEU GLU LEU LEU HIS
SEQRES 14 A 282 ARG PHE LEU ARG ASN GLY LYS GLU ILE LEU GLN ARG ALA
SEQRES 15 A 282 ASP PRO PRO LYS ALA HIS VAL ALA HIS HIS PRO ARG PRO
SEQRES 16 A 282 LYS GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 282 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LYS ASP GLU
SEQRES 18 A 282 GLU ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 A 282 PRO SER GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 282 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS TYR
SEQRES 21 A 282 VAL HIS HIS GLU GLY LEU THR GLU PRO LEU ALA LEU LYS
SEQRES 22 A 282 TRP ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 B 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 B 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 B 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 B 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 B 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 B 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 C 9 FME TYR PHE ILE ASN ILE LEU THR LEU
SEQRES 1 D 282 GLY SER HIS SER LEU ARG TYR PHE HIS THR ALA VAL SER
SEQRES 2 D 282 ARG PRO GLY ARG GLY GLU PRO GLN TYR ILE SER VAL GLY
SEQRES 3 D 282 TYR VAL ASP ASP VAL GLN PHE GLN ARG CYS ASP SER ILE
SEQRES 4 D 282 GLU GLU ILE PRO ARG MET GLU PRO ARG ALA PRO TRP MET
SEQRES 5 D 282 GLU LYS GLU ARG PRO GLU TYR TRP LYS GLU LEU LYS LEU
SEQRES 6 D 282 LYS VAL LYS ASN ILE ALA GLN SER ALA ARG ALA ASN LEU
SEQRES 7 D 282 ARG THR LEU LEU ARG TYR TYR ASN GLN SER GLU GLY GLY
SEQRES 8 D 282 SER HIS ILE LEU GLN TRP MET VAL SER CYS GLU VAL GLY
SEQRES 9 D 282 PRO ASP MET ARG LEU LEU GLY ALA HIS TYR GLN ALA ALA
SEQRES 10 D 282 TYR ASP GLY SER ASP TYR ILE THR LEU ASN GLU ASP LEU
SEQRES 11 D 282 SER SER TRP THR ALA VAL ASP MET VAL SER GLN ILE THR
SEQRES 12 D 282 LYS SER ARG LEU GLU SER ALA GLY THR ALA GLU TYR PHE
SEQRES 13 D 282 ARG ALA TYR VAL GLU GLY GLU CYS LEU GLU LEU LEU HIS
SEQRES 14 D 282 ARG PHE LEU ARG ASN GLY LYS GLU ILE LEU GLN ARG ALA
SEQRES 15 D 282 ASP PRO PRO LYS ALA HIS VAL ALA HIS HIS PRO ARG PRO
SEQRES 16 D 282 LYS GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 D 282 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LYS ASP GLU
SEQRES 18 D 282 GLU ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 D 282 PRO SER GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 D 282 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS TYR
SEQRES 21 D 282 VAL HIS HIS GLU GLY LEU THR GLU PRO LEU ALA LEU LYS
SEQRES 22 D 282 TRP ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 E 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 E 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 E 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 E 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 E 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 E 99 ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO LYS
SEQRES 8 E 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 F 9 FME TYR PHE ILE ASN ILE LEU THR LEU
MODRES 1MHC ASN D 86 ASN GLYCOSYLATION SITE
MODRES 1MHC FME C 1 MET N-FORMYLMETHIONINE
MODRES 1MHC FME F 1 MET N-FORMYLMETHIONINE
HET FME C 1 10
HET FME F 1 10
HET NAG 3 14
HETNAM FME N-FORMYLMETHIONINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 FME 2(C6 H11 N O3 S)
FORMUL 7 NAG C8 H15 N O6
FORMUL 8 HOH *372(H2 O)
HELIX 1 1 PRO A 50 MET A 52 5 3
HELIX 2 2 GLU A 58 TYR A 84 1 27
HELIX 3 3 MET A 1050 ALA A 1061A 1 13
HELIX 4 4 THR A 1063 GLU A 1072 1 10
HELIX 5 5 GLU A 1073 ASN A 1084 1 12
HELIX 6 6 LYS A 1086 LEU A 1089 1 4
HELIX 7 7 GLU A 2099 ARG A 2101 5 3
HELIX 8 8 PRO D 50 LYS D 54 5 5
HELIX 9 9 PRO D 57 TYR D 84 1 28
HELIX 10 10 MET D 1050 ALA D 1061A 1 13
HELIX 11 11 THR D 1063 GLU D 1072 1 10
HELIX 12 12 GLU D 1073 ASN D 1084 1 12
HELIX 13 13 LYS D 1086 LEU D 1089 1 4
HELIX 14 14 GLU D 2098 ARG D 2101 5 4
SHEET 1 A 8 ILE A 42 PRO A 47 0
SHEET 2 A 8 VAL A 31 ILE A 39 -1 N ILE A 39 O ILE A 42
SHEET 3 A 8 TYR A 22 VAL A 28 -1 N VAL A 28 O VAL A 31
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N THR A 10 O ILE A 23
SHEET 5 A 8 ILE A1004 VAL A1013 -1 N VAL A1013 O HIS A 3
SHEET 6 A 8 LEU A1019 TYR A1028 -1 N ALA A1027 O GLN A1006
SHEET 7 A 8 SER A1031 LEU A1036 -1 N ILE A1034 O ALA A1026
SHEET 8 A 8 TRP A1045 ALA A1047 -1 N THR A1046 O THR A1035
SHEET 1 B 3 LYS A2003 PRO A2010 0
SHEET 2 B 3 VAL A2019 PHE A2028 -1 N LEU A2026 O LYS A2003
SHEET 3 B 3 PHE A2085B VAL A2091 -1 N VAL A2091 O VAL A2019
SHEET 1 C 3 ILE A2037 LYS A2043 0
SHEET 2 C 3 TYR A2102 HIS A2108 -1 N HIS A2107 O THR A2038
SHEET 3 C 3 LEU A2117 LEU A2119 -1 N LEU A2119 O CYS A2104
SHEET 1 D 3 GLN B 3 SER B 8 0
SHEET 2 D 3 PRO B 18 PHE B 28 -1 N THR B 26 O GLN B 3
SHEET 3 D 3 PHE B 85B THR B 92 -1 N PHE B 91 O ASN B 19
SHEET 1 E 3 ILE B 37 LYS B 43 0
SHEET 2 E 3 TYR B 102 HIS B 108 -1 N LYS B 107 O GLU B 38
SHEET 3 E 3 LYS B 117 TYR B 120 -1 N VAL B 119 O CYS B 104
SHEET 1 F 8 ILE D 42 PRO D 47 0
SHEET 2 F 8 VAL D 31 ILE D 39 -1 N ILE D 39 O ILE D 42
SHEET 3 F 8 TYR D 22 VAL D 28 -1 N VAL D 28 O VAL D 31
SHEET 4 F 8 HIS D 3 VAL D 12 -1 N THR D 10 O ILE D 23
SHEET 5 F 8 ILE D1004 VAL D1013 -1 N VAL D1013 O HIS D 3
SHEET 6 F 8 LEU D1019 TYR D1028 -1 N ALA D1027 O GLN D1006
SHEET 7 F 8 SER D1031 LEU D1036 -1 N ILE D1034 O ALA D1026
SHEET 8 F 8 TRP D1045 ALA D1047 -1 N THR D1046 O THR D1035
SHEET 1 G 3 LYS D2003 PRO D2010 0
SHEET 2 G 3 VAL D2019 LEU D2026 -1 N LEU D2026 O LYS D2003
SHEET 3 G 3 LYS D2085 VAL D2091 -1 N VAL D2091 O VAL D2019
SHEET 1 H 3 THR D2038 LYS D2043 0
SHEET 2 H 3 TYR D2102 HIS D2107 -1 N HIS D2107 O THR D2038
SHEET 3 H 3 LEU D2117 LEU D2119 -1 N LEU D2119 O CYS D2104
SHEET 1 I 3 GLN E 3 SER E 8 0
SHEET 2 I 3 PRO E 18 PHE E 28 -1 N THR E 26 O GLN E 3
SHEET 3 I 3 PHE E 85B THR E 92 -1 N PHE E 91 O ASN E 19
SHEET 1 J 3 ILE E 37 LYS E 43 0
SHEET 2 J 3 TYR E 102 HIS E 108 -1 N LYS E 107 O GLU E 38
SHEET 3 J 3 LYS E 117 TYR E 120 -1 N VAL E 119 O CYS E 104
SSBOND 1 CYS A 1011 CYS A 1074 1555 1555
SSBOND 2 CYS A 2023 CYS A 2104 1555 1555
SSBOND 3 CYS B 23 CYS B 104 1555 1555
SSBOND 4 CYS D 1011 CYS D 1074 1555 1555
SSBOND 5 CYS D 2023 CYS D 2104 1555 1555
SSBOND 6 CYS E 23 CYS E 104 1555 1555
LINK ND2 ASN D 86 C1 NAG 3 1555 1555
LINK C FME C 1 N TYR C 2 1555 1555
LINK C FME F 1 N TYR F 2 1555 1555
CISPEP 1 TYR A 2029 PRO A 2030 0 0.34
CISPEP 2 HIS B 29 PRO B 30 0 0.14
CISPEP 3 TYR D 2029 PRO D 2030 0 -0.01
CISPEP 4 HIS E 29 PRO E 30 0 0.13
SITE 1 AC1 2 ASN D 86 HOH 105
CRYST1 65.250 66.100 55.170 102.71 96.28 110.19 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 0.015326 0.005636 0.003375 0.00000
SCALE2 0.000000 0.016119 0.004634 0.00000
SCALE3 0.000000 0.000000 0.018974 0.00000
MTRIX1 1 0.958500 -0.190600 0.211900 4.91290 1
MTRIX2 1 -0.230200 -0.956100 0.181200 38.81280 1
MTRIX3 1 0.168100 -0.222500 -0.960300 28.69440 1
MTRIX1 2 0.964100 -0.186700 0.188600 4.86950 1
MTRIX2 2 -0.221700 -0.957300 0.185400 38.73280 1
MTRIX3 2 0.145900 -0.220600 -0.964400 28.69280 1
MTRIX1 3 0.964600 -0.199100 0.172900 4.96920 1
MTRIX2 3 -0.231700 -0.953000 0.195300 38.69880 1
MTRIX3 3 0.125900 -0.228400 -0.965400 28.64530 1
ATOM 1 N GLY A 1 8.884 46.028 46.965 1.00 53.30 N
ATOM 2 CA GLY A 1 8.479 45.030 48.003 1.00 48.93 C
ATOM 3 C GLY A 1 7.310 44.229 47.464 1.00 49.01 C
ATOM 4 O GLY A 1 6.633 44.700 46.548 1.00 53.05 O
ATOM 5 N SER A 2 7.053 43.058 48.056 1.00 43.28 N
ATOM 6 CA SER A 2 5.978 42.144 47.643 1.00 35.29 C
ATOM 7 C SER A 2 6.419 41.326 46.422 1.00 31.78 C
ATOM 8 O SER A 2 6.637 41.873 45.337 1.00 27.76 O
ATOM 9 CB SER A 2 4.681 42.893 47.359 1.00 32.53 C
ATOM 10 OG SER A 2 3.690 42.001 46.877 1.00 41.49 O
ATOM 11 N HIS A 3 6.595 40.018 46.625 1.00 28.17 N
ATOM 12 CA HIS A 3 7.060 39.129 45.556 1.00 24.36 C
ATOM 13 C HIS A 3 6.120 37.991 45.223 1.00 21.75 C
ATOM 14 O HIS A 3 5.317 37.586 46.058 1.00 27.38 O
ATOM 15 CB HIS A 3 8.450 38.601 45.864 1.00 14.43 C
ATOM 16 CG HIS A 3 9.411 39.665 46.255 1.00 5.49 C
ATOM 17 ND1 HIS A 3 10.270 40.255 45.356 1.00 7.15 N
ATOM 18 CD2 HIS A 3 9.596 40.305 47.430 1.00 5.82 C
ATOM 19 CE1 HIS A 3 10.935 41.224 45.952 1.00 2.00 C
ATOM 20 NE2 HIS A 3 10.544 41.275 47.212 1.00 19.41 N
ATOM 21 N SER A 4 6.320 37.396 44.050 1.00 20.06 N
ATOM 22 CA SER A 4 5.433 36.356 43.554 1.00 15.68 C
ATOM 23 C SER A 4 6.170 35.299 42.703 1.00 15.48 C
ATOM 24 O SER A 4 7.135 35.643 42.024 1.00 24.59 O
ATOM 25 CB SER A 4 4.358 37.107 42.744 1.00 9.70 C
ATOM 26 OG SER A 4 3.548 36.279 41.951 1.00 19.97 O
ATOM 27 N LEU A 5 5.812 34.018 42.842 1.00 13.56 N
ATOM 28 CA LEU A 5 6.398 32.940 42.041 1.00 13.07 C
ATOM 29 C LEU A 5 5.248 32.507 41.130 1.00 13.35 C
ATOM 30 O LEU A 5 4.187 32.163 41.642 1.00 14.45 O
ATOM 31 CB LEU A 5 6.832 31.767 42.949 1.00 16.44 C
ATOM 32 CG LEU A 5 7.292 30.473 42.280 1.00 11.89 C
ATOM 33 CD1 LEU A 5 8.372 30.809 41.282 1.00 13.54 C
ATOM 34 CD2 LEU A 5 7.781 29.458 43.286 1.00 8.06 C
ATOM 35 N ARG A 6 5.426 32.554 39.807 1.00 10.98 N
ATOM 36 CA ARG A 6 4.347 32.209 38.879 1.00 14.39 C
ATOM 37 C ARG A 6 4.744 31.252 37.744 1.00 17.17 C
ATOM 38 O ARG A 6 5.814 31.383 37.168 1.00 18.61 O
ATOM 39 CB ARG A 6 3.795 33.493 38.240 1.00 18.55 C
ATOM 40 CG ARG A 6 3.743 34.697 39.191 1.00 29.88 C
ATOM 41 CD ARG A 6 2.999 35.949 38.652 1.00 31.16 C
ATOM 42 NE ARG A 6 3.563 36.509 37.421 1.00 31.67 N
ATOM 43 CZ ARG A 6 4.780 37.033 37.302 1.00 35.07 C
ATOM 44 NH1 ARG A 6 5.599 37.088 38.341 1.00 30.95 N
ATOM 45 NH2 ARG A 6 5.196 37.458 36.117 1.00 41.41 N
ATOM 46 N TYR A 7 3.848 30.345 37.371 1.00 13.00 N
ATOM 47 CA TYR A 7 4.117 29.414 36.289 1.00 12.41 C
ATOM 48 C TYR A 7 3.014 29.548 35.256 1.00 10.98 C
ATOM 49 O TYR A 7 1.844 29.583 35.604 1.00 14.17 O
ATOM 50 CB TYR A 7 4.128 27.967 36.797 1.00 6.88 C
ATOM 51 CG TYR A 7 5.264 27.606 37.727 1.00 12.08 C
ATOM 52 CD1 TYR A 7 5.176 27.871 39.073 1.00 14.46 C
ATOM 53 CD2 TYR A 7 6.393 26.929 37.270 1.00 11.38 C
ATOM 54 CE1 TYR A 7 6.157 27.473 39.945 1.00 16.84 C
ATOM 55 CE2 TYR A 7 7.373 26.533 38.134 1.00 11.26 C
ATOM 56 CZ TYR A 7 7.252 26.806 39.479 1.00 15.76 C
ATOM 57 OH TYR A 7 8.227 26.421 40.384 1.00 21.69 O
ATOM 58 N PHE A 8 3.374 29.545 33.982 1.00 13.50 N
ATOM 59 CA PHE A 8 2.384 29.648 32.913 1.00 9.80 C
ATOM 60 C PHE A 8 2.514 28.368 32.127 1.00 9.84 C
ATOM 61 O PHE A 8 3.589 28.082 31.650 1.00 11.65 O
ATOM 62 CB PHE A 8 2.704 30.881 32.058 1.00 10.61 C
ATOM 63 CG PHE A 8 2.643 32.158 32.826 1.00 9.93 C
ATOM 64 CD1 PHE A 8 3.683 32.536 33.654 1.00 14.05 C
ATOM 65 CD2 PHE A 8 1.487 32.930 32.815 1.00 12.92 C
ATOM 66 CE1 PHE A 8 3.576 33.666 34.475 1.00 15.56 C
ATOM 67 CE2 PHE A 8 1.371 34.055 33.623 1.00 15.54 C
ATOM 68 CZ PHE A 8 2.413 34.428 34.456 1.00 16.19 C
ATOM 69 N HIS A 9 1.451 27.574 32.017 1.00 4.94 N
ATOM 70 CA HIS A 9 1.563 26.296 31.320 1.00 6.49 C
ATOM 71 C HIS A 9 0.639 26.250 30.135 1.00 13.04 C
ATOM 72 O HIS A 9 -0.522 26.593 30.268 1.00 17.22 O
ATOM 73 CB HIS A 9 1.136 25.087 32.202 1.00 13.98 C
ATOM 74 CG HIS A 9 1.681 25.065 33.605 1.00 10.47 C
ATOM 75 ND1 HIS A 9 2.346 23.972 34.119 1.00 10.07 N
ATOM 76 CD2 HIS A 9 1.539 25.928 34.640 1.00 10.82 C
ATOM 77 CE1 HIS A 9 2.577 24.157 35.405 1.00 2.00 C
ATOM 78 NE2 HIS A 9 2.099 25.340 35.744 1.00 6.42 N
ATOM 79 N THR A 10 1.094 25.640 29.048 1.00 10.50 N
ATOM 80 CA THR A 10 0.316 25.516 27.840 1.00 13.91 C
ATOM 81 C THR A 10 0.435 24.106 27.278 1.00 14.32 C
ATOM 82 O THR A 10 1.539 23.607 27.100 1.00 17.81 O
ATOM 83 CB THR A 10 0.859 26.462 26.745 1.00 15.36 C
ATOM 84 OG1 THR A 10 1.118 27.752 27.306 1.00 15.44 O
ATOM 85 CG2 THR A 10 -0.122 26.570 25.597 1.00 10.92 C
ATOM 86 N ALA A 11 -0.691 23.485 26.965 1.00 9.65 N
ATOM 87 CA ALA A 11 -0.723 22.163 26.372 1.00 6.25 C
ATOM 88 C ALA A 11 -1.426 22.387 25.048 1.00 14.95 C
ATOM 89 O ALA A 11 -2.406 23.127 24.971 1.00 16.40 O
ATOM 90 CB ALA A 11 -1.526 21.219 27.218 1.00 9.93 C
ATOM 91 N VAL A 12 -0.911 21.759 24.006 1.00 13.63 N
ATOM 92 CA VAL A 12 -1.421 21.891 22.665 1.00 17.44 C
ATOM 93 C VAL A 12 -1.787 20.503 22.209 1.00 20.37 C
ATOM 94 O VAL A 12 -1.049 19.575 22.493 1.00 30.85 O
ATOM 95 CB VAL A 12 -0.307 22.460 21.804 1.00 17.00 C
ATOM 96 CG1 VAL A 12 -0.627 22.378 20.351 1.00 22.24 C
ATOM 97 CG2 VAL A 12 -0.036 23.924 22.213 1.00 24.10 C
ATOM 98 N SER A 13 -2.922 20.324 21.539 1.00 22.58 N
ATOM 99 CA SER A 13 -3.310 18.980 21.075 1.00 25.11 C
ATOM 100 C SER A 13 -2.805 18.485 19.696 1.00 29.28 C
ATOM 101 O SER A 13 -2.936 17.287 19.400 1.00 33.03 O
ATOM 102 CB SER A 13 -4.826 18.816 21.130 1.00 29.34 C
ATOM 103 OG SER A 13 -5.479 19.562 20.115 1.00 30.08 O
ATOM 104 N ARG A 14 -2.313 19.389 18.833 1.00 27.00 N
ATOM 105 CA ARG A 14 -1.794 19.041 17.489 1.00 25.99 C
ATOM 106 C ARG A 14 -0.632 19.992 17.247 1.00 28.27 C
ATOM 107 O ARG A 14 -0.730 20.913 16.434 1.00 32.18 O
ATOM 108 CB ARG A 14 -2.836 19.270 16.379 1.00 27.03 C
ATOM 109 CG ARG A 14 -4.186 18.584 16.577 1.00 32.05 C
ATOM 110 CD ARG A 14 -4.153 17.088 16.358 1.00 32.62 C
ATOM 111 NE ARG A 14 -4.867 16.687 15.144 1.00 40.15 N
ATOM 112 CZ ARG A 14 -4.537 17.080 13.912 1.00 39.00 C
ATOM 113 NH1 ARG A 14 -3.498 17.896 13.719 1.00 37.86 N
ATOM 114 NH2 ARG A 14 -5.221 16.624 12.868 1.00 34.94 N
ATOM 115 N PRO A 15 0.490 19.762 17.939 1.00 26.69 N
ATOM 116 CA PRO A 15 1.726 20.531 17.903 1.00 29.44 C
ATOM 117 C PRO A 15 2.396 20.748 16.553 1.00 34.02 C
ATOM 118 O PRO A 15 2.693 21.870 16.158 1.00 39.42 O
ATOM 119 CB PRO A 15 2.641 19.713 18.811 1.00 24.69 C
ATOM 120 CG PRO A 15 1.734 19.000 19.679 1.00 24.58 C
ATOM 121 CD PRO A 15 0.694 18.556 18.752 1.00 25.44 C
ATOM 122 N GLY A 16 2.648 19.668 15.847 1.00 36.67 N
ATOM 123 CA GLY A 16 3.370 19.776 14.603 1.00 44.46 C
ATOM 124 C GLY A 16 4.624 18.959 14.892 1.00 47.05 C
ATOM 125 O GLY A 16 4.732 18.349 15.970 1.00 47.36 O
ATOM 126 N ARG A 17 5.548 18.885 13.940 1.00 49.76 N
ATOM 127 CA ARG A 17 6.768 18.112 14.152 1.00 48.76 C
ATOM 128 C ARG A 17 7.841 19.034 14.698 1.00 44.89 C
ATOM 129 O ARG A 17 8.122 20.090 14.129 1.00 42.31 O
ATOM 130 CB ARG A 17 7.205 17.399 12.863 1.00 53.32 C
ATOM 131 CG ARG A 17 6.211 16.314 12.411 1.00 60.89 C
ATOM 132 CD ARG A 17 6.798 15.377 11.349 1.00 69.37 C
ATOM 133 NE ARG A 17 5.839 14.358 10.905 1.00 77.44 N
ATOM 134 CZ ARG A 17 5.357 13.378 11.673 1.00 80.78 C
ATOM 135 NH1 ARG A 17 5.741 13.267 12.940 1.00 82.01 N
ATOM 136 NH2 ARG A 17 4.477 12.507 11.176 1.00 83.11 N
ATOM 137 N GLY A 18 8.361 18.679 15.865 1.00 42.41 N
ATOM 138 CA GLY A 18 9.389 19.499 16.476 1.00 42.48 C
ATOM 139 C GLY A 18 8.844 20.663 17.290 1.00 41.61 C
ATOM 140 O GLY A 18 9.552 21.644 17.569 1.00 44.37 O
ATOM 141 N GLU A 19 7.565 20.599 17.626 1.00 35.95 N
ATOM 142 CA GLU A 19 6.977 21.648 18.429 1.00 30.13 C
ATOM 143 C GLU A 19 6.450 20.902 19.648 1.00 23.88 C
ATOM 144 O GLU A 19 6.002 19.752 19.520 1.00 22.82 O
ATOM 145 CB GLU A 19 5.868 22.374 17.665 1.00 30.95 C
ATOM 146 CG GLU A 19 6.348 23.155 16.448 1.00 36.50 C
ATOM 147 CD GLU A 19 5.326 24.202 15.937 1.00 42.91 C
ATOM 148 OE1 GLU A 19 5.765 25.328 15.593 1.00 43.15 O
ATOM 149 OE2 GLU A 19 4.099 23.912 15.876 1.00 41.48 O
ATOM 150 N PRO A 20 6.642 21.474 20.861 1.00 22.71 N
ATOM 151 CA PRO A 20 6.172 20.829 22.094 1.00 17.43 C
ATOM 152 C PRO A 20 4.664 20.726 22.164 1.00 21.91 C
ATOM 153 O PRO A 20 3.940 21.533 21.569 1.00 25.21 O
ATOM 154 CB PRO A 20 6.665 21.768 23.202 1.00 12.51 C
ATOM 155 CG PRO A 20 7.792 22.501 22.593 1.00 18.15 C
ATOM 156 CD PRO A 20 7.369 22.720 21.170 1.00 21.80 C
ATOM 157 N GLN A 21 4.193 19.702 22.853 1.00 15.31 N
ATOM 158 CA GLN A 21 2.793 19.567 23.057 1.00 16.08 C
ATOM 159 C GLN A 21 2.510 20.033 24.486 1.00 13.06 C
ATOM 160 O GLN A 21 1.376 20.023 24.920 1.00 15.61 O
ATOM 161 CB GLN A 21 2.320 18.133 22.784 1.00 27.24 C
ATOM 162 CG GLN A 21 3.015 17.003 23.523 1.00 36.47 C
ATOM 163 CD GLN A 21 3.058 15.715 22.705 1.00 43.24 C
ATOM 164 OE1 GLN A 21 4.114 15.083 22.587 1.00 47.20 O
ATOM 165 NE2 GLN A 21 1.919 15.330 22.123 1.00 48.08 N
ATOM 166 N TYR A 22 3.563 20.360 25.233 1.00 10.81 N
ATOM 167 CA TYR A 22 3.462 20.890 26.599 1.00 9.55 C
ATOM 168 C TYR A 22 4.620 21.834 26.803 1.00 15.15 C
ATOM 169 O TYR A 22 5.739 21.529 26.425 1.00 24.77 O
ATOM 170 CB TYR A 22 3.538 19.822 27.681 1.00 10.15 C
ATOM 171 CG TYR A 22 3.746 20.429 29.054 1.00 14.27 C
ATOM 172 CD1 TYR A 22 2.732 21.139 29.671 1.00 10.16 C
ATOM 173 CD2 TYR A 22 4.976 20.338 29.711 1.00 16.56 C
ATOM 174 CE1 TYR A 22 2.918 21.744 30.899 1.00 11.04 C
ATOM 175 CE2 TYR A 22 5.175 20.955 30.954 1.00 12.26 C
ATOM 176 CZ TYR A 22 4.129 21.652 31.531 1.00 13.71 C
ATOM 177 OH TYR A 22 4.290 22.271 32.743 1.00 17.55 O
ATOM 178 N ILE A 23 4.378 22.973 27.428 1.00 17.98 N
ATOM 179 CA ILE A 23 5.449 23.922 27.656 1.00 17.18 C
ATOM 180 C ILE A 23 5.086 24.810 28.812 1.00 19.27 C
ATOM 181 O ILE A 23 3.947 25.240 28.910 1.00 28.53 O
ATOM 182 CB ILE A 23 5.721 24.774 26.371 1.00 20.73 C
ATOM 183 CG1 ILE A 23 6.489 26.039 26.722 1.00 13.56 C
ATOM 184 CG2 ILE A 23 4.425 25.085 25.615 1.00 18.95 C
ATOM 185 CD1 ILE A 23 6.906 26.851 25.510 1.00 22.82 C
ATOM 186 N SER A 24 6.003 25.012 29.744 1.00 19.47 N
ATOM 187 CA SER A 24 5.703 25.889 30.854 1.00 18.91 C
ATOM 188 C SER A 24 6.914 26.717 31.208 1.00 21.82 C
ATOM 189 O SER A 24 8.044 26.274 31.050 1.00 26.98 O
ATOM 190 CB SER A 24 5.218 25.110 32.068 1.00 22.68 C
ATOM 191 OG SER A 24 6.227 24.285 32.586 1.00 18.49 O
ATOM 192 N VAL A 25 6.669 27.937 31.662 1.00 21.76 N
ATOM 193 CA VAL A 25 7.713 28.853 32.055 1.00 17.14 C
ATOM 194 C VAL A 25 7.433 29.367 33.457 1.00 11.21 C
ATOM 195 O VAL A 25 6.290 29.488 33.862 1.00 12.14 O
ATOM 196 CB VAL A 25 7.846 30.018 31.039 1.00 25.01 C
ATOM 197 CG1 VAL A 25 8.328 29.482 29.693 1.00 29.37 C
ATOM 198 CG2 VAL A 25 6.518 30.738 30.840 1.00 22.05 C
ATOM 199 N GLY A 26 8.492 29.640 34.201 1.00 9.19 N
ATOM 200 CA GLY A 26 8.344 30.105 35.552 1.00 6.33 C
ATOM 201 C GLY A 26 9.027 31.431 35.701 1.00 8.27 C
ATOM 202 O GLY A 26 10.078 31.662 35.113 1.00 7.08 O
ATOM 203 N TYR A 27 8.456 32.274 36.551 1.00 9.23 N
ATOM 204 CA TYR A 27 8.945 33.606 36.799 1.00 9.22 C
ATOM 205 C TYR A 27 8.910 33.899 38.272 1.00 10.45 C
ATOM 206 O TYR A 27 8.113 33.317 39.007 1.00 8.70 O
ATOM 207 CB TYR A 27 7.970 34.607 36.182 1.00 12.52 C
ATOM 208 CG TYR A 27 8.108 34.821 34.706 1.00 9.82 C
ATOM 209 CD1 TYR A 27 7.415 34.049 33.800 1.00 3.61 C
ATOM 210 CD2 TYR A 27 8.916 35.853 34.225 1.00 12.36 C
ATOM 211 CE1 TYR A 27 7.510 34.310 32.420 1.00 10.54 C
ATOM 212 CE2 TYR A 27 9.031 36.117 32.879 1.00 13.40 C
ATOM 213 CZ TYR A 27 8.320 35.347 31.975 1.00 14.47 C
ATOM 214 OH TYR A 27 8.416 35.654 30.634 1.00 21.07 O
ATOM 215 N VAL A 28 9.822 34.749 38.718 1.00 13.55 N
ATOM 216 CA VAL A 28 9.788 35.224 40.091 1.00 16.51 C
ATOM 217 C VAL A 28 9.708 36.703 39.776 1.00 15.66 C
ATOM 218 O VAL A 28 10.619 37.266 39.194 1.00 19.54 O
ATOM 219 CB VAL A 28 11.014 34.925 40.908 1.00 15.38 C
ATOM 220 CG1 VAL A 28 10.850 35.583 42.245 1.00 13.58 C
ATOM 221 CG2 VAL A 28 11.138 33.442 41.115 1.00 16.11 C
ATOM 222 N ASP A 29 8.545 37.282 40.026 1.00 17.52 N
ATOM 223 CA ASP A 29 8.310 38.665 39.695 1.00 17.05 C
ATOM 224 C ASP A 29 8.464 38.841 38.169 1.00 20.53 C
ATOM 225 O ASP A 29 7.829 38.108 37.394 1.00 16.76 O
ATOM 226 CB ASP A 29 9.232 39.560 40.496 1.00 11.60 C
ATOM 227 CG ASP A 29 8.955 39.489 41.959 1.00 9.97 C
ATOM 228 OD1 ASP A 29 7.846 39.111 42.381 1.00 16.23 O
ATOM 229 OD2 ASP A 29 9.851 39.816 42.722 1.00 16.19 O
ATOM 230 N ASP A 30 9.328 39.745 37.721 1.00 19.01 N
ATOM 231 CA ASP A 30 9.467 39.960 36.285 1.00 20.47 C
ATOM 232 C ASP A 30 10.653 39.244 35.649 1.00 22.20 C
ATOM 233 O ASP A 30 11.050 39.545 34.507 1.00 23.09 O
ATOM 234 CB ASP A 30 9.524 41.472 36.003 1.00 25.74 C
ATOM 235 CG ASP A 30 8.214 42.200 36.378 1.00 27.04 C
ATOM 236 OD1 ASP A 30 7.118 41.603 36.218 1.00 32.71 O
ATOM 237 OD2 ASP A 30 8.286 43.378 36.811 1.00 27.56 O
ATOM 238 N VAL A 31 11.202 38.281 36.379 1.00 23.28 N
ATOM 239 CA VAL A 31 12.362 37.539 35.910 1.00 19.21 C
ATOM 240 C VAL A 31 12.034 36.072 35.686 1.00 18.88 C
ATOM 241 O VAL A 31 11.498 35.393 36.570 1.00 18.09 O
ATOM 242 CB VAL A 31 13.533 37.643 36.903 1.00 13.02 C
ATOM 243 CG1 VAL A 31 14.731 36.882 36.378 1.00 19.53 C
ATOM 244 CG2 VAL A 31 13.910 39.077 37.131 1.00 6.59 C
ATOM 245 N GLN A 32 12.316 35.605 34.474 1.00 19.48 N
ATOM 246 CA GLN A 32 12.091 34.218 34.134 1.00 19.73 C
ATOM 247 C GLN A 32 13.244 33.377 34.677 1.00 18.67 C
ATOM 248 O GLN A 32 14.420 33.746 34.523 1.00 15.98 O
ATOM 249 CB GLN A 32 12.026 34.063 32.627 1.00 17.95 C
ATOM 250 CG GLN A 32 11.451 32.734 32.208 1.00 22.24 C
ATOM 251 CD GLN A 32 11.701 32.476 30.763 1.00 18.95 C
ATOM 252 OE1 GLN A 32 12.100 33.381 30.034 1.00 21.21 O
ATOM 253 NE2 GLN A 32 11.501 31.240 30.335 1.00 18.81 N
ATOM 254 N PHE A 33 12.907 32.254 35.312 1.00 22.14 N
ATOM 255 CA PHE A 33 13.913 31.357 35.874 1.00 21.46 C
ATOM 256 C PHE A 33 14.128 30.017 35.153 1.00 23.26 C
ATOM 257 O PHE A 33 15.245 29.526 35.124 1.00 26.80 O
ATOM 258 CB PHE A 33 13.719 31.173 37.380 1.00 20.16 C
ATOM 259 CG PHE A 33 12.433 30.474 37.780 1.00 14.98 C
ATOM 260 CD1 PHE A 33 11.369 31.194 38.279 1.00 18.27 C
ATOM 261 CD2 PHE A 33 12.356 29.093 37.827 1.00 17.02 C
ATOM 262 CE1 PHE A 33 10.262 30.551 38.832 1.00 5.03 C
ATOM 263 CE2 PHE A 33 11.238 28.444 38.388 1.00 9.67 C
ATOM 264 CZ PHE A 33 10.206 29.176 38.888 1.00 9.38 C
ATOM 265 N GLN A 34 13.108 29.469 34.496 1.00 24.36 N
ATOM 266 CA GLN A 34 13.292 28.212 33.775 1.00 19.91 C
ATOM 267 C GLN A 34 12.278 28.019 32.666 1.00 24.01 C
ATOM 268 O GLN A 34 11.346 28.819 32.531 1.00 25.81 O