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1RJZ.pdb
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HEADER IMMUNE SYSTEM 20-NOV-03 1RJZ
TITLE MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED
TITLE 2 WITH BETA-2 MICROGLOBULIN AND HERPIES SIMPLEX VIRUS MUTANT
TITLE 3 GLYCOPROTEIN B PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B
COMPND 3 ALPHA CHAIN;
COMPND 4 CHAIN: A, D;
COMPND 5 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 6 SYNONYM: H-2KB;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 10 CHAIN: B, E;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: GLYCOPROTEIN B;
COMPND 14 CHAIN: P, Q;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: 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-K;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: B2M;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 OTHER_DETAILS: NATURALLY OCCURING SEQUENCE IN HERPIES
SOURCE 18 SIMPLEX VIRUS WITH S2E POINT MUTATION
KEYWDS MHC, CLASS I, PEPTIDE, VIRUS, TCR, HERPES, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.MILEY,I.MESSAOUDI,J.NIKOLICH-ZUGICH,D.H.FREMONT
REVDAT 2 24-FEB-09 1RJZ 1 VERSN
REVDAT 1 14-DEC-04 1RJZ 0
JRNL AUTH M.J.MILEY,I.MESSAOUDI,B.M.METZNER,Y.WU,
JRNL AUTH 2 J.NIKOLICH-ZUGICH,D.H.FREMONT
JRNL TITL STRUCTURAL BASIS FOR THE RESTORATION OF TCR
JRNL TITL 2 RECOGNITION OF AN MHC ALLELIC VARIANT BY PEPTIDE
JRNL TITL 3 SECONDARY ANCHOR SUBSTITUTION
JRNL REF J.EXP.MED. V. 200 1445 2004
JRNL REFN ISSN 0022-1007
JRNL PMID 15557346
JRNL DOI 10.1084/JEM.20040217
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 184621.780
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.7
REMARK 3 NUMBER OF REFLECTIONS : 25910
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) : 0.230
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1270
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3423
REMARK 3 BIN R VALUE (WORKING SET) : 0.3890
REMARK 3 BIN FREE R VALUE : 0.4310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 179
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6308
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.10000
REMARK 3 B22 (A**2) : 14.96000
REMARK 3 B33 (A**2) : -8.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.92000
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) : 0.49
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.54
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.92
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) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.650 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.180 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 26.86
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1RJZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-03.
REMARK 100 THE RCSB ID CODE IS RCSB020821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE 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 : 29043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.770
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CA ACETATE, SODIUM
REMARK 280 CHLORIDE, CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 45.08850
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, D, E, Q
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 410
REMARK 410 IMGT/3Dstructure-DB annotations
REMARK 410 (http://www.imgt.org)
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Glycoprotein B peptide 448-505 (P06436), S2>E
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Human alphaherpesvirus 1 (Herpes simplex virus type 1)
REMARK 410 Chain ID
REMARK 410 1rjz_Q
REMARK 410
REMARK 410 ligand(s)
REMARK 410 Glycoprotein B peptide 448-505 (P06436), S2>E
REMARK 410 IMGT receptor type
REMARK 410
REMARK 410 IMGT receptor description
REMARK 410 Peptide
REMARK 410 Species
REMARK 410 Human alphaherpesvirus 1 (Herpes simplex virus type 1)
REMARK 410 Chain ID
REMARK 410 1rjz_P
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-K1b (H2-K1b)
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 1rjz_A,1rjz_B
REMARK 410
REMARK 410 IMGT protein name
REMARK 410 MH1-K1b (H2-K1b)
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 1rjz_D,1rjz_E
REMARK 410
REMARK 410
REMARK 410 Chain ID 1rjz_A (1RJZA)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSLRYFVTAVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDK
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQ
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPST
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (95.6%)
REMARK 410 G-DOMAIN ..........GPHSLRY.FVTAVSRPGLGEPRFISVGYVDNTEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......RWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYN
REMARK 410 G-DOMAIN QSKG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAALITKHKWEQA.GEAERLRAYLEGTCVEWLRRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHSRPE......DKVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELIQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQYYT
REMARK 410 C-LIKE-DOMAIN CHVYHQG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1rjz_B (1RJZB)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (2-100) [D1]
REMARK 410 MIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYIL
REMARK 410 ]
REMARK 410 AHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
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 1rjz_D (1RJZD)
REMARK 410 IMGT chain description I-ALPHA
REMARK 410 Chain amino acid sequence
REMARK 410 [ G-ALPHA1 (1-90) [D1]
REMARK 410 GPHSLRYFVTAVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQK
REMARK 410 ][ G-ALPHA
REMARK 410 AKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKT
REMARK 410 2 (91-182) [D2] ][
REMARK 410 WTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDK
REMARK 410 C-LIKE (183-274) [D3]
REMARK 410 VTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQ
REMARK 410 ]
REMARK 410 GLPEPLTLRWEPPPST
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA1
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (95.6%)
REMARK 410 G-DOMAIN ..........GPHSLRY.FVTAVSRPGLGEPRFISVGYVDNTEFVRFDSDAE
REMARK 410 G-DOMAIN NPRYEPRA.......RWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYN
REMARK 410 G-DOMAIN QSKG...
REMARK 410 G-DOMAIN IMGT domain description G-ALPHA2
REMARK 410 G-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 G-DOMAIN IMGT gene and allele (100%)
REMARK 410 G-DOMAIN ..........GSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNED..L
REMARK 410 G-DOMAIN KTWTAAD.......MAALITKHKWEQA.GEAERLRAYLEGTCVEWLRRYLKN
REMARK 410 G-DOMAIN GNATLLRT.
REMARK 410 C-LIKE-DOMAIN IMGT domain description C-LIKE
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele Mus musculus MH1-K1b
REMARK 410 C-LIKE-DOMAIN IMGT gene and allele (100%)
REMARK 410 C-LIKE-DOMAIN Sheet composition [A B D E] [C F G]
REMARK 410 C-LIKE-DOMAIN .......DSPKAHVTHHSRPE......DKVTLRCWALGFYP..ADITLTWQL
REMARK 410 C-LIKE-DOMAIN NGEELIQ..DMELVETRPAGD......GTFQKWASVVVPLG.....KEQYYT
REMARK 410 C-LIKE-DOMAIN CHVYHQG..LPEPLTLRW
REMARK 410
REMARK 410 Chain ID 1rjz_E (1RJZE)
REMARK 410 IMGT chain description B2M
REMARK 410 Chain amino acid sequence
REMARK 410 [ C-LIKE (2-100) [D1]
REMARK 410 MIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYIL
REMARK 410 ]
REMARK 410 AHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
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 SER A 279
REMARK 465 THR A 280
REMARK 465 SER D 279
REMARK 465 THR D 280
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 4 144.82 -173.18
REMARK 500 ASP A 37 108.69 -162.08
REMARK 500 ASP A 39 36.83 -70.51
REMARK 500 GLU A 41 -75.59 -35.70
REMARK 500 PRO A 43 119.54 -37.77
REMARK 500 ARG A 50 -39.55 -38.62
REMARK 500 ASN A 86 64.71 39.96
REMARK 500 ARG A 111 132.26 -170.60
REMARK 500 GLN A 114 89.98 -173.24
REMARK 500 ASP A 122 130.62 -35.69
REMARK 500 TYR A 123 -61.94 -107.86
REMARK 500 LYS A 131 -32.83 -145.21
REMARK 500 THR A 163 -53.57 -27.67
REMARK 500 LYS A 173 -32.44 -38.03
REMARK 500 ARG A 181 158.86 -48.15
REMARK 500 GLU A 196 -140.25 77.89
REMARK 500 LYS A 243 145.04 -175.73
REMARK 500 PRO A 269 157.29 -34.92
REMARK 500 LYS B 45 135.70 -39.26
REMARK 500 PRO B 47 -77.12 -72.31
REMARK 500 LYS B 48 92.35 -62.39
REMARK 500 TRP B 60 -22.65 73.27
REMARK 500 PHE B 70 149.04 178.94
REMARK 500 ASP B 85 -18.58 -48.69
REMARK 500 ASP B 98 39.71 -89.80
REMARK 500 PRO D 15 119.18 -38.82
REMARK 500 LEU D 17 -2.13 -51.57
REMARK 500 PRO D 57 -38.11 -39.78
REMARK 500 ARG D 111 150.59 175.33
REMARK 500 GLN D 114 76.71 -170.36
REMARK 500 TYR D 123 -61.18 -121.32
REMARK 500 LYS D 131 -35.78 -137.39
REMARK 500 ALA D 177 12.22 -65.82
REMARK 500 THR D 178 -56.18 -133.58
REMARK 500 LEU D 180 -7.13 -56.63
REMARK 500 HIS D 188 154.01 168.14
REMARK 500 GLU D 196 -132.89 70.14
REMARK 500 GLU D 222 107.55 177.98
REMARK 500 LEU D 224 54.47 -93.01
REMARK 500 LYS D 243 155.99 176.65
REMARK 500 GLN D 264 28.67 -79.63
REMARK 500 PRO E 47 -75.24 -80.82
REMARK 500 TRP E 60 -25.91 73.17
REMARK 500 ASP E 85 -28.76 -38.42
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RJZ A 1 280 UNP P01901 HA1B_MOUSE 22 301
DBREF 1RJZ D 1 280 UNP P01901 HA1B_MOUSE 22 301
DBREF 1RJZ B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1RJZ E 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 1RJZ P 1 8 UNP P06436 VGLB_HHV1F 498 505
DBREF 1RJZ Q 1 8 UNP P06436 VGLB_HHV1F 498 505
SEQADV 1RJZ PHE A 22 UNP P01901 TYR 43 ENGINEERED
SEQADV 1RJZ ILE A 23 UNP P01901 MET 44 ENGINEERED
SEQADV 1RJZ SER A 24 UNP P01901 GLU 45 ENGINEERED
SEQADV 1RJZ ASN A 30 UNP P01901 ASP 51 ENGINEERED
SEQADV 1RJZ PHE D 22 UNP P01901 TYR 43 ENGINEERED
SEQADV 1RJZ ILE D 23 UNP P01901 MET 44 ENGINEERED
SEQADV 1RJZ SER D 24 UNP P01901 GLU 45 ENGINEERED
SEQADV 1RJZ ASN D 30 UNP P01901 ASP 51 ENGINEERED
SEQADV 1RJZ MET B 1 UNP P01887 CLONING ARTIFACT
SEQADV 1RJZ MET E 1 UNP P01887 CLONING ARTIFACT
SEQADV 1RJZ GLU P 2 UNP P06436 SER 499 ENGINEERED
SEQADV 1RJZ GLU Q 2 UNP P06436 SER 499 ENGINEERED
SEQRES 1 A 280 GLY PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER
SEQRES 2 A 280 ARG PRO GLY LEU GLY GLU PRO ARG PHE ILE SER VAL GLY
SEQRES 3 A 280 TYR VAL ASP ASN THR GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP MET
SEQRES 5 A 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 A 280 LYS ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU
SEQRES 7 A 280 ARG THR LEU LEU GLY TYR TYR ASN GLN SER LYS GLY GLY
SEQRES 8 A 280 SER HIS THR ILE GLN VAL ILE SER GLY CYS GLU VAL GLY
SEQRES 9 A 280 SER ASP GLY ARG LEU LEU ARG GLY TYR GLN GLN TYR ALA
SEQRES 10 A 280 TYR ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA LEU ILE THR
SEQRES 12 A 280 LYS HIS LYS TRP GLU GLN ALA GLY GLU ALA GLU ARG LEU
SEQRES 13 A 280 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 A 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS SER ARG PRO
SEQRES 16 A 280 GLU ASP LYS VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 A 280 GLU GLU LEU ILE GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 A 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 A 280 VAL VAL PRO LEU GLY LYS GLU GLN TYR TYR THR CYS HIS
SEQRES 21 A 280 VAL TYR HIS GLN GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 A 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 B 100 MET ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS
SEQRES 3 B 100 TYR VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN
SEQRES 4 B 100 MET LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET
SEQRES 5 B 100 SER ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE
SEQRES 6 B 100 LEU ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR
SEQRES 7 B 100 TYR ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO
SEQRES 8 B 100 LYS THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 P 8 SER GLU ILE GLU PHE ALA ARG LEU
SEQRES 1 D 280 GLY PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER
SEQRES 2 D 280 ARG PRO GLY LEU GLY GLU PRO ARG PHE ILE SER VAL GLY
SEQRES 3 D 280 TYR VAL ASP ASN THR GLU PHE VAL ARG PHE ASP SER ASP
SEQRES 4 D 280 ALA GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP MET
SEQRES 5 D 280 GLU GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN
SEQRES 6 D 280 LYS ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU
SEQRES 7 D 280 ARG THR LEU LEU GLY TYR TYR ASN GLN SER LYS GLY GLY
SEQRES 8 D 280 SER HIS THR ILE GLN VAL ILE SER GLY CYS GLU VAL GLY
SEQRES 9 D 280 SER ASP GLY ARG LEU LEU ARG GLY TYR GLN GLN TYR ALA
SEQRES 10 D 280 TYR ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 D 280 LYS THR TRP THR ALA ALA ASP MET ALA ALA LEU ILE THR
SEQRES 12 D 280 LYS HIS LYS TRP GLU GLN ALA GLY GLU ALA GLU ARG LEU
SEQRES 13 D 280 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 D 280 ARG TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR
SEQRES 15 D 280 ASP SER PRO LYS ALA HIS VAL THR HIS HIS SER ARG PRO
SEQRES 16 D 280 GLU ASP LYS VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 D 280 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 D 280 GLU GLU LEU ILE GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 D 280 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL
SEQRES 20 D 280 VAL VAL PRO LEU GLY LYS GLU GLN TYR TYR THR CYS HIS
SEQRES 21 D 280 VAL TYR HIS GLN GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 D 280 TRP GLU PRO PRO PRO SER THR
SEQRES 1 E 100 MET ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG
SEQRES 2 E 100 HIS PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS
SEQRES 3 E 100 TYR VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN
SEQRES 4 E 100 MET LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET
SEQRES 5 E 100 SER ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE
SEQRES 6 E 100 LEU ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR
SEQRES 7 E 100 TYR ALA CYS ARG VAL LYS HIS ASP SER MET ALA GLU PRO
SEQRES 8 E 100 LYS THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 Q 8 SER GLU ILE GLU PHE ALA ARG LEU
FORMUL 7 HOH *230(H2 O)
HELIX 1 1 ALA A 49 GLU A 55 5 7
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ASP A 1049 GLY A 1062 1 15
HELIX 4 4 GLY A 1062 GLY A 1072A 1 12
HELIX 5 5 GLY A 1072A ASN A 1084 1 13
HELIX 6 6 GLY A 1085 LEU A 1090 1 6
HELIX 7 7 LYS A 2098 GLN A 2100 5 3
HELIX 8 8 ALA D 49 GLU D 55 5 7
HELIX 9 9 GLY D 56 TYR D 85 1 30
HELIX 10 10 ASP D 1049 GLY D 1062 1 15
HELIX 11 11 GLY D 1062 GLY D 1072A 1 12
HELIX 12 12 GLY D 1072A LEU D 1090 1 19
HELIX 13 13 LYS D 2098 GLN D 2100 5 3
SHEET 1 A 7 GLU A 46 PRO A 47 0
SHEET 2 A 7 GLU A 32 ARG A 35 -1 N ARG A 35 O GLU A 46
SHEET 3 A 7 GLY A 18 VAL A 28 -1 N GLY A 26 O PHE A 33
SHEET 4 A 7 HIS A 3 ARG A 14 -1 N ARG A 6 O TYR A 27
SHEET 5 A 7 THR A1004 VAL A1013 -1 O SER A1009 N TYR A 7
SHEET 6 A 7 LEU A1019 TYR A1028 -1 O LEU A1020 N GLU A1012
SHEET 7 A 7 CYS A1031 ALA A1035 -1 O CYS A1031 N TYR A1028
SHEET 1 B 4 LYS A2003 SER A2010 0
SHEET 2 B 4 LYS A2018 PHE A2028 -1 O THR A2020 N HIS A2009
SHEET 3 B 4 PHE A2085B PRO A2092 -1 O ALA A2087 N CYS A2023
SHEET 4 B 4 GLU A2079 LEU A2080 -1 N GLU A2079 O SER A2088
SHEET 1 C 4 LYS A2003 SER A2010 0
SHEET 2 C 4 LYS A2018 PHE A2028 -1 O THR A2020 N HIS A2009
SHEET 3 C 4 PHE A2085B PRO A2092 -1 O ALA A2087 N CYS A2023
SHEET 4 C 4 ARG A2084 PRO A2084A-1 N ARG A2084 O GLN A2085A
SHEET 1 D 3 THR A2038 LEU A2043 0
SHEET 2 D 3 TYR A2102 TYR A2107 -1 O TYR A2107 N THR A2038
SHEET 3 D 3 LEU A2117 LEU A2119 -1 O LEU A2119 N CYS A2104
SHEET 1 E 4 GLN B1003 SER B1008 0
SHEET 2 E 4 ASN B1019 PHE B1028 -1 O ASN B1022 N TYR B1007
SHEET 3 E 4 PHE B1085B PHE B1091 -1 O PHE B1085B N PHE B1028
SHEET 4 E 4 GLU B1079 MET B1080 -1 N GLU B1079 O HIS B1088
SHEET 1 F 4 GLN B1003 SER B1008 0
SHEET 2 F 4 ASN B1019 PHE B1028 -1 O ASN B1022 N TYR B1007
SHEET 3 F 4 PHE B1085B PHE B1091 -1 O PHE B1085B N PHE B1028
SHEET 4 F 4 SER B1084 PHE B1084A-1 N SER B1084 O TYR B1085A
SHEET 1 G 4 LYS B1045A LYS B1045B 0
SHEET 2 G 4 GLU B1038 LYS B1043 -1 N LYS B1043 O LYS B1045A
SHEET 3 G 4 TYR B1102 LYS B1107 -1 O ARG B1105 N GLN B1040
SHEET 4 G 4 LYS B1117 TYR B1120 -1 O LYS B1117 N VAL B1106
SHEET 1 H 8 GLU D 46 PRO D 47 0
SHEET 2 H 8 GLU D 32 ASP D 37 -1 N ARG D 35 O GLU D 46
SHEET 3 H 8 ARG D 21 VAL D 28 -1 N GLY D 26 O VAL D 34
SHEET 4 H 8 HIS D 3 VAL D 12 -1 N PHE D 8 O VAL D 25
SHEET 5 H 8 THR D1004 VAL D1013 -1 O VAL D1013 N HIS D 3
SHEET 6 H 8 LEU D1019 TYR D1028 -1 O ARG D1021 N GLU D1012
SHEET 7 H 8 CYS D1031 LEU D1036 -1 O ILE D1034 N TYR D1026
SHEET 8 H 8 TRP D1045 ALA D1047 -1 O THR D1046 N ALA D1035
SHEET 1 I 4 LYS D2003 SER D2010 0
SHEET 2 I 4 LYS D2018 PHE D2028 -1 O TRP D2024 N HIS D2005
SHEET 3 I 4 PHE D2085B PRO D2092 -1 O ALA D2087 N CYS D2023
SHEET 4 I 4 GLU D2079 LEU D2080 -1 N GLU D2079 O SER D2088
SHEET 1 J 4 LYS D2003 SER D2010 0
SHEET 2 J 4 LYS D2018 PHE D2028 -1 O TRP D2024 N HIS D2005
SHEET 3 J 4 PHE D2085B PRO D2092 -1 O ALA D2087 N CYS D2023
SHEET 4 J 4 ARG D2084 PRO D2084A-1 N ARG D2084 O GLN D2085A
SHEET 1 K 3 ILE D2037 LEU D2043 0
SHEET 2 K 3 TYR D2102 HIS D2108 -1 O THR D2103 N GLN D2042
SHEET 3 K 3 LEU D2117 LEU D2119 -1 O LEU D2117 N VAL D2106
SHEET 1 L 4 GLN E1003 SER E1008 0
SHEET 2 L 4 ASN E1019 PHE E1028 -1 O THR E1026 N GLN E1003
SHEET 3 L 4 PHE E1085B PHE E1091 -1 O THR E1089 N LEU E1021
SHEET 4 L 4 GLU E1079 MET E1080 -1 N GLU E1079 O HIS E1088
SHEET 1 M 4 GLN E1003 SER E1008 0
SHEET 2 M 4 ASN E1019 PHE E1028 -1 O THR E1026 N GLN E1003
SHEET 3 M 4 PHE E1085B PHE E1091 -1 O THR E1089 N LEU E1021
SHEET 4 M 4 SER E1084 PHE E1084A-1 N SER E1084 O TYR E1085A
SHEET 1 N 4 LYS E1045A LYS E1045B 0
SHEET 2 N 4 GLU E1038 LYS E1043 -1 N LYS E1043 O LYS E1045A
SHEET 3 N 4 TYR E1102 LYS E1107 -1 O ARG E1105 N GLN E1040
SHEET 4 N 4 LYS E1117 TYR E1120 -1 O LYS E1117 N VAL E1106
SSBOND 1 CYS A 1011 CYS A 1074 1555 1555
SSBOND 2 CYS A 2023 CYS A 2104 1555 1555
SSBOND 3 CYS B 1023 CYS B 1104 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 1023 CYS E 1104 1555 1555
CISPEP 1 TYR A 2029 PRO A 2030 0 -0.04
CISPEP 2 HIS B 1029 PRO B 1030 0 0.38
CISPEP 3 TYR D 2029 PRO D 2030 0 -0.13
CISPEP 4 HIS E 1029 PRO E 1030 0 -0.92
CRYST1 66.572 90.177 88.984 90.00 111.32 90.00 P 1 21 1 4
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 0.015021 0.000000 0.005863 0.00000
SCALE2 0.000000 0.011089 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012064 0.00000
ATOM 1 N GLY A 1 7.005 -7.231 42.268 1.00 56.84 N
ATOM 2 CA GLY A 1 7.073 -5.876 41.653 1.00 56.99 C
ATOM 3 C GLY A 1 5.710 -5.225 41.528 1.00 57.44 C
ATOM 4 O GLY A 1 4.693 -5.880 41.770 1.00 56.45 O
ATOM 5 N PRO A 2 5.650 -3.930 41.154 1.00 58.06 N
ATOM 6 CA PRO A 2 4.367 -3.231 41.011 1.00 57.96 C
ATOM 7 C PRO A 2 3.538 -3.827 39.875 1.00 57.67 C
ATOM 8 O PRO A 2 4.039 -4.633 39.089 1.00 57.27 O
ATOM 9 CB PRO A 2 4.788 -1.784 40.746 1.00 57.41 C
ATOM 10 CG PRO A 2 6.067 -1.949 39.998 1.00 57.36 C
ATOM 11 CD PRO A 2 6.768 -3.048 40.771 1.00 58.29 C
ATOM 12 N HIS A 3 2.270 -3.438 39.800 1.00 57.27 N
ATOM 13 CA HIS A 3 1.377 -3.949 38.766 1.00 56.93 C
ATOM 14 C HIS A 3 0.408 -2.862 38.341 1.00 54.62 C
ATOM 15 O HIS A 3 0.439 -1.756 38.885 1.00 55.34 O
ATOM 16 CB HIS A 3 0.620 -5.167 39.290 1.00 60.09 C
ATOM 17 CG HIS A 3 1.519 -6.252 39.794 1.00 64.23 C
ATOM 18 ND1 HIS A 3 2.349 -6.977 38.964 1.00 65.68 N
ATOM 19 CD2 HIS A 3 1.755 -6.704 41.049 1.00 65.72 C
ATOM 20 CE1 HIS A 3 3.056 -7.828 39.686 1.00 67.05 C
ATOM 21 NE2 HIS A 3 2.716 -7.681 40.954 1.00 67.32 N
ATOM 22 N SER A 4 -0.453 -3.164 37.375 1.00 51.17 N
ATOM 23 CA SER A 4 -1.382 -2.148 36.908 1.00 47.28 C
ATOM 24 C SER A 4 -2.433 -2.621 35.921 1.00 43.96 C
ATOM 25 O SER A 4 -2.172 -3.482 35.081 1.00 43.57 O
ATOM 26 CB SER A 4 -0.593 -1.005 36.273 1.00 47.77 C
ATOM 27 OG SER A 4 0.181 -1.481 35.185 1.00 48.60 O
ATOM 28 N LEU A 5 -3.621 -2.033 36.039 1.00 40.24 N
ATOM 29 CA LEU A 5 -4.754 -2.315 35.164 1.00 37.07 C
ATOM 30 C LEU A 5 -5.220 -0.990 34.579 1.00 37.33 C
ATOM 31 O LEU A 5 -5.731 -0.131 35.302 1.00 36.83 O
ATOM 32 CB LEU A 5 -5.913 -2.939 35.934 1.00 33.65 C
ATOM 33 CG LEU A 5 -7.254 -2.936 35.190 1.00 30.41 C
ATOM 34 CD1 LEU A 5 -7.206 -3.892 34.011 1.00 29.94 C
ATOM 35 CD2 LEU A 5 -8.357 -3.336 36.143 1.00 29.05 C
ATOM 36 N ARG A 6 -5.042 -0.837 33.268 1.00 36.93 N
ATOM 37 CA ARG A 6 -5.428 0.375 32.558 1.00 34.91 C
ATOM 38 C ARG A 6 -6.211 0.017 31.292 1.00 32.59 C
ATOM 39 O ARG A 6 -6.004 -1.044 30.709 1.00 31.81 O
ATOM 40 CB ARG A 6 -4.173 1.161 32.157 1.00 36.93 C
ATOM 41 CG ARG A 6 -3.133 1.335 33.262 1.00 40.91 C
ATOM 42 CD ARG A 6 -1.837 1.928 32.717 1.00 40.61 C
ATOM 43 NE ARG A 6 -1.287 1.115 31.635 1.00 43.70 N
ATOM 44 CZ ARG A 6 -0.308 1.506 30.822 1.00 46.67 C
ATOM 45 NH1 ARG A 6 0.243 2.710 30.965 1.00 47.42 N
ATOM 46 NH2 ARG A 6 0.111 0.703 29.849 1.00 45.16 N
ATOM 47 N TYR A 7 -7.108 0.908 30.878 1.00 30.22 N
ATOM 48 CA TYR A 7 -7.887 0.712 29.661 1.00 28.75 C
ATOM 49 C TYR A 7 -7.602 1.859 28.686 1.00 28.77 C
ATOM 50 O TYR A 7 -7.651 3.035 29.059 1.00 29.89 O
ATOM 51 CB TYR A 7 -9.390 0.658 29.966 1.00 27.93 C
ATOM 52 CG TYR A 7 -9.825 -0.570 30.730 1.00 28.78 C
ATOM 53 CD1 TYR A 7 -10.095 -0.512 32.094 1.00 29.81 C
ATOM 54 CD2 TYR A 7 -9.926 -1.804 30.096 1.00 30.65 C
ATOM 55 CE1 TYR A 7 -10.452 -1.663 32.816 1.00 30.50 C
ATOM 56 CE2 TYR A 7 -10.280 -2.962 30.800 1.00 31.67 C
ATOM 57 CZ TYR A 7 -10.541 -2.888 32.160 1.00 32.82 C
ATOM 58 OH TYR A 7 -10.882 -4.037 32.849 1.00 29.88 O
ATOM 59 N PHE A 8 -7.280 1.507 27.444 1.00 27.62 N
ATOM 60 CA PHE A 8 -7.002 2.480 26.387 1.00 26.57 C
ATOM 61 C PHE A 8 -8.186 2.482 25.416 1.00 25.84 C
ATOM 62 O PHE A 8 -8.307 1.604 24.565 1.00 26.34 O
ATOM 63 CB PHE A 8 -5.714 2.110 25.638 1.00 27.30 C
ATOM 64 CG PHE A 8 -4.442 2.470 26.377 1.00 27.99 C
ATOM 65 CD1 PHE A 8 -4.261 2.114 27.712 1.00 28.92 C
ATOM 66 CD2 PHE A 8 -3.405 3.126 25.719 1.00 26.48 C
ATOM 67 CE1 PHE A 8 -3.067 2.406 28.375 1.00 27.36 C
ATOM 68 CE2 PHE A 8 -2.216 3.419 26.370 1.00 26.30 C
ATOM 69 CZ PHE A 8 -2.045 3.057 27.701 1.00 26.94 C
ATOM 70 N VAL A 9 -9.048 3.480 25.561 1.00 24.66 N
ATOM 71 CA VAL A 9 -10.246 3.625 24.748 1.00 22.72 C
ATOM 72 C VAL A 9 -10.151 4.677 23.637 1.00 23.35 C
ATOM 73 O VAL A 9 -9.652 5.788 23.844 1.00 23.83 O
ATOM 74 CB VAL A 9 -11.426 3.982 25.649 1.00 22.97 C
ATOM 75 CG1 VAL A 9 -12.674 4.218 24.826 1.00 23.06 C
ATOM 76 CG2 VAL A 9 -11.641 2.876 26.650 1.00 23.09 C
ATOM 77 N THR A 10 -10.658 4.321 22.459 1.00 22.32 N
ATOM 78 CA THR A 10 -10.651 5.219 21.315 1.00 19.91 C
ATOM 79 C THR A 10 -11.973 5.230 20.573 1.00 20.66 C
ATOM 80 O THR A 10 -12.565 4.181 20.328 1.00 20.16 O
ATOM 81 CB THR A 10 -9.591 4.827 20.307 1.00 18.21 C
ATOM 82 OG1 THR A 10 -8.315 4.805 20.946 1.00 19.00 O
ATOM 83 CG2 THR A 10 -9.570 5.827 19.162 1.00 17.43 C
ATOM 84 N ALA A 11 -12.426 6.423 20.205 1.00 21.47 N
ATOM 85 CA ALA A 11 -13.666 6.569 19.455 1.00 22.51 C
ATOM 86 C ALA A 11 -13.373 7.502 18.288 1.00 24.68 C
ATOM 87 O ALA A 11 -13.005 8.658 18.505 1.00 26.86 O
ATOM 88 CB ALA A 11 -14.744 7.152 20.333 1.00 20.11 C
ATOM 89 N VAL A 12 -13.512 6.999 17.060 1.00 25.16 N
ATOM 90 CA VAL A 12 -13.250 7.805 15.865 1.00 26.04 C
ATOM 91 C VAL A 12 -14.499 8.044 15.039 1.00 28.05 C
ATOM 92 O VAL A 12 -15.046 7.116 14.442 1.00 28.86 O
ATOM 93 CB VAL A 12 -12.257 7.135 14.922 1.00 26.37 C
ATOM 94 CG1 VAL A 12 -11.850 8.114 13.837 1.00 25.73 C
ATOM 95 CG2 VAL A 12 -11.059 6.629 15.695 1.00 29.42 C
ATOM 96 N SER A 13 -14.945 9.290 14.992 1.00 29.26 N
ATOM 97 CA SER A 13 -16.117 9.618 14.212 1.00 30.33 C
ATOM 98 C SER A 13 -15.698 9.501 12.757 1.00 32.16 C
ATOM 99 O SER A 13 -14.644 9.995 12.361 1.00 31.71 O
ATOM 100 CB SER A 13 -16.591 11.040 14.519 1.00 28.55 C
ATOM 101 OG SER A 13 -15.654 11.997 14.071 1.00 27.54 O
ATOM 102 N ARG A 14 -16.517 8.812 11.975 1.00 34.72 N
ATOM 103 CA ARG A 14 -16.261 8.615 10.557 1.00 36.99 C
ATOM 104 C ARG A 14 -17.463 9.186 9.815 1.00 39.07 C
ATOM 105 O ARG A 14 -18.249 8.442 9.227 1.00 40.24 O
ATOM 106 CB ARG A 14 -16.148 7.126 10.240 1.00 37.23 C
ATOM 107 CG ARG A 14 -15.043 6.410 10.954 1.00 38.70 C
ATOM 108 CD ARG A 14 -15.046 4.927 10.603 1.00 39.78 C
ATOM 109 NE ARG A 14 -16.275 4.274 11.041 1.00 40.78 N
ATOM 110 CZ ARG A 14 -16.433 2.957 11.127 1.00 40.18 C
ATOM 111 NH1 ARG A 14 -15.438 2.148 10.801 1.00 40.31 N
ATOM 112 NH2 ARG A 14 -17.580 2.448 11.559 1.00 39.95 N
ATOM 113 N PRO A 15 -17.633 10.514 9.840 1.00 40.40 N
ATOM 114 CA PRO A 15 -18.784 11.086 9.136 1.00 40.34 C
ATOM 115 C PRO A 15 -18.899 10.588 7.694 1.00 41.39 C
ATOM 116 O PRO A 15 -17.915 10.572 6.933 1.00 39.63 O
ATOM 117 CB PRO A 15 -18.540 12.592 9.241 1.00 40.50 C
ATOM 118 CG PRO A 15 -17.040 12.692 9.359 1.00 40.60 C
ATOM 119 CD PRO A 15 -16.716 11.570 10.302 1.00 40.00 C
ATOM 120 N GLY A 16 -20.112 10.166 7.338 1.00 42.37 N
ATOM 121 CA GLY A 16 -20.363 9.656 6.004 1.00 42.96 C
ATOM 122 C GLY A 16 -20.149 8.157 5.940 1.00 43.12 C
ATOM 123 O GLY A 16 -21.061 7.409 5.596 1.00 44.73 O
ATOM 124 N LEU A 17 -18.944 7.714 6.279 1.00 41.97 N
ATOM 125 CA LEU A 17 -18.620 6.296 6.260 1.00 39.98 C
ATOM 126 C LEU A 17 -19.509 5.469 7.177 1.00 39.44 C
ATOM 127 O LEU A 17 -19.579 4.248 7.036 1.00 40.09 O
ATOM 128 CB LEU A 17 -17.166 6.086 6.664 1.00 39.24 C
ATOM 129 CG LEU A 17 -16.126 6.726 5.751 1.00 40.05 C
ATOM 130 CD1 LEU A 17 -14.743 6.198 6.142 1.00 39.60 C
ATOM 131 CD2 LEU A 17 -16.438 6.401 4.286 1.00 39.84 C
ATOM 132 N GLY A 18 -20.176 6.131 8.121 1.00 38.15 N
ATOM 133 CA GLY A 18 -21.047 5.426 9.048 1.00 36.52 C
ATOM 134 C GLY A 18 -20.851 5.824 10.504 1.00 35.12 C
ATOM 135 O GLY A 18 -20.296 6.879 10.799 1.00 35.44 O
ATOM 136 N GLU A 19 -21.316 4.978 11.420 1.00 34.10 N
ATOM 137 CA GLU A 19 -21.189 5.235 12.853 1.00 31.33 C
ATOM 138 C GLU A 19 -19.723 5.260 13.299 1.00 28.76 C
ATOM 139 O GLU A 19 -18.866 4.638 12.668 1.00 28.74 O
ATOM 140 CB GLU A 19 -21.955 4.165 13.625 1.00 32.93 C
ATOM 141 CG GLU A 19 -23.456 4.356 13.602 1.00 35.44 C
ATOM 142 CD GLU A 19 -23.881 5.608 14.351 1.00 38.20 C
ATOM 143 OE1 GLU A 19 -23.349 5.855 15.460 1.00 38.93 O
ATOM 144 OE2 GLU A 19 -24.755 6.339 13.840 1.00 39.07 O
ATOM 145 N PRO A 20 -19.419 5.969 14.402 1.00 25.22 N
ATOM 146 CA PRO A 20 -18.055 6.078 14.928 1.00 22.62 C
ATOM 147 C PRO A 20 -17.440 4.742 15.341 1.00 21.41 C
ATOM 148 O PRO A 20 -18.101 3.910 15.960 1.00 19.07 O
ATOM 149 CB PRO A 20 -18.215 7.020 16.121 1.00 22.64 C
ATOM 150 CG PRO A 20 -19.444 7.784 15.817 1.00 22.75 C
ATOM 151 CD PRO A 20 -20.349 6.731 15.247 1.00 24.92 C
ATOM 152 N ARG A 21 -16.167 4.559 14.999 1.00 20.43 N
ATOM 153 CA ARG A 21 -15.422 3.347 15.327 1.00 20.83 C
ATOM 154 C ARG A 21 -14.982 3.408 16.791 1.00 20.32 C
ATOM 155 O ARG A 21 -14.151 4.235 17.149 1.00 21.28 O
ATOM 156 CB ARG A 21 -14.182 3.252 14.431 1.00 21.67 C
ATOM 157 CG ARG A 21 -13.839 1.856 13.910 1.00 22.24 C
ATOM 158 CD ARG A 21 -13.599 0.887 15.040 1.00 24.07 C
ATOM 159 NE ARG A 21 -13.035 -0.391 14.600 1.00 24.14 N
ATOM 160 CZ ARG A 21 -12.008 -0.515 13.764 1.00 23.64 C
ATOM 161 NH1 ARG A 21 -11.434 0.562 13.255 1.00 24.75 N
ATOM 162 NH2 ARG A 21 -11.524 -1.712 13.475 1.00 20.48 N
ATOM 163 N PHE A 22 -15.542 2.546 17.633 1.00 19.79 N
ATOM 164 CA PHE A 22 -15.183 2.506 19.052 1.00 21.01 C
ATOM 165 C PHE A 22 -14.281 1.293 19.341 1.00 24.26 C
ATOM 166 O PHE A 22 -14.616 0.162 18.967 1.00 26.71 O
ATOM 167 CB PHE A 22 -16.437 2.394 19.897 1.00 20.07 C
ATOM 168 CG PHE A 22 -16.179 2.395 21.377 1.00 22.82 C
ATOM 169 CD1 PHE A 22 -15.855 3.567 22.040 1.00 22.93 C
ATOM 170 CD2 PHE A 22 -16.292 1.228 22.116 1.00 25.29 C
ATOM 171 CE1 PHE A 22 -15.655 3.575 23.416 1.00 24.66 C
ATOM 172 CE2 PHE A 22 -16.091 1.229 23.504 1.00 25.04 C
ATOM 173 CZ PHE A 22 -15.774 2.403 24.148 1.00 24.58 C
ATOM 174 N ILE A 23 -13.145 1.514 20.001 1.00 23.50 N
ATOM 175 CA ILE A 23 -12.235 0.417 20.312 1.00 22.52 C
ATOM 176 C ILE A 23 -11.649 0.525 21.714 1.00 24.72 C
ATOM 177 O ILE A 23 -10.787 1.370 21.971 1.00 25.73 O
ATOM 178 CB ILE A 23 -11.083 0.364 19.308 1.00 20.87 C
ATOM 179 CG1 ILE A 23 -11.616 -0.008 17.933 1.00 22.85 C
ATOM 180 CG2 ILE A 23 -10.060 -0.642 19.740 1.00 19.16 C
ATOM 181 CD1 ILE A 23 -10.515 -0.157 16.876 1.00 26.87 C
ATOM 182 N SER A 24 -12.101 -0.348 22.612 1.00 25.86 N
ATOM 183 CA SER A 24 -11.626 -0.355 23.992 1.00 27.59 C
ATOM 184 C SER A 24 -10.627 -1.496 24.233 1.00 30.74 C
ATOM 185 O SER A 24 -10.927 -2.659 23.940 1.00 30.63 O
ATOM 186 CB SER A 24 -12.814 -0.500 24.925 1.00 27.40 C
ATOM 187 OG SER A 24 -12.453 -0.170 26.245 1.00 32.10 O
ATOM 188 N VAL A 25 -9.448 -1.168 24.770 1.00 31.79 N
ATOM 189 CA VAL A 25 -8.407 -2.173 25.021 1.00 32.21 C
ATOM 190 C VAL A 25 -7.835 -2.145 26.443 1.00 33.50 C
ATOM 191 O VAL A 25 -7.227 -1.166 26.863 1.00 34.11 O
ATOM 192 CB VAL A 25 -7.247 -1.995 24.023 1.00 31.42 C
ATOM 193 CG1 VAL A 25 -6.155 -3.007 24.289 1.00 29.89 C
ATOM 194 CG2 VAL A 25 -7.767 -2.147 22.613 1.00 31.85 C
ATOM 195 N GLY A 26 -8.020 -3.233 27.180 1.00 35.00 N
ATOM 196 CA GLY A 26 -7.513 -3.285 28.544 1.00 35.45 C
ATOM 197 C GLY A 26 -6.127 -3.885 28.667 1.00 35.25 C
ATOM 198 O GLY A 26 -5.844 -4.917 28.058 1.00 35.72 O
ATOM 199 N TYR A 27 -5.267 -3.244 29.452 1.00 35.38 N
ATOM 200 CA TYR A 27 -3.902 -3.725 29.650 1.00 37.61 C
ATOM 201 C TYR A 27 -3.605 -4.004 31.120 1.00 40.14 C
ATOM 202 O TYR A 27 -3.970 -3.216 31.991 1.00 41.65 O
ATOM 203 CB TYR A 27 -2.870 -2.699 29.159 1.00 36.35 C
ATOM 204 CG TYR A 27 -2.862 -2.423 27.673 1.00 35.59 C
ATOM 205 CD1 TYR A 27 -3.747 -1.506 27.104 1.00 36.75 C
ATOM 206 CD2 TYR A 27 -1.986 -3.094 26.832 1.00 34.15 C
ATOM 207 CE1 TYR A 27 -3.758 -1.271 25.726 1.00 36.19 C
ATOM 208 CE2 TYR A 27 -1.991 -2.871 25.459 1.00 35.12 C
ATOM 209 CZ TYR A 27 -2.880 -1.963 24.905 1.00 34.91 C
ATOM 210 OH TYR A 27 -2.912 -1.793 23.535 1.00 32.23 O
ATOM 211 N VAL A 28 -2.946 -5.127 31.391 1.00 42.48 N
ATOM 212 CA VAL A 28 -2.544 -5.488 32.753 1.00 43.48 C
ATOM 213 C VAL A 28 -1.031 -5.587 32.690 1.00 44.79 C
ATOM 214 O VAL A 28 -0.496 -6.468 32.016 1.00 45.75 O
ATOM 215 CB VAL A 28 -3.086 -6.864 33.198 1.00 43.08 C
ATOM 216 CG1 VAL A 28 -2.528 -7.208 34.571 1.00 42.15 C
ATOM 217 CG2 VAL A 28 -4.602 -6.847 33.238 1.00 42.85 C
ATOM 218 N ASP A 29 -0.339 -4.689 33.379 1.00 46.34 N
ATOM 219 CA ASP A 29 1.117 -4.705 33.342 1.00 47.82 C
ATOM 220 C ASP A 29 1.521 -4.484 31.888 1.00 47.50 C
ATOM 221 O ASP A 29 2.331 -5.228 31.344 1.00 49.10 O
ATOM 222 CB ASP A 29 1.665 -6.064 33.813 1.00 50.53 C
ATOM 223 CG ASP A 29 1.514 -6.282 35.312 1.00 53.24 C
ATOM 224 OD1 ASP A 29 0.439 -5.959 35.866 1.00 56.21 O
ATOM 225 OD2 ASP A 29 2.469 -6.794 35.935 1.00 53.21 O
ATOM 226 N ASN A 30 0.938 -3.479 31.249 1.00 46.35 N
ATOM 227 CA ASN A 30 1.273 -3.200 29.863 1.00 45.26 C
ATOM 228 C ASN A 30 1.092 -4.396 28.927 1.00 43.34 C
ATOM 229 O ASN A 30 1.782 -4.496 27.915 1.00 43.55 O
ATOM 230 CB ASN A 30 2.718 -2.703 29.764 1.00 46.91 C
ATOM 231 CG ASN A 30 2.849 -1.232 30.088 1.00 49.91 C
ATOM 232 OD1 ASN A 30 2.293 -0.381 29.394 1.00 52.74 O
ATOM 233 ND2 ASN A 30 3.585 -0.921 31.143 1.00 51.45 N
ATOM 234 N THR A 31 0.174 -5.300 29.261 1.00 40.57 N
ATOM 235 CA THR A 31 -0.091 -6.471 28.420 1.00 36.82 C
ATOM 236 C THR A 31 -1.565 -6.587 28.096 1.00 35.69 C
ATOM 237 O THR A 31 -2.379 -6.877 28.966 1.00 36.38 O
ATOM 238 CB THR A 31 0.354 -7.773 29.090 1.00 34.73 C
ATOM 239 OG1 THR A 31 1.754 -7.955 28.871 1.00 36.35 O
ATOM 240 CG2 THR A 31 -0.380 -8.955 28.508 1.00 34.02 C
ATOM 241 N GLU A 32 -1.908 -6.365 26.834 1.00 34.19 N
ATOM 242 CA GLU A 32 -3.297 -6.440 26.412 1.00 33.06 C
ATOM 243 C GLU A 32 -3.905 -7.757 26.888 1.00 33.30 C
ATOM 244 O GLU A 32 -3.307 -8.823 26.707 1.00 33.81 O
ATOM 245 CB GLU A 32 -3.390 -6.337 24.884 1.00 30.36 C
ATOM 246 CG GLU A 32 -4.761 -5.920 24.380 1.00 28.76 C
ATOM 247 CD GLU A 32 -4.836 -5.795 22.866 1.00 28.56 C
ATOM 248 OE1 GLU A 32 -3.938 -5.161 22.264 1.00 26.71 O
ATOM 249 OE2 GLU A 32 -5.807 -6.326 22.282 1.00 27.70 O
ATOM 250 N PHE A 33 -5.073 -7.685 27.522 1.00 32.04 N
ATOM 251 CA PHE A 33 -5.739 -8.897 27.974 1.00 31.92 C
ATOM 252 C PHE A 33 -7.195 -8.943 27.488 1.00 31.67 C
ATOM 253 O PHE A 33 -7.808 -10.011 27.411 1.00 31.03 O
ATOM 254 CB PHE A 33 -5.641 -9.035 29.500 1.00 30.00 C
ATOM 255 CG PHE A 33 -6.512 -8.087 30.272 1.00 32.79 C
ATOM 256 CD1 PHE A 33 -6.253 -6.720 30.279 1.00 33.03 C
ATOM 257 CD2 PHE A 33 -7.572 -8.571 31.040 1.00 33.45 C
ATOM 258 CE1 PHE A 33 -7.034 -5.842 31.044 1.00 32.19 C
ATOM 259 CE2 PHE A 33 -8.360 -7.702 31.807 1.00 33.37 C
ATOM 260 CZ PHE A 33 -8.085 -6.331 31.807 1.00 31.87 C
ATOM 261 N VAL A 34 -7.732 -7.779 27.136 1.00 31.61 N
ATOM 262 CA VAL A 34 -9.099 -7.680 26.622 1.00 31.61 C
ATOM 263 C VAL A 34 -9.205 -6.589 25.570 1.00 30.71 C
ATOM 264 O VAL A 34 -8.379 -5.673 25.512 1.00 31.32 O
ATOM 265 CB VAL A 34 -10.146 -7.370 27.727 1.00 31.44 C
ATOM 266 CG1 VAL A 34 -10.286 -8.564 28.652 1.00 31.83 C
ATOM 267 CG2 VAL A 34 -9.757 -6.107 28.490 1.00 30.44 C
ATOM 268 N ARG A 35 -10.241 -6.688 24.747 1.00 29.35 N
ATOM 269 CA ARG A 35 -10.455 -5.722 23.687 1.00 28.47 C
ATOM 270 C ARG A 35 -11.874 -5.768 23.165 1.00 28.52 C
ATOM 271 O ARG A 35 -12.458 -6.838 23.039 1.00 29.79 O
ATOM 272 CB ARG A 35 -9.484 -6.001 22.542 1.00 27.39 C
ATOM 273 CG ARG A 35 -9.708 -5.175 21.304 1.00 28.12 C
ATOM 274 CD ARG A 35 -8.698 -5.542 20.225 1.00 29.17 C
ATOM 275 NE ARG A 35 -7.343 -5.098 20.542 1.00 29.86 N
ATOM 276 CZ ARG A 35 -6.758 -4.034 19.999 1.00 30.91 C
ATOM 277 NH1 ARG A 35 -7.405 -3.295 19.102 1.00 29.63 N
ATOM 278 NH2 ARG A 35 -5.521 -3.708 20.351 1.00 31.86 N
ATOM 279 N PHE A 36 -12.424 -4.590 22.885 1.00 29.36 N
ATOM 280 CA PHE A 36 -13.765 -4.447 22.321 1.00 28.34 C
ATOM 281 C PHE A 36 -13.579 -3.696 21.009 1.00 27.93 C
ATOM 282 O PHE A 36 -12.587 -3.002 20.835 1.00 29.09 O
ATOM 283 CB PHE A 36 -14.661 -3.624 23.239 1.00 26.34 C
ATOM 284 CG PHE A 36 -16.035 -3.387 22.685 1.00 26.25 C
ATOM 285 CD1 PHE A 36 -17.041 -4.323 22.855 1.00 27.28 C
ATOM 286 CD2 PHE A 36 -16.326 -2.223 21.994 1.00 27.05 C
ATOM 287 CE1 PHE A 36 -18.321 -4.100 22.346 1.00 26.24 C
ATOM 288 CE2 PHE A 36 -17.601 -1.995 21.484 1.00 26.08 C
ATOM 289 CZ PHE A 36 -18.596 -2.936 21.662 1.00 25.91 C
ATOM 290 N ASP A 37 -14.520 -3.833 20.085 1.00 29.58 N
ATOM 291 CA ASP A 37 -14.426 -3.136 18.799 1.00 29.52 C
ATOM 292 C ASP A 37 -15.790 -3.101 18.127 1.00 31.52 C
ATOM 293 O ASP A 37 -16.281 -4.122 17.652 1.00 32.35 O
ATOM 294 CB ASP A 37 -13.429 -3.829 17.878 1.00 24.88 C
ATOM 295 CG ASP A 37 -13.134 -3.016 16.660 1.00 22.70 C
ATOM 296 OD1 ASP A 37 -14.013 -2.228 16.279 1.00 26.05 O
ATOM 297 OD2 ASP A 37 -12.046 -3.157 16.075 1.00 20.58 O
ATOM 298 N SER A 38 -16.401 -1.923 18.082 1.00 34.52 N
ATOM 299 CA SER A 38 -17.725 -1.794 17.492 1.00 37.32 C
ATOM 300 C SER A 38 -17.715 -2.202 16.037 1.00 39.45 C
ATOM 301 O SER A 38 -18.626 -2.881 15.570 1.00 39.97 O
ATOM 302 CB SER A 38 -18.232 -0.356 17.613 1.00 36.86 C
ATOM 303 OG SER A 38 -17.453 0.529 16.828 1.00 38.17 O
ATOM 304 N ASP A 39 -16.672 -1.795 15.324 1.00 42.38 N
ATOM 305 CA ASP A 39 -16.567 -2.100 13.910 1.00 46.02 C
ATOM 306 C ASP A 39 -16.298 -3.572 13.654 1.00 49.32 C
ATOM 307 O ASP A 39 -15.560 -3.940 12.741 1.00 48.67 O
ATOM 308 CB ASP A 39 -15.478 -1.258 13.268 1.00 45.52 C
ATOM 309 CG ASP A 39 -15.587 -1.239 11.771 1.00 46.13 C
ATOM 310 OD1 ASP A 39 -16.584 -0.681 11.266 1.00 46.91 O
ATOM 311 OD2 ASP A 39 -14.687 -1.788 11.102 1.00 45.03 O
ATOM 312 N ALA A 40 -16.910 -4.410 14.478 1.00 54.31 N
ATOM 313 CA ALA A 40 -16.785 -5.851 14.352 1.00 58.84 C
ATOM 314 C ALA A 40 -18.193 -6.404 14.184 1.00 61.81 C
ATOM 315 O ALA A 40 -19.183 -5.751 14.533 1.00 61.68 O
ATOM 316 CB ALA A 40 -16.123 -6.445 15.596 1.00 58.97 C
ATOM 317 N GLU A 41 -18.260 -7.609 13.636 1.00 65.22 N
ATOM 318 CA GLU A 41 -19.509 -8.317 13.371 1.00 68.12 C
ATOM 319 C GLU A 41 -20.575 -8.066 14.443 1.00 67.98 C
ATOM 320 O GLU A 41 -21.539 -7.317 14.219 1.00 67.45 O
ATOM 321 CB GLU A 41 -19.159 -9.792 13.234 1.00 70.81 C
ATOM 322 CG GLU A 41 -17.798 -9.929 12.547 1.00 75.41 C
ATOM 323 CD GLU A 41 -17.331 -11.354 12.382 1.00 79.19 C
ATOM 324 OE1 GLU A 41 -17.360 -12.112 13.378 1.00 82.07 O
ATOM 325 OE2 GLU A 41 -16.921 -11.710 11.254 1.00 80.92 O
ATOM 326 N ASN A 42 -20.409 -8.700 15.598 1.00 67.32 N
ATOM 327 CA ASN A 42 -21.328 -8.503 16.715 1.00 66.61 C
ATOM 328 C ASN A 42 -20.431 -8.142 17.895 1.00 65.92 C
ATOM 329 O ASN A 42 -20.064 -8.997 18.692 1.00 66.15 O
ATOM 330 CB ASN A 42 -22.104 -9.782 17.030 1.00 66.52 C
ATOM 331 CG ASN A 42 -23.206 -9.556 18.056 1.00 66.23 C
ATOM 332 OD1 ASN A 42 -23.069 -8.731 18.960 1.00 66.30 O
ATOM 333 ND2 ASN A 42 -24.297 -10.299 17.927 1.00 65.41 N
ATOM 334 N PRO A 43 -20.079 -6.858 18.027 1.00 64.68 N
ATOM 335 CA PRO A 43 -19.213 -6.360 19.101 1.00 63.14 C
ATOM 336 C PRO A 43 -19.397 -6.992 20.480 1.00 61.24 C
ATOM 337 O PRO A 43 -20.472 -6.922 21.074 1.00 60.85 O
ATOM 338 CB PRO A 43 -19.502 -4.863 19.104 1.00 64.53 C
ATOM 339 CG PRO A 43 -20.924 -4.797 18.628 1.00 65.40 C
ATOM 340 CD PRO A 43 -20.883 -5.758 17.471 1.00 65.44 C
ATOM 341 N ARG A 44 -18.327 -7.607 20.976 1.00 59.37 N
ATOM 342 CA ARG A 44 -18.315 -8.249 22.288 1.00 58.10 C
ATOM 343 C ARG A 44 -16.892 -8.199 22.816 1.00 55.80 C
ATOM 344 O ARG A 44 -15.947 -8.047 22.045 1.00 54.36 O
ATOM 345 CB ARG A 44 -18.749 -9.713 22.185 1.00 60.59 C
ATOM 346 CG ARG A 44 -20.202 -9.928 21.814 1.00 64.28 C
ATOM 347 CD ARG A 44 -20.348 -11.154 20.923 1.00 67.49 C
ATOM 348 NE ARG A 44 -19.526 -11.021 19.719 1.00 71.02 N
ATOM 349 CZ ARG A 44 -19.598 -11.811 18.647 1.00 72.34 C
ATOM 350 NH1 ARG A 44 -20.464 -12.817 18.610 1.00 72.59 N
ATOM 351 NH2 ARG A 44 -18.806 -11.585 17.603 1.00 73.06 N
ATOM 352 N TYR A 45 -16.738 -8.322 24.128 1.00 54.25 N
ATOM 353 CA TYR A 45 -15.411 -8.315 24.722 1.00 53.49 C
ATOM 354 C TYR A 45 -14.794 -9.676 24.517 1.00 54.27 C
ATOM 355 O TYR A 45 -15.380 -10.690 24.883 1.00 54.40 O
ATOM 356 CB TYR A 45 -15.477 -8.007 26.219 1.00 51.15 C