HEADER IMMUNE SYSTEM 05-MAR-12 4E0R
TITLE STRUCTURE OF THE CHICKEN MHC CLASS I MOLECULE BF2*0401
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS I ALPHA CHAIN 2;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: UNP RESIDUES 22-291;
COMPND 5 SYNONYM: MHC CLASS I GLYCOPROTEIN, MHC CLASS I MOLECULE;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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: 8-MERIC PEPTIDE (FUS/TLS);
COMPND 14 CHAIN: C, F;
COMPND 15 FRAGMENT: UNP RESIDUES 319-326;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKENS;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: B-FIV, BF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 13 ORGANISM_COMMON: CHICKENS;
SOURCE 14 ORGANISM_TAXID: 9031;
SOURCE 15 GENE: B-F-S-B2M02;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET21A(+);
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 24 ORGANISM_COMMON: CHICKENS;
SOURCE 25 ORGANISM_TAXID: 9031;
SOURCE 26 OTHER_DETAILS: CHEMICAL SYNTHESIS FROM FUS PROTO-ONC GENE
KEYWDS MHC I COMPLEX, NARROW BINDING GROOVE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHANG,Y.CHEN,J.QI,F.GAO,J.KAUFMAN,C.XIA,G.F.GAO
REVDAT 2 08-NOV-23 4E0R 1 SEQADV
REVDAT 1 21-NOV-12 4E0R 0
JRNL AUTH J.ZHANG,Y.CHEN,J.QI,F.GAO,Y.LIU,J.LIU,X.ZHOU,J.KAUFMAN,
JRNL AUTH 2 C.XIA,G.F.GAO
JRNL TITL NARROW GROOVE AND RESTRICTED ANCHORS OF MHC CLASS I MOLECULE
JRNL TITL 2 BF2*0401 PLUS PEPTIDE TRANSPORTER RESTRICTION CAN EXPLAIN
JRNL TITL 3 DISEASE SUSCEPTIBILITY OF B4 CHICKENS.
JRNL REF J.IMMUNOL. V. 189 4478 2012
JRNL REFN ISSN 0022-1767
JRNL PMID 23041567
JRNL DOI 10.4049/JIMMUNOL.1200885
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 34927
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.8397 - 5.1698 0.97 2912 180 0.1969 0.2284
REMARK 3 2 5.1698 - 4.1044 0.99 2843 162 0.1514 0.1788
REMARK 3 3 4.1044 - 3.5859 0.97 2793 171 0.1663 0.2261
REMARK 3 4 3.5859 - 3.2581 0.97 2795 142 0.1829 0.2703
REMARK 3 5 3.2581 - 3.0247 0.97 2769 153 0.2056 0.2532
REMARK 3 6 3.0247 - 2.8464 0.98 2776 148 0.2205 0.2911
REMARK 3 7 2.8464 - 2.7038 0.97 2775 137 0.2179 0.3337
REMARK 3 8 2.7038 - 2.5862 0.95 2713 134 0.2129 0.2493
REMARK 3 9 2.5862 - 2.4866 0.97 2748 141 0.2067 0.2761
REMARK 3 10 2.4866 - 2.4008 0.95 2701 131 0.2071 0.2876
REMARK 3 11 2.4008 - 2.3257 0.96 2724 128 0.2028 0.3369
REMARK 3 12 2.3257 - 2.2593 0.93 2631 120 0.2211 0.3103
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 39.95
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.85720
REMARK 3 B22 (A**2) : 10.04760
REMARK 3 B33 (A**2) : -6.19040
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.20640
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 6302
REMARK 3 ANGLE : 0.771 8554
REMARK 3 CHIRALITY : 0.058 862
REMARK 3 PLANARITY : 0.003 1124
REMARK 3 DIHEDRAL : 17.138 2264
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFMAC WAS ALSO USED IN REFINEMENT.
REMARK 4
REMARK 4 4E0R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34950
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.259
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.19600
REMARK 200 R SYM FOR SHELL (I) : 0.19600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3BEV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES BUFFER (PH 7.0), 5% MPD,
REMARK 280 20% PEG 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 83.09800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.14300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.09800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.14300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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: 4540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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 MET A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 MET B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 PHE B 98
REMARK 465 MET D -2
REMARK 465 GLU D -1
REMARK 465 PHE D 0
REMARK 465 MET E -2
REMARK 465 GLU E -1
REMARK 465 PHE E 0
REMARK 465 PHE E 98
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER B 51 O HOH B 166 2.00
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 2 N - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 ASP A 249 CB - CA - C ANGL. DEV. = -12.2 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 GLU A 103 34.97 -79.98
REMARK 500 GLU A 159 -72.92 -119.25
REMARK 500 ASP A 192 -167.34 -126.70
REMARK 500 MET B 45 -158.75 -92.51
REMARK 500 GLU B 46 -78.52 -103.67
REMARK 500 SER B 51 -35.40 -32.48
REMARK 500 TRP B 59 -11.08 83.80
REMARK 500 PHE D 120 -61.89 -122.16
REMARK 500 GLU D 159 -78.15 -106.99
REMARK 500 ASP D 223 30.98 70.55
REMARK 500 TRP E 59 -12.27 78.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET B 45 GLU B 46 -138.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BEW RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHICKEN MHC CLASS I MOLECULE BF2*2101 WITH A 10-
REMARK 900 MER PEPTIDE
REMARK 900 RELATED ID: 3BEV RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHICKEN MHC CLASS I MOLECULE BF2*2101 WITH A 11-
REMARK 900 MER PEPTIDE
DBREF 4E0R A 1 270 UNP O46790 O46790_CHICK 22 291
DBREF 4E0R B 1 98 UNP P21611 B2MG_CHICK 22 119
DBREF 4E0R C 1 8 UNP Q6J4Y8 Q6J4Y8_CHICK 319 326
DBREF 4E0R D 1 270 UNP O46790 O46790_CHICK 22 291
DBREF 4E0R E 1 98 UNP P21611 B2MG_CHICK 22 119
DBREF 4E0R F 1 8 UNP Q6J4Y8 Q6J4Y8_CHICK 319 326
SEQADV 4E0R MET A -2 UNP O46790 EXPRESSION TAG
SEQADV 4E0R GLU A -1 UNP O46790 EXPRESSION TAG
SEQADV 4E0R PHE A 0 UNP O46790 EXPRESSION TAG
SEQADV 4E0R GLU A 244 UNP O46790 ASP 265 ENGINEERED MUTATION
SEQADV 4E0R LYS A 271 UNP O46790 EXPRESSION TAG
SEQADV 4E0R LEU A 272 UNP O46790 EXPRESSION TAG
SEQADV 4E0R MET B -2 UNP P21611 EXPRESSION TAG
SEQADV 4E0R GLU B -1 UNP P21611 EXPRESSION TAG
SEQADV 4E0R PHE B 0 UNP P21611 EXPRESSION TAG
SEQADV 4E0R MET D -2 UNP O46790 EXPRESSION TAG
SEQADV 4E0R GLU D -1 UNP O46790 EXPRESSION TAG
SEQADV 4E0R PHE D 0 UNP O46790 EXPRESSION TAG
SEQADV 4E0R GLU D 244 UNP O46790 ASP 265 ENGINEERED MUTATION
SEQADV 4E0R LYS D 271 UNP O46790 EXPRESSION TAG
SEQADV 4E0R LEU D 272 UNP O46790 EXPRESSION TAG
SEQADV 4E0R MET E -2 UNP P21611 EXPRESSION TAG
SEQADV 4E0R GLU E -1 UNP P21611 EXPRESSION TAG
SEQADV 4E0R PHE E 0 UNP P21611 EXPRESSION TAG
SEQRES 1 A 275 MET GLU PHE GLU LEU HIS THR LEU ARG TYR ILE ARG THR
SEQRES 2 A 275 ALA MET THR ASP PRO GLY PRO GLY GLN PRO TRP PHE VAL
SEQRES 3 A 275 THR VAL GLY TYR VAL ASP GLY GLU LEU PHE VAL HIS TYR
SEQRES 4 A 275 ASN SER THR ALA ARG ARG TYR VAL PRO ARG THR GLU TRP
SEQRES 5 A 275 ILE ALA ALA ASN THR ASP GLN GLN TYR TRP ASP GLY GLN
SEQRES 6 A 275 THR GLN ILE GLY GLN LEU ASN GLU GLN ILE ASN ARG GLU
SEQRES 7 A 275 ASN LEU GLY ILE ARG GLN ARG ARG TYR ASN GLN THR GLY
SEQRES 8 A 275 GLY SER HIS THR VAL GLN TRP MET PHE GLY CYS ASP ILE
SEQRES 9 A 275 LEU GLU ASP GLY THR ILE ARG GLY TYR ARG GLN SER ALA
SEQRES 10 A 275 TYR ASP GLY ARG ASP PHE ILE ALA LEU ASP LYS ASP MET
SEQRES 11 A 275 LYS THR PHE THR ALA ALA VAL PRO GLU ALA VAL PRO THR
SEQRES 12 A 275 LYS ARG LYS TRP GLU GLU GLU SER GLU PRO GLU ARG TRP
SEQRES 13 A 275 LYS ASN TYR LEU GLU GLU THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 275 ARG TYR VAL GLU TYR GLY LYS ALA GLU LEU GLY ARG ARG
SEQRES 15 A 275 GLU ARG PRO GLU VAL ARG VAL TRP GLY LYS GLU ALA ASP
SEQRES 16 A 275 GLY ILE LEU THR LEU SER CYS ARG ALA HIS GLY PHE TYR
SEQRES 17 A 275 PRO ARG PRO ILE VAL VAL SER TRP LEU LYS ASP GLY ALA
SEQRES 18 A 275 VAL ARG GLY GLN ASP ALA HIS SER GLY GLY ILE VAL PRO
SEQRES 19 A 275 ASN GLY ASP GLY THR TYR HIS THR TRP VAL THR ILE GLU
SEQRES 20 A 275 ALA GLN PRO GLY ASP GLY ASP LYS TYR GLN CYS ARG VAL
SEQRES 21 A 275 GLU HIS ALA SER LEU PRO GLN PRO GLY LEU TYR SER TRP
SEQRES 22 A 275 LYS LEU
SEQRES 1 B 101 MET GLU PHE ASP LEU THR PRO LYS VAL GLN VAL TYR SER
SEQRES 2 B 101 ARG PHE PRO ALA SER ALA GLY THR LYS ASN VAL LEU ASN
SEQRES 3 B 101 CYS PHE ALA ALA GLY PHE HIS PRO PRO LYS ILE SER ILE
SEQRES 4 B 101 THR LEU MET LYS ASP GLY VAL PRO MET GLU GLY ALA GLN
SEQRES 5 B 101 TYR SER ASP MET SER PHE ASN ASP ASP TRP THR PHE GLN
SEQRES 6 B 101 ARG LEU VAL HIS ALA ASP PHE THR PRO SER SER GLY SER
SEQRES 7 B 101 THR TYR ALA CYS LYS VAL GLU HIS GLU THR LEU LYS GLU
SEQRES 8 B 101 PRO GLN VAL TYR LYS TRP ASP PRO GLU PHE
SEQRES 1 C 8 ILE ASP TRP PHE ASP GLY LYS GLU
SEQRES 1 D 275 MET GLU PHE GLU LEU HIS THR LEU ARG TYR ILE ARG THR
SEQRES 2 D 275 ALA MET THR ASP PRO GLY PRO GLY GLN PRO TRP PHE VAL
SEQRES 3 D 275 THR VAL GLY TYR VAL ASP GLY GLU LEU PHE VAL HIS TYR
SEQRES 4 D 275 ASN SER THR ALA ARG ARG TYR VAL PRO ARG THR GLU TRP
SEQRES 5 D 275 ILE ALA ALA ASN THR ASP GLN GLN TYR TRP ASP GLY GLN
SEQRES 6 D 275 THR GLN ILE GLY GLN LEU ASN GLU GLN ILE ASN ARG GLU
SEQRES 7 D 275 ASN LEU GLY ILE ARG GLN ARG ARG TYR ASN GLN THR GLY
SEQRES 8 D 275 GLY SER HIS THR VAL GLN TRP MET PHE GLY CYS ASP ILE
SEQRES 9 D 275 LEU GLU ASP GLY THR ILE ARG GLY TYR ARG GLN SER ALA
SEQRES 10 D 275 TYR ASP GLY ARG ASP PHE ILE ALA LEU ASP LYS ASP MET
SEQRES 11 D 275 LYS THR PHE THR ALA ALA VAL PRO GLU ALA VAL PRO THR
SEQRES 12 D 275 LYS ARG LYS TRP GLU GLU GLU SER GLU PRO GLU ARG TRP
SEQRES 13 D 275 LYS ASN TYR LEU GLU GLU THR CYS VAL GLU TRP LEU ARG
SEQRES 14 D 275 ARG TYR VAL GLU TYR GLY LYS ALA GLU LEU GLY ARG ARG
SEQRES 15 D 275 GLU ARG PRO GLU VAL ARG VAL TRP GLY LYS GLU ALA ASP
SEQRES 16 D 275 GLY ILE LEU THR LEU SER CYS ARG ALA HIS GLY PHE TYR
SEQRES 17 D 275 PRO ARG PRO ILE VAL VAL SER TRP LEU LYS ASP GLY ALA
SEQRES 18 D 275 VAL ARG GLY GLN ASP ALA HIS SER GLY GLY ILE VAL PRO
SEQRES 19 D 275 ASN GLY ASP GLY THR TYR HIS THR TRP VAL THR ILE GLU
SEQRES 20 D 275 ALA GLN PRO GLY ASP GLY ASP LYS TYR GLN CYS ARG VAL
SEQRES 21 D 275 GLU HIS ALA SER LEU PRO GLN PRO GLY LEU TYR SER TRP
SEQRES 22 D 275 LYS LEU
SEQRES 1 E 101 MET GLU PHE ASP LEU THR PRO LYS VAL GLN VAL TYR SER
SEQRES 2 E 101 ARG PHE PRO ALA SER ALA GLY THR LYS ASN VAL LEU ASN
SEQRES 3 E 101 CYS PHE ALA ALA GLY PHE HIS PRO PRO LYS ILE SER ILE
SEQRES 4 E 101 THR LEU MET LYS ASP GLY VAL PRO MET GLU GLY ALA GLN
SEQRES 5 E 101 TYR SER ASP MET SER PHE ASN ASP ASP TRP THR PHE GLN
SEQRES 6 E 101 ARG LEU VAL HIS ALA ASP PHE THR PRO SER SER GLY SER
SEQRES 7 E 101 THR TYR ALA CYS LYS VAL GLU HIS GLU THR LEU LYS GLU
SEQRES 8 E 101 PRO GLN VAL TYR LYS TRP ASP PRO GLU PHE
SEQRES 1 F 8 ILE ASP TRP PHE ASP GLY LYS GLU
FORMUL 7 HOH *517(H2 O)
HELIX 1 1 THR A 47 ASN A 53 1 7
HELIX 2 2 ASP A 55 TYR A 84 1 30
HELIX 3 3 VAL A 134 GLU A 136 5 3
HELIX 4 4 ALA A 137 GLU A 147 1 11
HELIX 5 5 SER A 148 GLU A 159 1 12
HELIX 6 6 GLU A 159 GLY A 172 1 14
HELIX 7 7 GLY A 172 GLY A 177 1 6
HELIX 8 8 GLY A 221 ALA A 224 5 4
HELIX 9 9 THR D 47 ASN D 53 1 7
HELIX 10 10 ASP D 55 TYR D 84 1 30
HELIX 11 11 VAL D 134 GLU D 136 5 3
HELIX 12 12 ALA D 137 GLU D 146 1 10
HELIX 13 13 SER D 148 GLU D 159 1 12
HELIX 14 14 GLU D 159 GLY D 172 1 14
HELIX 15 15 GLY D 172 GLY D 177 1 6
HELIX 16 16 ASP D 249 ASP D 251 5 3
SHEET 1 A 8 TYR A 43 PRO A 45 0
SHEET 2 A 8 GLU A 31 ASN A 37 -1 N HIS A 35 O VAL A 44
SHEET 3 A 8 PHE A 22 VAL A 28 -1 N THR A 24 O TYR A 36
SHEET 4 A 8 HIS A 3 MET A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 A 8 THR A 92 ILE A 101 -1 O PHE A 97 N TYR A 7
SHEET 6 A 8 ILE A 107 TYR A 115 -1 O GLN A 112 N MET A 96
SHEET 7 A 8 ARG A 118 LEU A 123 -1 O ILE A 121 N SER A 113
SHEET 8 A 8 PHE A 130 ALA A 132 -1 O THR A 131 N ALA A 122
SHEET 1 B 4 GLU A 183 LYS A 189 0
SHEET 2 B 4 LEU A 195 PHE A 204 -1 O SER A 198 N TRP A 187
SHEET 3 B 4 TYR A 237 ALA A 245 -1 O ALA A 245 N LEU A 195
SHEET 4 B 4 HIS A 225 SER A 226 -1 N HIS A 225 O THR A 242
SHEET 1 C 4 GLU A 183 LYS A 189 0
SHEET 2 C 4 LEU A 195 PHE A 204 -1 O SER A 198 N TRP A 187
SHEET 3 C 4 TYR A 237 ALA A 245 -1 O ALA A 245 N LEU A 195
SHEET 4 C 4 VAL A 230 PRO A 231 -1 N VAL A 230 O HIS A 238
SHEET 1 D 4 ALA A 218 VAL A 219 0
SHEET 2 D 4 VAL A 210 LYS A 215 -1 N LYS A 215 O ALA A 218
SHEET 3 D 4 TYR A 253 GLU A 258 -1 O GLN A 254 N LEU A 214
SHEET 4 D 4 GLY A 266 SER A 269 -1 O TYR A 268 N CYS A 255
SHEET 1 E 4 LYS B 5 SER B 10 0
SHEET 2 E 4 ASN B 20 PHE B 29 -1 O PHE B 25 N GLN B 7
SHEET 3 E 4 PHE B 61 PHE B 69 -1 O PHE B 61 N PHE B 29
SHEET 4 E 4 ALA B 48 PHE B 55 -1 N GLN B 49 O HIS B 66
SHEET 1 F 4 VAL B 43 PRO B 44 0
SHEET 2 F 4 SER B 35 LYS B 40 -1 N LYS B 40 O VAL B 43
SHEET 3 F 4 TYR B 77 GLU B 82 -1 O LYS B 80 N THR B 37
SHEET 4 F 4 GLN B 90 LYS B 93 -1 O GLN B 90 N VAL B 81
SHEET 1 G 8 VAL D 44 PRO D 45 0
SHEET 2 G 8 GLU D 31 ASN D 37 -1 N HIS D 35 O VAL D 44
SHEET 3 G 8 PHE D 22 VAL D 28 -1 N THR D 24 O TYR D 36
SHEET 4 G 8 HIS D 3 MET D 12 -1 N ARG D 6 O TYR D 27
SHEET 5 G 8 THR D 92 ILE D 101 -1 O PHE D 97 N TYR D 7
SHEET 6 G 8 ILE D 107 TYR D 115 -1 O GLN D 112 N MET D 96
SHEET 7 G 8 ARG D 118 ASP D 124 -1 O LEU D 123 N ARG D 111
SHEET 8 G 8 THR D 129 ALA D 132 -1 O THR D 131 N ALA D 122
SHEET 1 H 4 GLU D 183 ALA D 191 0
SHEET 2 H 4 ILE D 194 PHE D 204 -1 O SER D 198 N TRP D 187
SHEET 3 H 4 TYR D 237 ALA D 245 -1 O ILE D 243 N LEU D 197
SHEET 4 H 4 HIS D 225 SER D 226 -1 N HIS D 225 O THR D 242
SHEET 1 I 4 GLU D 183 ALA D 191 0
SHEET 2 I 4 ILE D 194 PHE D 204 -1 O SER D 198 N TRP D 187
SHEET 3 I 4 TYR D 237 ALA D 245 -1 O ILE D 243 N LEU D 197
SHEET 4 I 4 VAL D 230 PRO D 231 -1 N VAL D 230 O HIS D 238
SHEET 1 J 4 VAL D 219 ARG D 220 0
SHEET 2 J 4 VAL D 210 LYS D 215 -1 N LYS D 215 O VAL D 219
SHEET 3 J 4 TYR D 253 GLU D 258 -1 O GLN D 254 N LEU D 214
SHEET 4 J 4 GLY D 266 TYR D 268 -1 O TYR D 268 N CYS D 255
SHEET 1 K 4 LYS E 5 SER E 10 0
SHEET 2 K 4 ASN E 20 PHE E 29 -1 O ASN E 23 N TYR E 9
SHEET 3 K 4 PHE E 61 PHE E 69 -1 O VAL E 65 N CYS E 24
SHEET 4 K 4 GLN E 49 TYR E 50 -1 N GLN E 49 O HIS E 66
SHEET 1 L 4 LYS E 5 SER E 10 0
SHEET 2 L 4 ASN E 20 PHE E 29 -1 O ASN E 23 N TYR E 9
SHEET 3 L 4 PHE E 61 PHE E 69 -1 O VAL E 65 N CYS E 24
SHEET 4 L 4 SER E 54 PHE E 55 -1 N SER E 54 O GLN E 62
SHEET 1 M 4 VAL E 43 PRO E 44 0
SHEET 2 M 4 SER E 35 LYS E 40 -1 N LYS E 40 O VAL E 43
SHEET 3 M 4 TYR E 77 GLU E 82 -1 O LYS E 80 N THR E 37
SHEET 4 M 4 GLN E 90 LYS E 93 -1 O TYR E 92 N CYS E 79
SSBOND 1 CYS A 99 CYS A 161 1555 1555 2.04
SSBOND 2 CYS A 199 CYS A 255 1555 1555 2.03
SSBOND 3 CYS B 24 CYS B 79 1555 1555 2.03
SSBOND 4 CYS D 99 CYS D 161 1555 1555 2.04
SSBOND 5 CYS D 199 CYS D 255 1555 1555 2.03
SSBOND 6 CYS E 24 CYS E 79 1555 1555 2.03
CISPEP 1 PRO A 15 GLY A 16 0 -3.01
CISPEP 2 TYR A 205 PRO A 206 0 6.49
CISPEP 3 HIS B 30 PRO B 31 0 4.21
CISPEP 4 PRO D 15 GLY D 16 0 -4.75
CISPEP 5 TYR D 205 PRO D 206 0 3.70
CISPEP 6 HIS E 30 PRO E 31 0 0.97
CRYST1 166.196 40.286 131.585 90.00 119.71 90.00 C 1 2 1 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 0.006017 0.000000 0.003433 0.00000
SCALE2 0.000000 0.024823 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008750 0.00000
(ATOM LINES ARE NOT SHOWN.)
END