HEADER IMMUNE SYSTEM 29-JUL-07 2QRT
TITLE CRYSTAL STRUCTURE OF A DISULFIDE TRAPPED SINGLE CHAIN TRIMER COMPOSED
TITLE 2 OF THE MHC I HEAVY CHAIN H-2KB Y84C, BETA-2MICROGLOBULIN, AND
TITLE 3 OVALBUMIN-DERIVED PEPTIDE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN K-B ALPHA CHAIN,
COMPND 3 BETA-2 MICROGLOBULIN, OVALBUMIN-DERIVED PEPTIDE;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: FUSION PROTEIN OF OVALBUMIN-DERIVED PEPTIDE, LINKER, BETA-2
COMPND 6 MICROGLOBULIN, LINKER, AND H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN K-B
COMPND 7 ALPHA CHAIN EXTRACELLULAR DOMAIN;
COMPND 8 SYNONYM: H-2KB;
COMPND 9 ENGINEERED: YES;
COMPND 10 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-K1, H2-K, B2M;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS MHC-I, OVA, SINGLE CHAIN MHC-I, GLYCOPROTEIN, IMMUNE RESPONSE,
KEYWDS 2 MEMBRANE, MHC I, TRANSMEMBRANE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR V.E.MITAKSOV,D.H.FREMONT
REVDAT 5 30-AUG-23 2QRT 1 REMARK
REVDAT 4 20-OCT-21 2QRT 1 SEQADV
REVDAT 3 26-JUL-17 2QRT 1 SOURCE
REVDAT 2 24-FEB-09 2QRT 1 VERSN
REVDAT 1 06-NOV-07 2QRT 0
JRNL AUTH V.MITAKSOV,S.M.TRUSCOTT,L.LYBARGER,J.M.CONNOLLY,T.H.HANSEN,
JRNL AUTH 2 D.H.FREMONT
JRNL TITL STRUCTURAL ENGINEERING OF PMHC REAGENTS FOR T CELL VACCINES
JRNL TITL 2 AND DIAGNOSTICS.
JRNL REF CHEM.BIOL. V. 14 909 2007
JRNL REFN ISSN 1074-5521
JRNL PMID 17719490
JRNL DOI 10.1016/J.CHEMBIOL.2007.07.010
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 89351
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) : 0.208
REMARK 3 FREE R VALUE : 0.239
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 : 6388
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 755
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.95
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 2QRT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000043974.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96928
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
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) : 0.49100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.610
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RJY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 6000, 100 MM MES, PH 6.3,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 44.55000
REMARK 290 SMTRY3 2 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 300 REMARK: THERE ARE TWO MOLECULES OF THE BIOLOGICAL ASSEMBLY IN THE
REMARK 300 ASSYMETRIC UNIT
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 100B
REMARK 465 GLY A 101B
REMARK 465 GLY A 102B
REMARK 465 GLY A 103B
REMARK 465 SER A 104B
REMARK 465 GLY A 105B
REMARK 465 GLY A 106B
REMARK 465 GLY A 107B
REMARK 465 GLY A 108B
REMARK 465 SER A 109B
REMARK 465 GLY A 110B
REMARK 465 GLY A 111B
REMARK 465 GLY A 112B
REMARK 465 GLY A 113B
REMARK 465 SER A 114B
REMARK 465 GLY A 115B
REMARK 465 GLY A 116B
REMARK 465 GLY A 117B
REMARK 465 GLY A 118B
REMARK 465 SER A 119B
REMARK 465 PRO A 277H
REMARK 465 PRO A 278H
REMARK 465 SER A 279H
REMARK 465 THR A 280H
REMARK 465 GLY B 100B
REMARK 465 GLY B 101B
REMARK 465 GLY B 102B
REMARK 465 GLY B 103B
REMARK 465 SER B 104B
REMARK 465 GLY B 105B
REMARK 465 GLY B 106B
REMARK 465 GLY B 107B
REMARK 465 GLY B 108B
REMARK 465 SER B 109B
REMARK 465 GLY B 110B
REMARK 465 GLY B 111B
REMARK 465 GLY B 112B
REMARK 465 GLY B 113B
REMARK 465 SER B 114B
REMARK 465 GLY B 115B
REMARK 465 GLY B 116B
REMARK 465 GLY B 117B
REMARK 465 GLY B 118B
REMARK 465 SER B 119B
REMARK 465 PRO B 277H
REMARK 465 PRO B 278H
REMARK 465 SER B 279H
REMARK 465 THR B 280H
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 GLY A 21P OD2 ASP A 119H 2.04
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 GLY A 19P N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 LEU B 272H CA - CB - CG ANGL. DEV. = 17.3 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 TRP A 60B -8.92 77.18
REMARK 500 ASP A 98B -62.75 -14.15
REMARK 500 ASN A 176H -88.89 -3.36
REMARK 500 GLU A 196H -142.18 59.12
REMARK 500 ASP A 197H 32.28 -85.26
REMARK 500 ASN A 220H 70.11 36.89
REMARK 500 TRP B 60B -8.78 80.98
REMARK 500 ARG B 14H 72.07 -155.62
REMARK 500 PRO B 15H 121.17 -39.46
REMARK 500 LEU B 17H 13.39 -52.22
REMARK 500 ASP B 29H 72.64 41.51
REMARK 500 ASP B 30H -3.12 57.84
REMARK 500 PRO B 43H 111.29 -36.84
REMARK 500 GLN B 114H 85.07 -154.96
REMARK 500 LEU B 180H -5.94 71.61
REMARK 500 GLU B 196H -141.65 54.56
REMARK 500 ASP B 197H 19.98 -69.82
REMARK 500 ASN B 220H 71.11 48.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QRI RELATED DB: PDB
REMARK 900 RELATED ID: 2QRS RELATED DB: PDB
DBREF 2QRT A 1H 280H UNP P01901 HA1B_MOUSE 22 301
DBREF 2QRT B 1H 280H UNP P01901 HA1B_MOUSE 22 301
DBREF 2QRT A 1B 99B UNP Q91XJ8 Q91XJ8_MOUSE 21 119
DBREF 2QRT B 1B 99B UNP Q91XJ8 Q91XJ8_MOUSE 21 119
SEQADV 2QRT GLY A 9P UNP P01901 LINKER
SEQADV 2QRT CYS A 10P UNP P01901 LINKER
SEQADV 2QRT GLY A 11P UNP P01901 LINKER
SEQADV 2QRT ALA A 12P UNP P01901 LINKER
SEQADV 2QRT SER A 13P UNP P01901 LINKER
SEQADV 2QRT GLY A 14P UNP P01901 LINKER
SEQADV 2QRT GLY A 15P UNP P01901 LINKER
SEQADV 2QRT GLY A 16P UNP P01901 LINKER
SEQADV 2QRT GLY A 17P UNP P01901 LINKER
SEQADV 2QRT SER A 18P UNP P01901 LINKER
SEQADV 2QRT GLY A 19P UNP P01901 LINKER
SEQADV 2QRT GLY A 20P UNP P01901 LINKER
SEQADV 2QRT GLY A 21P UNP P01901 LINKER
SEQADV 2QRT GLY A 22P UNP P01901 LINKER
SEQADV 2QRT SER A 23P UNP P01901 LINKER
SEQADV 2QRT GLY A 100B UNP P01901 LINKER
SEQADV 2QRT GLY A 101B UNP P01901 LINKER
SEQADV 2QRT GLY A 102B UNP P01901 LINKER
SEQADV 2QRT GLY A 103B UNP P01901 LINKER
SEQADV 2QRT SER A 104B UNP P01901 LINKER
SEQADV 2QRT GLY A 105B UNP P01901 LINKER
SEQADV 2QRT GLY A 106B UNP P01901 LINKER
SEQADV 2QRT GLY A 107B UNP P01901 LINKER
SEQADV 2QRT GLY A 108B UNP P01901 LINKER
SEQADV 2QRT SER A 109B UNP P01901 LINKER
SEQADV 2QRT GLY A 110B UNP P01901 LINKER
SEQADV 2QRT GLY A 111B UNP P01901 LINKER
SEQADV 2QRT GLY A 112B UNP P01901 LINKER
SEQADV 2QRT GLY A 113B UNP P01901 LINKER
SEQADV 2QRT SER A 114B UNP P01901 LINKER
SEQADV 2QRT GLY A 115B UNP P01901 LINKER
SEQADV 2QRT GLY A 116B UNP P01901 LINKER
SEQADV 2QRT GLY A 117B UNP P01901 LINKER
SEQADV 2QRT GLY A 118B UNP P01901 LINKER
SEQADV 2QRT SER A 119B UNP P01901 LINKER
SEQADV 2QRT CYS A 84H UNP P01901 TYR 105 ENGINEERED MUTATION
SEQADV 2QRT GLY B 9P UNP P01901 LINKER
SEQADV 2QRT CYS B 10P UNP P01901 LINKER
SEQADV 2QRT GLY B 11P UNP P01901 LINKER
SEQADV 2QRT ALA B 12P UNP P01901 LINKER
SEQADV 2QRT SER B 13P UNP P01901 LINKER
SEQADV 2QRT GLY B 14P UNP P01901 LINKER
SEQADV 2QRT GLY B 15P UNP P01901 LINKER
SEQADV 2QRT GLY B 16P UNP P01901 LINKER
SEQADV 2QRT GLY B 17P UNP P01901 LINKER
SEQADV 2QRT SER B 18P UNP P01901 LINKER
SEQADV 2QRT GLY B 19P UNP P01901 LINKER
SEQADV 2QRT GLY B 20P UNP P01901 LINKER
SEQADV 2QRT GLY B 21P UNP P01901 LINKER
SEQADV 2QRT GLY B 22P UNP P01901 LINKER
SEQADV 2QRT SER B 23P UNP P01901 LINKER
SEQADV 2QRT GLY B 100B UNP P01901 LINKER
SEQADV 2QRT GLY B 101B UNP P01901 LINKER
SEQADV 2QRT GLY B 102B UNP P01901 LINKER
SEQADV 2QRT GLY B 103B UNP P01901 LINKER
SEQADV 2QRT SER B 104B UNP P01901 LINKER
SEQADV 2QRT GLY B 105B UNP P01901 LINKER
SEQADV 2QRT GLY B 106B UNP P01901 LINKER
SEQADV 2QRT GLY B 107B UNP P01901 LINKER
SEQADV 2QRT GLY B 108B UNP P01901 LINKER
SEQADV 2QRT SER B 109B UNP P01901 LINKER
SEQADV 2QRT GLY B 110B UNP P01901 LINKER
SEQADV 2QRT GLY B 111B UNP P01901 LINKER
SEQADV 2QRT GLY B 112B UNP P01901 LINKER
SEQADV 2QRT GLY B 113B UNP P01901 LINKER
SEQADV 2QRT SER B 114B UNP P01901 LINKER
SEQADV 2QRT GLY B 115B UNP P01901 LINKER
SEQADV 2QRT GLY B 116B UNP P01901 LINKER
SEQADV 2QRT GLY B 117B UNP P01901 LINKER
SEQADV 2QRT GLY B 118B UNP P01901 LINKER
SEQADV 2QRT SER B 119B UNP P01901 LINKER
SEQADV 2QRT CYS B 84H UNP P01901 TYR 105 ENGINEERED MUTATION
SEQRES 1 A 422 SER ILE ILE ASN PHE GLU LYS LEU GLY CYS GLY ALA SER
SEQRES 2 A 422 GLY GLY GLY GLY SER GLY GLY GLY GLY SER ILE GLN LYS
SEQRES 3 A 422 THR PRO GLN ILE GLN VAL TYR SER ARG HIS PRO PRO GLU
SEQRES 4 A 422 ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR VAL THR GLN
SEQRES 5 A 422 PHE HIS PRO PRO HIS ILE GLU ILE GLN MET LEU LYS ASN
SEQRES 6 A 422 GLY LYS LYS ILE PRO LYS VAL GLU MET SER ASP MET SER
SEQRES 7 A 422 PHE SER LYS ASP TRP SER PHE TYR ILE LEU ALA HIS THR
SEQRES 8 A 422 GLU PHE THR PRO THR GLU THR ASP THR TYR ALA CYS ARG
SEQRES 9 A 422 VAL LYS HIS ALA SER MET ALA GLU PRO LYS THR VAL TYR
SEQRES 10 A 422 TRP ASP ARG ASP MET GLY GLY GLY GLY SER GLY GLY GLY
SEQRES 11 A 422 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY
SEQRES 12 A 422 PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 13 A 422 PRO GLY LEU GLY GLU PRO ARG TYR MET GLU VAL GLY TYR
SEQRES 14 A 422 VAL ASP ASP THR GLU PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 15 A 422 GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP MET GLU
SEQRES 16 A 422 GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN LYS
SEQRES 17 A 422 ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU ARG
SEQRES 18 A 422 THR LEU LEU GLY CYS TYR ASN GLN SER LYS GLY GLY SER
SEQRES 19 A 422 HIS THR ILE GLN VAL ILE SER GLY CYS GLU VAL GLY SER
SEQRES 20 A 422 ASP GLY ARG LEU LEU ARG GLY TYR GLN GLN TYR ALA TYR
SEQRES 21 A 422 ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 22 A 422 THR TRP THR ALA ALA ASP MET ALA ALA LEU ILE THR LYS
SEQRES 23 A 422 HIS LYS TRP GLU GLN ALA GLY GLU ALA GLU ARG LEU ARG
SEQRES 24 A 422 ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG ARG
SEQRES 25 A 422 TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR ASP
SEQRES 26 A 422 SER PRO LYS ALA HIS VAL THR HIS HIS SER ARG PRO GLU
SEQRES 27 A 422 ASP LYS VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 28 A 422 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 29 A 422 GLU LEU ILE GLN ASP MET GLU LEU VAL GLU THR ARG PRO
SEQRES 30 A 422 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL VAL
SEQRES 31 A 422 VAL PRO LEU GLY LYS GLU GLN TYR TYR THR CYS HIS VAL
SEQRES 32 A 422 TYR HIS GLN GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 33 A 422 GLU PRO PRO PRO SER THR
SEQRES 1 B 422 SER ILE ILE ASN PHE GLU LYS LEU GLY CYS GLY ALA SER
SEQRES 2 B 422 GLY GLY GLY GLY SER GLY GLY GLY GLY SER ILE GLN LYS
SEQRES 3 B 422 THR PRO GLN ILE GLN VAL TYR SER ARG HIS PRO PRO GLU
SEQRES 4 B 422 ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR VAL THR GLN
SEQRES 5 B 422 PHE HIS PRO PRO HIS ILE GLU ILE GLN MET LEU LYS ASN
SEQRES 6 B 422 GLY LYS LYS ILE PRO LYS VAL GLU MET SER ASP MET SER
SEQRES 7 B 422 PHE SER LYS ASP TRP SER PHE TYR ILE LEU ALA HIS THR
SEQRES 8 B 422 GLU PHE THR PRO THR GLU THR ASP THR TYR ALA CYS ARG
SEQRES 9 B 422 VAL LYS HIS ALA SER MET ALA GLU PRO LYS THR VAL TYR
SEQRES 10 B 422 TRP ASP ARG ASP MET GLY GLY GLY GLY SER GLY GLY GLY
SEQRES 11 B 422 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY
SEQRES 12 B 422 PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER ARG
SEQRES 13 B 422 PRO GLY LEU GLY GLU PRO ARG TYR MET GLU VAL GLY TYR
SEQRES 14 B 422 VAL ASP ASP THR GLU PHE VAL ARG PHE ASP SER ASP ALA
SEQRES 15 B 422 GLU ASN PRO ARG TYR GLU PRO ARG ALA ARG TRP MET GLU
SEQRES 16 B 422 GLN GLU GLY PRO GLU TYR TRP GLU ARG GLU THR GLN LYS
SEQRES 17 B 422 ALA LYS GLY ASN GLU GLN SER PHE ARG VAL ASP LEU ARG
SEQRES 18 B 422 THR LEU LEU GLY CYS TYR ASN GLN SER LYS GLY GLY SER
SEQRES 19 B 422 HIS THR ILE GLN VAL ILE SER GLY CYS GLU VAL GLY SER
SEQRES 20 B 422 ASP GLY ARG LEU LEU ARG GLY TYR GLN GLN TYR ALA TYR
SEQRES 21 B 422 ASP GLY CYS ASP TYR ILE ALA LEU ASN GLU ASP LEU LYS
SEQRES 22 B 422 THR TRP THR ALA ALA ASP MET ALA ALA LEU ILE THR LYS
SEQRES 23 B 422 HIS LYS TRP GLU GLN ALA GLY GLU ALA GLU ARG LEU ARG
SEQRES 24 B 422 ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG ARG
SEQRES 25 B 422 TYR LEU LYS ASN GLY ASN ALA THR LEU LEU ARG THR ASP
SEQRES 26 B 422 SER PRO LYS ALA HIS VAL THR HIS HIS SER ARG PRO GLU
SEQRES 27 B 422 ASP LYS VAL THR LEU ARG CYS TRP ALA LEU GLY PHE TYR
SEQRES 28 B 422 PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY GLU
SEQRES 29 B 422 GLU LEU ILE GLN ASP MET GLU LEU VAL GLU THR ARG PRO
SEQRES 30 B 422 ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL VAL
SEQRES 31 B 422 VAL PRO LEU GLY LYS GLU GLN TYR TYR THR CYS HIS VAL
SEQRES 32 B 422 TYR HIS GLN GLY LEU PRO GLU PRO LEU THR LEU ARG TRP
SEQRES 33 B 422 GLU PRO PRO PRO SER THR
FORMUL 3 HOH *755(H2 O)
HELIX 1 1 ALA A 49H GLU A 55H 5 7
HELIX 2 2 GLY A 56H TYR A 85H 1 30
HELIX 3 3 ASP A 137H GLY A 151H 1 15
HELIX 4 4 GLY A 151H GLY A 162H 1 12
HELIX 5 5 GLY A 162H ARG A 181H 1 20
HELIX 6 6 LYS A 253H GLN A 255H 5 3
HELIX 7 7 ALA B 49H GLU B 55H 5 7
HELIX 8 8 GLY B 56H TYR B 85H 1 30
HELIX 9 9 ASP B 137H GLY B 151H 1 15
HELIX 10 10 GLY B 151H GLY B 162H 1 12
HELIX 11 11 GLY B 162H ASN B 176H 1 15
HELIX 12 12 LYS B 253H GLN B 255H 5 3
SHEET 1 A 4 GLN A 6B SER A 11B 0
SHEET 2 A 4 ASN A 21B PHE A 30B-1 O ASN A 24B N TYR A 10B
SHEET 3 A 4 PHE A 62B PHE A 70B-1 O PHE A 70B N ASN A 21B
SHEET 4 A 4 GLU A 50B MET A 51B-1 N GLU A 50B O HIS A 67B
SHEET 1 B 4 GLN A 6B SER A 11B 0
SHEET 2 B 4 ASN A 21B PHE A 30B-1 O ASN A 24B N TYR A 10B
SHEET 3 B 4 PHE A 62B PHE A 70B-1 O PHE A 70B N ASN A 21B
SHEET 4 B 4 SER A 55B PHE A 56B-1 N SER A 55B O TYR A 63B
SHEET 1 C 4 LYS A 44B LYS A 45B 0
SHEET 2 C 4 GLU A 36B LYS A 41B-1 N LYS A 41B O LYS A 44B
SHEET 3 C 4 TYR A 78B LYS A 83B-1 O ARG A 81B N GLN A 38B
SHEET 4 C 4 LYS A 91B TYR A 94B-1 O VAL A 93B N CYS A 80B
SHEET 1 D 8 GLU A 46H PRO A 47H 0
SHEET 2 D 8 THR A 31H ASP A 37H-1 N ARG A 35H O GLU A 46H
SHEET 3 D 8 ARG A 21H VAL A 28H-1 N GLY A 26H O PHE A 33H
SHEET 4 D 8 HIS A 3H VAL A 12H-1 N PHE A 8H O VAL A 25H
SHEET 5 D 8 THR A 94H VAL A 103H-1 O SER A 99H N TYR A 7H
SHEET 6 D 8 LEU A 109H TYR A 118H-1 O LEU A 110H N GLU A 102H
SHEET 7 D 8 CYS A 121H LEU A 126H-1 O ILE A 124H N TYR A 116H
SHEET 8 D 8 TRP A 133H ALA A 135H-1 O THR A 134H N ALA A 125H
SHEET 1 E 4 LYS A 186H SER A 193H 0
SHEET 2 E 4 LYS A 198H PHE A 208H-1 O THR A 200H N HIS A 192H
SHEET 3 E 4 PHE A 241H PRO A 250H-1 O ALA A 245H N CYS A 203H
SHEET 4 E 4 GLU A 229H LEU A 230H-1 N GLU A 229H O SER A 246H
SHEET 1 F 4 LYS A 186H SER A 193H 0
SHEET 2 F 4 LYS A 198H PHE A 208H-1 O THR A 200H N HIS A 192H
SHEET 3 F 4 PHE A 241H PRO A 250H-1 O ALA A 245H N CYS A 203H
SHEET 4 F 4 ARG A 234H PRO A 235H-1 N ARG A 234H O GLN A 242H
SHEET 1 G 4 GLU A 222H GLU A 223H 0
SHEET 2 G 4 THR A 214H LEU A 219H-1 N LEU A 219H O GLU A 222H
SHEET 3 G 4 TYR A 257H TYR A 262H-1 O TYR A 262H N THR A 214H
SHEET 4 G 4 LEU A 270H LEU A 272H-1 O LEU A 272H N CYS A 259H
SHEET 1 H 4 GLN B 6B SER B 11B 0
SHEET 2 H 4 ASN B 21B PHE B 30B-1 O ASN B 24B N TYR B 10B
SHEET 3 H 4 PHE B 62B PHE B 70B-1 O THR B 68B N LEU B 23B
SHEET 4 H 4 GLU B 50B MET B 51B-1 N GLU B 50B O HIS B 67B
SHEET 1 I 4 GLN B 6B SER B 11B 0
SHEET 2 I 4 ASN B 21B PHE B 30B-1 O ASN B 24B N TYR B 10B
SHEET 3 I 4 PHE B 62B PHE B 70B-1 O THR B 68B N LEU B 23B
SHEET 4 I 4 SER B 55B PHE B 56B-1 N SER B 55B O TYR B 63B
SHEET 1 J 4 LYS B 44B LYS B 45B 0
SHEET 2 J 4 GLU B 36B LYS B 41B-1 N LYS B 41B O LYS B 44B
SHEET 3 J 4 TYR B 78B LYS B 83B-1 O ARG B 81B N GLN B 38B
SHEET 4 J 4 LYS B 91B TYR B 94B-1 O VAL B 93B N CYS B 80B
SHEET 1 K 8 GLU B 46H PRO B 47H 0
SHEET 2 K 8 THR B 31H ASP B 37H-1 N ARG B 35H O GLU B 46H
SHEET 3 K 8 ARG B 21H VAL B 28H-1 N GLU B 24H O PHE B 36H
SHEET 4 K 8 HIS B 3H VAL B 12H-1 N PHE B 8H O VAL B 25H
SHEET 5 K 8 THR B 94H VAL B 103H-1 O VAL B 103H N HIS B 3H
SHEET 6 K 8 LEU B 109H TYR B 118H-1 O LEU B 110H N GLU B 102H
SHEET 7 K 8 CYS B 121H LEU B 126H-1 O ILE B 124H N TYR B 116H
SHEET 8 K 8 TRP B 133H ALA B 135H-1 O THR B 134H N ALA B 125H
SHEET 1 L 4 LYS B 186H SER B 193H 0
SHEET 2 L 4 LYS B 198H PHE B 208H-1 O THR B 200H N HIS B 192H
SHEET 3 L 4 PHE B 241H PRO B 250H-1 O ALA B 245H N CYS B 203H
SHEET 4 L 4 GLU B 229H LEU B 230H-1 N GLU B 229H O SER B 246H
SHEET 1 M 4 LYS B 186H SER B 193H 0
SHEET 2 M 4 LYS B 198H PHE B 208H-1 O THR B 200H N HIS B 192H
SHEET 3 M 4 PHE B 241H PRO B 250H-1 O ALA B 245H N CYS B 203H
SHEET 4 M 4 ARG B 234H PRO B 235H-1 N ARG B 234H O GLN B 242H
SHEET 1 N 4 GLU B 222H GLU B 223H 0
SHEET 2 N 4 THR B 214H LEU B 219H-1 N LEU B 219H O GLU B 222H
SHEET 3 N 4 TYR B 257H TYR B 262H-1 O TYR B 262H N THR B 214H
SHEET 4 N 4 LEU B 270H LEU B 272H-1 O LEU B 272H N CYS B 259H
SSBOND 1 CYS A 10P CYS A 84H 1555 1555 2.05
SSBOND 2 CYS A 25B CYS A 80B 1555 1555 2.04
SSBOND 3 CYS A 101H CYS A 164H 1555 1555 2.07
SSBOND 4 CYS A 203H CYS A 259H 1555 1555 2.04
SSBOND 5 CYS B 10P CYS B 84H 1555 1555 2.05
SSBOND 6 CYS B 25B CYS B 80B 1555 1555 2.04
SSBOND 7 CYS B 101H CYS B 164H 1555 1555 2.08
SSBOND 8 CYS B 203H CYS B 259H 1555 1555 2.03
CISPEP 1 HIS A 31B PRO A 32B 0 -1.42
CISPEP 2 TYR A 209H PRO A 210H 0 -0.45
CISPEP 3 HIS B 31B PRO B 32B 0 0.54
CISPEP 4 TYR B 209H PRO B 210H 0 -0.08
CRYST1 66.600 89.100 88.600 90.00 110.90 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 0.015015 0.000000 0.005734 0.00000
SCALE2 0.000000 0.011223 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012082 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
