HEADER IMMUNE SYSTEM 01-AUG-07 2QTE
TITLE CRYSTAL STRUCTURE OF NOVEL IMMUNE-TYPE RECEPTOR 11 EXTRACELLULAR
TITLE 2 FRAGMENT MUTANT N30D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOVEL IMMUNE-TYPE RECEPTOR 11;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR FRAGMENT;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ICTALURUS PUNCTATUS;
SOURCE 3 STRAIN: WILD TYPE;
SOURCE 4 GENE: NITR11;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TUNER;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-BLUE1
KEYWDS IMMUNOGLOBULIN VARIABLE DOMAIN-LIKE BETA-SANDWICH, IMMUNE-TYPE
KEYWDS 2 RECEPTOR, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.OSTROV,J.A.HERNANDEZ PRADA,R.N.HAIRE,J.P.CANNON,A.T.MAGIS,
AUTHOR 2 K.M.BAILEY,G.W.LITMAN
REVDAT 5 20-OCT-21 2QTE 1 SEQADV
REVDAT 4 25-OCT-17 2QTE 1 REMARK
REVDAT 3 29-DEC-09 2QTE 1 JRNL
REVDAT 2 24-FEB-09 2QTE 1 VERSN
REVDAT 1 02-SEP-08 2QTE 0
JRNL AUTH J.P.CANNON,R.N.HAIRE,A.T.MAGIS,D.D.EASON,K.N.WINFREY,
JRNL AUTH 2 J.A.HERNANDEZ PRADA,K.M.BAILEY,J.JAKONCIC,G.W.LITMAN,
JRNL AUTH 3 D.A.OSTROV
JRNL TITL A BONY FISH IMMUNOLOGICAL RECEPTOR OF THE NITR MULTIGENE
JRNL TITL 2 FAMILY MEDIATES ALLOGENEIC RECOGNITION.
JRNL REF IMMUNITY V. 29 228 2008
JRNL REFN ISSN 1074-7613
JRNL PMID 18674935
JRNL DOI 10.1016/J.IMMUNI.2008.05.018
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 32420
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) : 0.200
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1621
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.15
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 119
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 : 3544
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 607
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.23900
REMARK 3 B22 (A**2) : 0.08200
REMARK 3 B33 (A**2) : 0.15700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
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 : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.851 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.898 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.587 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.074 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 29.19
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QTE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9322
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : OXFORD DANFYSIK TOROIDAL
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32478
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.16000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 8000, 0.2M CALCIUM ACETATE
REMARK 280 HYDRATE, 0.1M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 32.23800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.81600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.33100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.81600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.23800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.33100
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER. THERE ARE TWO BIOLOGICAL
REMARK 300 UNITS IN THE ASYMMETRIC UNIT (CHAINS A & B AND CHAINS D & C).
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2610 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 1
REMARK 465 ASP A 2
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 MET D 1
REMARK 465 ASP D 2
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 LYS A 25 69.76 -111.77
REMARK 500 LYS A 29 -33.35 -36.24
REMARK 500 LYS A 63 73.91 -111.20
REMARK 500 ASN A 72 -159.96 -147.47
REMARK 500 ASN B 72 -154.22 -151.31
REMARK 500 SER C 51 96.94 -68.69
REMARK 500 SER D 52 173.04 179.22
REMARK 500 LYS D 63 73.31 -119.59
REMARK 500 ASN D 72 -157.43 -151.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QHL RELATED DB: PDB
REMARK 900 RELATED ID: 2QJD RELATED DB: PDB
REMARK 900 RELATED ID: 2QQQ RELATED DB: PDB
DBREF 2QTE A 2 111 UNP Q8UWK4 Q8UWK4_ICTPU 22 131
DBREF 2QTE B 2 111 UNP Q8UWK4 Q8UWK4_ICTPU 22 131
DBREF 2QTE C 2 111 UNP Q8UWK4 Q8UWK4_ICTPU 22 131
DBREF 2QTE D 2 111 UNP Q8UWK4 Q8UWK4_ICTPU 22 131
SEQADV 2QTE MET A 1 UNP Q8UWK4 INITIATING METHIONINE
SEQADV 2QTE ASP A 30 UNP Q8UWK4 ASN 50 ENGINEERED MUTATION
SEQADV 2QTE MET B 1 UNP Q8UWK4 INITIATING METHIONINE
SEQADV 2QTE ASP B 30 UNP Q8UWK4 ASN 50 ENGINEERED MUTATION
SEQADV 2QTE MET C 1 UNP Q8UWK4 INITIATING METHIONINE
SEQADV 2QTE ASP C 30 UNP Q8UWK4 ASN 50 ENGINEERED MUTATION
SEQADV 2QTE MET D 1 UNP Q8UWK4 INITIATING METHIONINE
SEQADV 2QTE ASP D 30 UNP Q8UWK4 ASN 50 ENGINEERED MUTATION
SEQRES 1 A 111 MET ASP ILE LYS GLU LEU HIS VAL LYS THR VAL LYS ARG
SEQRES 2 A 111 GLY GLU ASN VAL THR MET GLU CYS SER MET SER LYS VAL
SEQRES 3 A 111 THR ASN LYS ASP ASN LEU ALA TRP TYR ARG GLN SER PHE
SEQRES 4 A 111 GLY LYS VAL PRO GLN TYR PHE VAL ARG TYR TYR SER SER
SEQRES 5 A 111 ASN SER GLY TYR LYS PHE ALA GLU GLY PHE LYS ASP SER
SEQRES 6 A 111 ARG PHE SER MET THR VAL ASN ASP GLN LYS PHE ASP LEU
SEQRES 7 A 111 ASN ILE ILE GLY ALA ARG GLU ASP ASP GLY GLY GLU TYR
SEQRES 8 A 111 PHE CYS GLY GLU VAL GLU GLY ILE ILE ILE LYS PHE THR
SEQRES 9 A 111 SER GLY THR ARG LEU GLN PHE
SEQRES 1 B 111 MET ASP ILE LYS GLU LEU HIS VAL LYS THR VAL LYS ARG
SEQRES 2 B 111 GLY GLU ASN VAL THR MET GLU CYS SER MET SER LYS VAL
SEQRES 3 B 111 THR ASN LYS ASP ASN LEU ALA TRP TYR ARG GLN SER PHE
SEQRES 4 B 111 GLY LYS VAL PRO GLN TYR PHE VAL ARG TYR TYR SER SER
SEQRES 5 B 111 ASN SER GLY TYR LYS PHE ALA GLU GLY PHE LYS ASP SER
SEQRES 6 B 111 ARG PHE SER MET THR VAL ASN ASP GLN LYS PHE ASP LEU
SEQRES 7 B 111 ASN ILE ILE GLY ALA ARG GLU ASP ASP GLY GLY GLU TYR
SEQRES 8 B 111 PHE CYS GLY GLU VAL GLU GLY ILE ILE ILE LYS PHE THR
SEQRES 9 B 111 SER GLY THR ARG LEU GLN PHE
SEQRES 1 C 111 MET ASP ILE LYS GLU LEU HIS VAL LYS THR VAL LYS ARG
SEQRES 2 C 111 GLY GLU ASN VAL THR MET GLU CYS SER MET SER LYS VAL
SEQRES 3 C 111 THR ASN LYS ASP ASN LEU ALA TRP TYR ARG GLN SER PHE
SEQRES 4 C 111 GLY LYS VAL PRO GLN TYR PHE VAL ARG TYR TYR SER SER
SEQRES 5 C 111 ASN SER GLY TYR LYS PHE ALA GLU GLY PHE LYS ASP SER
SEQRES 6 C 111 ARG PHE SER MET THR VAL ASN ASP GLN LYS PHE ASP LEU
SEQRES 7 C 111 ASN ILE ILE GLY ALA ARG GLU ASP ASP GLY GLY GLU TYR
SEQRES 8 C 111 PHE CYS GLY GLU VAL GLU GLY ILE ILE ILE LYS PHE THR
SEQRES 9 C 111 SER GLY THR ARG LEU GLN PHE
SEQRES 1 D 111 MET ASP ILE LYS GLU LEU HIS VAL LYS THR VAL LYS ARG
SEQRES 2 D 111 GLY GLU ASN VAL THR MET GLU CYS SER MET SER LYS VAL
SEQRES 3 D 111 THR ASN LYS ASP ASN LEU ALA TRP TYR ARG GLN SER PHE
SEQRES 4 D 111 GLY LYS VAL PRO GLN TYR PHE VAL ARG TYR TYR SER SER
SEQRES 5 D 111 ASN SER GLY TYR LYS PHE ALA GLU GLY PHE LYS ASP SER
SEQRES 6 D 111 ARG PHE SER MET THR VAL ASN ASP GLN LYS PHE ASP LEU
SEQRES 7 D 111 ASN ILE ILE GLY ALA ARG GLU ASP ASP GLY GLY GLU TYR
SEQRES 8 D 111 PHE CYS GLY GLU VAL GLU GLY ILE ILE ILE LYS PHE THR
SEQRES 9 D 111 SER GLY THR ARG LEU GLN PHE
FORMUL 5 HOH *607(H2 O)
HELIX 1 1 ASN A 28 ASP A 30 5 3
HELIX 2 2 ARG A 84 GLY A 88 5 5
HELIX 3 3 ASN B 28 ASP B 30 5 3
HELIX 4 4 ARG B 84 GLY B 88 5 5
HELIX 5 5 ASN C 28 ASP C 30 5 3
HELIX 6 6 ARG C 84 GLY C 88 5 5
HELIX 7 7 SER D 22 VAL D 26 5 5
HELIX 8 8 ASN D 28 ASP D 30 5 3
HELIX 9 9 ARG D 84 GLY D 88 5 5
SHEET 1 A 6 HIS A 7 THR A 10 0
SHEET 2 A 6 ILE A 100 GLN A 110 1 O GLN A 110 N LYS A 9
SHEET 3 A 6 GLY A 89 GLU A 97 -1 N GLU A 97 O ILE A 100
SHEET 4 A 6 LEU A 32 GLN A 37 -1 N GLN A 37 O GLU A 90
SHEET 5 A 6 GLN A 44 TYR A 49 -1 O TYR A 49 N LEU A 32
SHEET 6 A 6 TYR A 56 PHE A 58 -1 O LYS A 57 N ARG A 48
SHEET 1 B 3 VAL A 17 MET A 19 0
SHEET 2 B 3 PHE A 76 ILE A 80 -1 O LEU A 78 N MET A 19
SHEET 3 B 3 PHE A 67 VAL A 71 -1 N SER A 68 O ASN A 79
SHEET 1 C 6 HIS B 7 THR B 10 0
SHEET 2 C 6 ILE B 100 GLN B 110 1 O ARG B 108 N LYS B 9
SHEET 3 C 6 GLY B 89 GLU B 97 -1 N GLU B 97 O ILE B 100
SHEET 4 C 6 LEU B 32 GLN B 37 -1 N GLN B 37 O GLU B 90
SHEET 5 C 6 GLN B 44 TYR B 49 -1 O GLN B 44 N ARG B 36
SHEET 6 C 6 TYR B 56 PHE B 58 -1 O LYS B 57 N ARG B 48
SHEET 1 D 3 ASN B 16 MET B 19 0
SHEET 2 D 3 PHE B 76 ILE B 81 -1 O LEU B 78 N MET B 19
SHEET 3 D 3 PHE B 67 VAL B 71 -1 N SER B 68 O ASN B 79
SHEET 1 E 6 HIS C 7 THR C 10 0
SHEET 2 E 6 ILE C 100 GLN C 110 1 O GLN C 110 N LYS C 9
SHEET 3 E 6 GLY C 89 GLU C 97 -1 N CYS C 93 O SER C 105
SHEET 4 E 6 LEU C 32 GLN C 37 -1 N GLN C 37 O GLU C 90
SHEET 5 E 6 GLN C 44 TYR C 49 -1 O PHE C 46 N TRP C 34
SHEET 6 E 6 TYR C 56 PHE C 58 -1 O LYS C 57 N ARG C 48
SHEET 1 F 3 VAL C 17 MET C 19 0
SHEET 2 F 3 PHE C 76 ILE C 80 -1 O ILE C 80 N VAL C 17
SHEET 3 F 3 PHE C 67 VAL C 71 -1 N THR C 70 O ASP C 77
SHEET 1 G 6 HIS D 7 THR D 10 0
SHEET 2 G 6 ILE D 100 GLN D 110 1 O ARG D 108 N HIS D 7
SHEET 3 G 6 GLY D 89 GLU D 97 -1 N TYR D 91 O THR D 107
SHEET 4 G 6 LEU D 32 GLN D 37 -1 N GLN D 37 O GLU D 90
SHEET 5 G 6 GLN D 44 TYR D 49 -1 O GLN D 44 N ARG D 36
SHEET 6 G 6 TYR D 56 PHE D 58 -1 O LYS D 57 N ARG D 48
SHEET 1 H 3 VAL D 17 MET D 19 0
SHEET 2 H 3 PHE D 76 ILE D 80 -1 O LEU D 78 N MET D 19
SHEET 3 H 3 PHE D 67 VAL D 71 -1 N SER D 68 O ASN D 79
SSBOND 1 CYS A 21 CYS A 93 1555 1555 2.02
SSBOND 2 CYS B 21 CYS B 93 1555 1555 2.05
SSBOND 3 CYS C 21 CYS C 93 1555 1555 2.08
SSBOND 4 CYS D 21 CYS D 93 1555 1555 2.09
CRYST1 64.476 68.662 99.632 90.00 90.00 90.00 P 21 21 21 16
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 0.015510 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014564 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010037 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
