HEADER IMMUNE SYSTEM 30-SEP-14 4V1P
TITLE BTN3 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BUTYROPHILIN SUBFAMILY 3 MEMBER A1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 325-512;
COMPND 5 SYNONYM: BUTYROPHILIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS IMMUNE SYSTEM, IMMUNE SIGNALLING
EXPDTA X-RAY DIFFRACTION
AUTHOR L.C.JAMES
REVDAT 1 22-JUL-15 4V1P 0
JRNL AUTH D.A.RHODES,H.CHEN,A.J.PRICE,A.H.KEEBLE,M.S.DAVEY,L.C.JAMES,
JRNL AUTH 2 M.EBERL,J.TROWSDALE
JRNL TITL ACTIVATION OF HUMAN GAMMADELTA T CELLS BY CYTOSOLIC
JRNL TITL 2 INTERACTIONS OF BTN3A1 WITH SOLUBLE PHOSPHOANTIGENS AND THE
JRNL TITL 3 CYTOSKELETAL ADAPTOR PERIPLAKIN.
JRNL REF J.IMMUNOL. V. 194 2390 2015
JRNL REFN ISSN 0022-1767
JRNL PMID 25637025
JRNL DOI 10.4049/JIMMUNOL.1401064
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.92
REMARK 3 NUMBER OF REFLECTIONS : 13333
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 + TEST SET) : 0.16780
REMARK 3 R VALUE (WORKING SET) : 0.16507
REMARK 3 FREE R VALUE : 0.22205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 702
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.045
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.098
REMARK 3 REFLECTION IN BIN (WORKING SET) : 872
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.186
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.271
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1531
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.313
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.73
REMARK 3 B22 (A**2) : 1.10
REMARK 3 B33 (A**2) : -0.37
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1578 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1472 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2146 ; 1.843 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3401 ; 0.873 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 187 ; 7.581 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;33.174 ;23.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 262 ;14.780 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;16.190 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 226 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1762 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 372 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 751 ; 5.066 ; 3.686
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 750 ; 5.065 ; 3.685
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 937 ; 5.509 ; 6.182
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 827 ; 7.954 ; 4.323
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4V1P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-SEP-14.
REMARK 100 THE PDBE ID CODE IS EBI-61876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14316
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 31.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 2.7
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 22.31000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.33200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.31000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.33200
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.2 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 44.62000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 HOH A 2078 O HOH A 2112 1.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 18 O HOH A 2106 2655 1.65
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 ASP A 34 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 53 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 CYS A 76 CA - CB - SG ANGL. DEV. = -7.1 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 ASP A 66 56.85 -105.79
REMARK 500 TRP A 100 148.65 -174.48
REMARK 500 ASN A 132 16.59 -148.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4V1P A 18 205 UNP O00481 BT3A1_HUMAN 325 512
SEQADV 4V1P SER A 202 UNP O00481 THR 509 CONFLICT
SEQRES 1 A 188 ARG HIS SER ALA TYR ASN GLU TRP LYS LYS ALA LEU PHE
SEQRES 2 A 188 LYS PRO ALA ASP VAL ILE LEU ASP PRO LYS THR ALA ASN
SEQRES 3 A 188 PRO ILE LEU LEU VAL SER GLU ASP GLN ARG SER VAL GLN
SEQRES 4 A 188 ARG ALA LYS GLU PRO GLN ASP LEU PRO ASP ASN PRO GLU
SEQRES 5 A 188 ARG PHE ASN TRP HIS TYR CYS VAL LEU GLY CYS GLU SER
SEQRES 6 A 188 PHE ILE SER GLY ARG HIS TYR TRP GLU VAL GLU VAL GLY
SEQRES 7 A 188 ASP ARG LYS GLU TRP HIS ILE GLY VAL CYS SER LYS ASN
SEQRES 8 A 188 VAL GLN ARG LYS GLY TRP VAL LYS MET THR PRO GLU ASN
SEQRES 9 A 188 GLY PHE TRP THR MET GLY LEU THR ASP GLY ASN LYS TYR
SEQRES 10 A 188 ARG THR LEU THR GLU PRO ARG THR ASN LEU LYS LEU PRO
SEQRES 11 A 188 LYS PRO PRO LYS LYS VAL GLY VAL PHE LEU ASP TYR GLU
SEQRES 12 A 188 THR GLY ASP ILE SER PHE TYR ASN ALA VAL ASP GLY SER
SEQRES 13 A 188 HIS ILE HIS THR PHE LEU ASP VAL SER PHE SER GLU ALA
SEQRES 14 A 188 LEU TYR PRO VAL PHE ARG ILE LEU THR LEU GLU PRO THR
SEQRES 15 A 188 ALA LEU SER ILE CYS PRO
FORMUL 2 HOH *119(H2 O)
HELIX 1 1 SER A 20 PHE A 30 1 11
HELIX 2 2 ASP A 38 ALA A 42 5 5
HELIX 3 3 THR A 118 ASN A 121 5 4
SHEET 1 AA 2 LYS A 31 PRO A 32 0
SHEET 2 AA 2 ARG A 87 GLU A 93 1 O ARG A 87 N LYS A 31
SHEET 1 AB 7 LEU A 46 VAL A 48 0
SHEET 2 AB 7 SER A 54 ARG A 57 -1 O GLN A 56 N LEU A 47
SHEET 3 AB 7 LEU A 201 CYS A 204 -1 O LEU A 201 N VAL A 55
SHEET 4 AB 7 ARG A 87 GLU A 93 -1 O GLU A 91 N CYS A 204
SHEET 5 AB 7 LYS A 152 ASP A 158 -1 O VAL A 153 N VAL A 92
SHEET 6 AB 7 ASP A 163 ASN A 168 -1 O ASP A 163 N ASP A 158
SHEET 7 AB 7 HIS A 174 PHE A 178 -1 N ILE A 175 O PHE A 166
SHEET 1 AC 5 LEU A 46 VAL A 48 0
SHEET 2 AC 5 SER A 54 ARG A 57 -1 O GLN A 56 N LEU A 47
SHEET 3 AC 5 LEU A 201 CYS A 204 -1 O LEU A 201 N VAL A 55
SHEET 4 AC 5 ARG A 87 GLU A 93 -1 O GLU A 91 N CYS A 204
SHEET 5 AC 5 LYS A 31 PRO A 32 1 O LYS A 31 N TYR A 89
SHEET 1 AD 6 CYS A 76 LEU A 78 0
SHEET 2 AD 6 LEU A 187 ARG A 192 -1 O PHE A 191 N VAL A 77
SHEET 3 AD 6 TRP A 100 SER A 106 -1 O HIS A 101 N ARG A 192
SHEET 4 AD 6 PHE A 123 THR A 129 -1 O TRP A 124 N VAL A 104
SHEET 5 AD 6 LYS A 133 THR A 136 -1 O LYS A 133 N THR A 129
SHEET 6 AD 6 THR A 142 LEU A 144 -1 O THR A 142 N THR A 136
CISPEP 1 GLU A 139 PRO A 140 0 -2.64
CRYST1 44.620 124.664 38.822 90.00 90.00 90.00 P 21 21 2 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 0.022411 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008022 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025759 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
