HEADER PROTEIN BINDING 22-AUG-15 5DC0
TITLE CRYSTAL STRUCTURE OF MONOBODY GG3/ABL1 SH2 DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FN,COLD-INSOLUBLE GLOBULIN,CIG;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TYROSINE-PROTEIN KINASE ABL1;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 1,ABELSON
COMPND 10 TYROSINE-PROTEIN KINASE 1,PROTO-ONCOGENE C-ABL,P150;
COMPND 11 EC: 2.7.10.2;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FN1, FN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PHFT2;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: ABL1, ABL, JTK7;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHFT2
KEYWDS ENGINEERED BINDING PROTEIN, ANTIBODY MIMIC, PROTEIN-PROTEIN COMPLEX,
KEYWDS 2 SH2 DOMAIN, TYROSINE-PROTEIN KINASE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.WOJCIK,G.GRABE,S.KOIDE
REVDAT 6 06-MAR-24 5DC0 1 REMARK
REVDAT 5 04-DEC-19 5DC0 1 REMARK
REVDAT 4 20-SEP-17 5DC0 1 JRNL REMARK
REVDAT 3 11-MAY-16 5DC0 1 JRNL
REVDAT 2 09-MAR-16 5DC0 1 JRNL
REVDAT 1 02-MAR-16 5DC0 0
JRNL AUTH J.WOJCIK,A.J.LAMONTANARA,G.GRABE,A.KOIDE,L.AKIN,B.GERIG,
JRNL AUTH 2 O.HANTSCHEL,S.KOIDE
JRNL TITL ALLOSTERIC INHIBITION OF BCR-ABL KINASE BY HIGH AFFINITY
JRNL TITL 2 MONOBODY INHIBITORS DIRECTED TO THE SRC HOMOLOGY 2
JRNL TITL 3 (SH2)-KINASE INTERFACE.
JRNL REF J.BIOL.CHEM. V. 291 8836 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 26912659
JRNL DOI 10.1074/JBC.M115.707901
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 8914
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 448
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) : 2.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 556
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 33
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1463
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 55
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : -0.26000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.319
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.852
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1503 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2057 ; 1.386 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 187 ; 6.199 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 60 ;34.570 ;22.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 223 ;15.945 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;12.394 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 237 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1137 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 5DC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212986.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : SI 111 SIDE BOUNCE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9392
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 65.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM TARTRATE PH=8 AND 25% W/V
REMARK 280 POLYETHYLENE GLYCOL 3350, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 65.71850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.67400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.71850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.67400
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 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 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 VAL A 1
REMARK 465 SER A 2
REMARK 465 PRO B 131
REMARK 465 SER B 132
REMARK 465 ASN B 133
REMARK 465 TYR B 134
REMARK 465 ILE B 135
REMARK 465 THR B 136
REMARK 465 PRO B 137
REMARK 465 VAL B 138
REMARK 465 ASN B 139
REMARK 465 SER B 140
REMARK 465 ARG B 239
REMARK 465 ASN B 240
REMARK 465 LYS B 241
REMARK 465 PRO B 242
REMARK 465 THR B 243
REMARK 465 VAL B 244
REMARK 465 TYR B 245
REMARK 465 GLY B 246
REMARK 465 VAL B 247
REMARK 465 SER B 248
REMARK 465 PRO B 249
REMARK 465 ASN B 250
REMARK 465 TYR B 251
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 ASN A 42 49.02 -86.11
REMARK 500 TRP A 81 43.20 -98.81
REMARK 500 GLU B 187 62.59 38.27
REMARK 500 HIS B 233 -56.18 -134.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DC9 RELATED DB: PDB
REMARK 900 RELATED ID: 5DC4 RELATED DB: PDB
DBREF 5DC0 A 1 93 PDB 5DC0 5DC0 1 93
DBREF 5DC0 B 131 251 UNP P00519 ABL1_HUMAN 131 251
SEQRES 1 A 93 VAL SER ASP VAL PRO THR LYS LEU GLU VAL VAL ALA ALA
SEQRES 2 A 93 THR PRO THR SER LEU LEU ILE SER TRP ASP ALA PRO ALA
SEQRES 3 A 93 VAL THR VAL VAL HIS TYR VAL ILE THR TYR GLY GLU THR
SEQRES 4 A 93 GLY GLY ASN SER PRO VAL GLN GLU PHE THR VAL PRO GLY
SEQRES 5 A 93 SER LYS SER THR ALA THR ILE SER GLY LEU SER PRO GLY
SEQRES 6 A 93 VAL ASP TYR THR ILE THR VAL TYR ALA LEU LEU SER SER
SEQRES 7 A 93 SER HIS TRP VAL TYR GLU SER PRO ILE SER ILE ASN TYR
SEQRES 8 A 93 ARG THR
SEQRES 1 B 121 PRO SER ASN TYR ILE THR PRO VAL ASN SER LEU GLU LYS
SEQRES 2 B 121 HIS SER TRP TYR HIS GLY PRO VAL SER ARG ASN ALA ALA
SEQRES 3 B 121 GLU TYR LEU LEU SER SER GLY ILE ASN GLY SER PHE LEU
SEQRES 4 B 121 VAL ARG GLU SER GLU SER SER PRO GLY GLN ARG SER ILE
SEQRES 5 B 121 SER LEU ARG TYR GLU GLY ARG VAL TYR HIS TYR ARG ILE
SEQRES 6 B 121 ASN THR ALA SER ASP GLY LYS LEU TYR VAL SER SER GLU
SEQRES 7 B 121 SER ARG PHE ASN THR LEU ALA GLU LEU VAL HIS HIS HIS
SEQRES 8 B 121 SER THR VAL ALA ASP GLY LEU ILE THR THR LEU HIS TYR
SEQRES 9 B 121 PRO ALA PRO LYS ARG ASN LYS PRO THR VAL TYR GLY VAL
SEQRES 10 B 121 SER PRO ASN TYR
FORMUL 3 HOH *55(H2 O)
HELIX 1 AA1 SER B 152 LEU B 160 1 9
HELIX 2 AA2 THR B 213 SER B 222 1 10
SHEET 1 AA1 3 THR A 6 ALA A 13 0
SHEET 2 AA1 3 LEU A 18 ASP A 23 -1 O ASP A 23 N THR A 6
SHEET 3 AA1 3 THR A 56 ILE A 59 -1 O ALA A 57 N ILE A 20
SHEET 1 AA2 4 GLN A 46 PRO A 51 0
SHEET 2 AA2 4 HIS A 31 GLU A 38 -1 N TYR A 32 O VAL A 50
SHEET 3 AA2 4 ASP A 67 LEU A 75 -1 O TYR A 73 N VAL A 33
SHEET 4 AA2 4 ILE A 87 ARG A 92 -1 O TYR A 91 N TYR A 68
SHEET 1 AA3 4 TYR B 147 PRO B 150 0
SHEET 2 AA3 4 SER B 167 GLU B 172 1 O VAL B 170 N HIS B 148
SHEET 3 AA3 4 ARG B 180 TYR B 186 -1 O ARG B 185 N SER B 167
SHEET 4 AA3 4 ARG B 189 ARG B 194 -1 O TYR B 193 N ILE B 182
SHEET 1 AA4 3 TYR B 147 PRO B 150 0
SHEET 2 AA4 3 SER B 167 GLU B 172 1 O VAL B 170 N HIS B 148
SHEET 3 AA4 3 TYR B 234 PRO B 235 1 O TYR B 234 N PHE B 168
SHEET 1 AA5 3 ASN B 196 THR B 197 0
SHEET 2 AA5 3 LEU B 203 TYR B 204 -1 O TYR B 204 N ASN B 196
SHEET 3 AA5 3 ARG B 210 PHE B 211 -1 O PHE B 211 N LEU B 203
CRYST1 131.437 37.348 39.705 90.00 98.42 90.00 C 1 2 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 0.007608 0.000000 0.001127 0.00000
SCALE2 0.000000 0.026775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025460 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
