HEADER HYDROLASE 15-JUN-16 5LB4
TITLE APO-STRUCTURE OF HUMANISED RADA-MUTANT HUMRADA14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA REPAIR AND RECOMBINATION PROTEIN RADA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS (STRAIN ATCC 43587 / DSM
SOURCE 3 3638 / JCM 8422 / VC1);
SOURCE 4 ORGANISM_TAXID: 186497;
SOURCE 5 STRAIN: ATCC 43587 / DSM 3638 / JCM 8422 / VC1;
SOURCE 6 GENE: RADA, PF1926;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAT4
KEYWDS DNA REPAIR, FRAGMENT BASED DRUG DESIGN, HUMANISATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MARSH,G.FISCHER,T.MOSCHETTI,T.SHARPE,D.SCOTT,M.MORGAN,H.NG,
AUTHOR 2 J.SKIDMORE,A.VENKITARAMAN,C.ABELL,T.L.BLUNDELL,M.HYVONEN
REVDAT 4 07-FEB-24 5LB4 1 REMARK
REVDAT 3 30-AUG-17 5LB4 1 REMARK
REVDAT 2 30-NOV-16 5LB4 1 JRNL
REVDAT 1 19-OCT-16 5LB4 0
JRNL AUTH T.MOSCHETTI,T.SHARPE,G.FISCHER,M.E.MARSH,H.K.NG,M.MORGAN,
JRNL AUTH 2 D.E.SCOTT,T.L.BLUNDELL,A.R VENKITARAMAN,J.SKIDMORE,C.ABELL,
JRNL AUTH 3 M.HYVONEN
JRNL TITL ENGINEERING ARCHEAL SURROGATE SYSTEMS FOR THE DEVELOPMENT OF
JRNL TITL 2 PROTEIN-PROTEIN INTERACTION INHIBITORS AGAINST HUMAN RAD51.
JRNL REF J.MOL.BIOL. V. 428 4589 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 27725183
JRNL DOI 10.1016/J.JMB.2016.10.009
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 14304
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 705
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.93
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2814
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2470
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2677
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.87
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 137
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1645
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 44
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.72280
REMARK 3 B22 (A**2) : -1.49880
REMARK 3 B33 (A**2) : -8.22400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.40910
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.350
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.215
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.176
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.219
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.179
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.908
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1708 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2305 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 619 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 44 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 252 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1708 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 225 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1990 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.18
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.30
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5LB4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97903
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14305
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.290
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: 4A6P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4000, 0.1 M TRIS PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 292K
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 18.90700
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 107
REMARK 465 ALA A 108
REMARK 465 ILE A 249
REMARK 465 GLY A 250
REMARK 465 ARG A 251
REMARK 465 GLY A 252
REMARK 465 ALA A 253
REMARK 465 LEU A 254
REMARK 465 VAL A 297
REMARK 465 GLN A 298
REMARK 465 ALA A 299
REMARK 465 ASN A 300
REMARK 465 GLY A 301
REMARK 465 GLY A 302
REMARK 465 HIS A 303
REMARK 465 ILE A 304
REMARK 465 LEU A 305
REMARK 465 ALA A 306
REMARK 465 HIS A 307
REMARK 465 SER A 308
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 ARG A 257 CG CD NE CZ NH1 NH2
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 ILE A 133 O THR A 310 1.87
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 ASN A 227 54.06 -96.06
REMARK 500 ARG A 257 -32.64 78.37
REMARK 500 GLN A 259 -73.35 -73.31
REMARK 500 LYS A 260 -18.88 -47.89
REMARK 500 LEU A 311 111.74 58.42
REMARK 500 GLU A 335 44.77 -80.42
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5LB4 A 108 349 UNP O74036 RADA_PYRFU 108 349
SEQADV 5LB4 MET A 107 UNP O74036 INITIATING METHIONINE
SEQADV 5LB4 ALA A 168 UNP O74036 VAL 168 ENGINEERED MUTATION
SEQADV 5LB4 MET A 169 UNP O74036 ILE 169 ENGINEERED MUTATION
SEQADV 5LB4 TYR A 170 UNP O74036 TRP 170 ENGINEERED MUTATION
SEQADV 5LB4 ALA A 201 UNP O74036 TYR 201 ENGINEERED MUTATION
SEQADV 5LB4 TYR A 202 UNP O74036 VAL 202 ENGINEERED MUTATION
SEQADV 5LB4 GLN A 213 UNP O74036 LEU 213 ENGINEERED MUTATION
SEQADV 5LB4 LEU A 215 UNP O74036 VAL 215 ENGINEERED MUTATION
SEQADV 5LB4 TYR A 216 UNP O74036 GLN 216 ENGINEERED MUTATION
SEQADV 5LB4 SER A 219 UNP O74036 GLU 219 ENGINEERED MUTATION
SEQADV 5LB4 ALA A 220 UNP O74036 ASP 220 ENGINEERED MUTATION
SEQADV 5LB4 MET A 221 UNP O74036 LYS 221 ENGINEERED MUTATION
SEQADV 5LB4 MET A 222 UNP O74036 ILE 222 ENGINEERED MUTATION
SEQADV 5LB4 VAL A 223 UNP O74036 LYS 223 ENGINEERED MUTATION
SEQADV 5LB4 SER A 225 UNP O74036 LEU 225 ENGINEERED MUTATION
SEQADV 5LB4 TYR A 232 UNP O74036 VAL 232 ENGINEERED MUTATION
SEQADV 5LB4 ARG A 263 UNP O74036 LYS 263 ENGINEERED MUTATION
SEQADV 5LB4 PHE A 264 UNP O74036 HIS 264 ENGINEERED MUTATION
SEQADV 5LB4 MET A 267 UNP O74036 ASP 267 ENGINEERED MUTATION
SEQADV 5LB4 GLU A 274 UNP O74036 LEU 274 ENGINEERED MUTATION
SEQADV 5LB4 PHE A 275 UNP O74036 TYR 275 ENGINEERED MUTATION
SEQADV 5LB4 A UNP O74036 ARG 288 DELETION
SEQADV 5LB4 A UNP O74036 PRO 289 DELETION
SEQADV 5LB4 A UNP O74036 ASP 290 DELETION
SEQADV 5LB4 A UNP O74036 ALA 291 DELETION
SEQADV 5LB4 A UNP O74036 PHE 292 DELETION
SEQADV 5LB4 A UNP O74036 PHE 293 DELETION
SEQADV 5LB4 A UNP O74036 GLY 294 DELETION
SEQADV 5LB4 A UNP O74036 ASP 295 DELETION
SEQADV 5LB4 A UNP O74036 PRO 296 DELETION
SEQADV 5LB4 A UNP O74036 THR 297 DELETION
SEQADV 5LB4 A UNP O74036 ARG 298 DELETION
SEQADV 5LB4 A UNP O74036 PRO 299 DELETION
SEQADV 5LB4 ASN A 300 UNP O74036 ILE 300 ENGINEERED MUTATION
SEQRES 1 A 231 MET ALA THR ILE GLY ARG ILE SER THR GLY SER LYS SER
SEQRES 2 A 231 LEU ASP LYS LEU LEU GLY GLY GLY ILE GLU THR GLN ALA
SEQRES 3 A 231 ILE THR GLU VAL PHE GLY GLU PHE GLY SER GLY LYS THR
SEQRES 4 A 231 GLN LEU ALA HIS THR LEU ALA VAL MET VAL GLN LEU PRO
SEQRES 5 A 231 PRO GLU GLU GLY GLY LEU ASN GLY SER ALA MET TYR ILE
SEQRES 6 A 231 ASP THR GLU ASN THR PHE ARG PRO GLU ARG ILE ARG GLU
SEQRES 7 A 231 ILE ALA GLN ASN ARG GLY LEU ASP PRO ASP GLU VAL LEU
SEQRES 8 A 231 LYS HIS ILE ALA TYR ALA ARG ALA PHE ASN SER ASN HIS
SEQRES 9 A 231 GLN MET GLN LEU LEU TYR GLN ALA SER ALA MET MET VAL
SEQRES 10 A 231 GLU SER LEU ASN THR ASP ARG PRO TYR LYS LEU LEU ILE
SEQRES 11 A 231 VAL ASP SER LEU THR SER HIS PHE ARG SER GLU TYR ILE
SEQRES 12 A 231 GLY ARG GLY ALA LEU ALA GLU ARG GLN GLN LYS LEU ALA
SEQRES 13 A 231 ARG PHE LEU ALA MET LEU HIS ARG LEU ALA ASN GLU PHE
SEQRES 14 A 231 ASP ILE ALA VAL PHE VAL THR ASN GLN VAL GLN ALA ASN
SEQRES 15 A 231 GLY GLY HIS ILE LEU ALA HIS SER ALA THR LEU ARG VAL
SEQRES 16 A 231 TYR LEU ARG LYS GLY LYS GLY GLY LYS ARG ILE ALA ARG
SEQRES 17 A 231 LEU ILE ASP ALA PRO HIS LEU PRO GLU GLY GLU ALA VAL
SEQRES 18 A 231 PHE SER ILE THR GLU LYS GLY ILE GLU ASP
FORMUL 2 HOH *44(H2 O)
HELIX 1 AA1 SER A 117 GLY A 125 1 9
HELIX 2 AA2 GLY A 143 VAL A 155 1 13
HELIX 3 AA3 GLN A 156 LEU A 157 5 2
HELIX 4 AA4 PRO A 158 GLY A 162 5 5
HELIX 5 AA5 ARG A 178 ARG A 189 1 12
HELIX 6 AA6 ASP A 192 HIS A 199 1 8
HELIX 7 AA7 ASN A 207 ASN A 227 1 21
HELIX 8 AA8 THR A 241 TYR A 248 1 8
HELIX 9 AA9 GLN A 258 PHE A 275 1 18
SHEET 1 AA1 2 ARG A 112 ILE A 113 0
SHEET 2 AA1 2 ILE A 128 GLU A 129 -1 O ILE A 128 N ILE A 113
SHEET 1 AA2 9 ILE A 200 ARG A 204 0
SHEET 2 AA2 9 SER A 167 ASP A 172 1 N ALA A 168 O ALA A 201
SHEET 3 AA2 9 TYR A 232 ASP A 238 1 O ILE A 236 N MET A 169
SHEET 4 AA2 9 ALA A 278 ASN A 283 1 O ALA A 278 N LYS A 233
SHEET 5 AA2 9 ALA A 132 PHE A 137 1 N THR A 134 O VAL A 281
SHEET 6 AA2 9 ARG A 312 LYS A 317 1 O LEU A 315 N PHE A 137
SHEET 7 AA2 9 LYS A 322 ILE A 328 -1 O ARG A 326 N TYR A 314
SHEET 8 AA2 9 GLU A 337 THR A 343 -1 O PHE A 340 N ARG A 323
SHEET 9 AA2 9 GLY A 346 GLU A 348 -1 O GLU A 348 N SER A 341
CISPEP 1 ASP A 238 SER A 239 0 -1.41
CISPEP 2 LYS A 319 GLY A 320 0 -0.85
CRYST1 39.511 37.814 69.451 90.00 92.40 90.00 P 1 21 1 2
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 0.025309 0.000000 0.001061 0.00000
SCALE2 0.000000 0.026445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014411 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
