HEADER TRANSFERASE 09-FEB-18 6CDT
TITLE STRUCTURE OF HUMAN ANAPLASTIC LYMPHOMA KINASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALK TYROSINE KINASE RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ANAPLASTIC LYMPHOMA KINASE;
COMPND 5 EC: 2.7.10.1;
COMPND 6 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: ALK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 2 RZ-2014;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1491790;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PFASTBAC1
KEYWDS KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MCTIGUE,Y.L.DENG,W.LIU,A.BROOUN
REVDAT 2 27-FEB-19 6CDT 1 JRNL
REVDAT 1 20-FEB-19 6CDT 0
JRNL AUTH T.W.JOHNSON,B.BOLANOS,A.BROOUN,R.A.GALLEGO,D.GEHLHAAR,
JRNL AUTH 2 M.JALAIE,M.MCTIGUE,S.TIMOFEEVSKI
JRNL TITL REVIVING B-FACTORS: ACTIVATING ALK MUTATIONS INCREASE
JRNL TITL 2 PROTEIN DYNAMICS OF THE UNPHOSPHORYLATED KINASE.
JRNL REF ACS MED CHEM LETT V. 9 872 2018
JRNL REFN ISSN 1948-5875
JRNL PMID 30258533
JRNL DOI 10.1021/ACSMEDCHEMLETT.8B00348
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 109585.250
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29196
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM SELECTION
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1356
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 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 : 2299
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 276
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.70
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 : 0.38
REMARK 3 BSOL : 54.14
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 6CDT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 87
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29890
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.29100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX 2005
REMARK 200 STARTING MODEL: 2XP2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZED BY THE HANGING DROP VAPOR
REMARK 280 DIFFUSION METHOD AT 13 DEGREES CELSIUS BY MIXING EQUAL VOLUMES
REMARK 280 OF A PURIFIED PROTEIN (11-15 MG/ML) SOLUTION WITH A
REMARK 280 CRYSTALLIZATION SOLUTION CONTAINING 0.15 M AMMONIUM SULFATE, 9 -
REMARK 280 10.5% (W/V) MONOMETHYLETHER POLYETHYLENE GLYCOL (MW 5 K) AND 0.1
REMARK 280 M MES BUFFER IN A PH RANGE OF 5.3-5.6., VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 286K
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 26.01400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.36450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.73600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.36450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.01400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.73600
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 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 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 1085
REMARK 465 ALA A 1086
REMARK 465 HIS A 1087
REMARK 465 HIS A 1088
REMARK 465 HIS A 1089
REMARK 465 HIS A 1090
REMARK 465 HIS A 1091
REMARK 465 HIS A 1092
REMARK 465 HIS A 1124
REMARK 465 GLY A 1125
REMARK 465 SER A 1136
REMARK 465 GLY A 1137
REMARK 465 MET A 1138
REMARK 465 PRO A 1139
REMARK 465 ASN A 1140
REMARK 465 ASP A 1141
REMARK 465 PRO A 1142
REMARK 465 SER A 1143
REMARK 465 ALA A 1280
REMARK 465 SER A 1281
REMARK 465 TYR A 1282
REMARK 465 TYR A 1283
REMARK 465 ARG A 1284
REMARK 465 LYS A 1285
REMARK 465 TYR A 1401
REMARK 465 GLY A 1402
REMARK 465 PRO A 1403
REMARK 465 LEU A 1404
REMARK 465 VAL A 1405
REMARK 465 GLU A 1406
REMARK 465 GLU A 1407
REMARK 465 GLU A 1408
REMARK 465 GLU A 1409
REMARK 465 LYS A 1410
REMARK 465 VAL A 1411
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 ARG A1248 -9.45 80.06
REMARK 500 ASP A1249 52.98 -150.67
REMARK 500 SER A1332 -0.57 74.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6CDT A 1093 1411 UNP Q9UM73 ALK_HUMAN 1093 1411
SEQADV 6CDT MET A 1085 UNP Q9UM73 EXPRESSION TAG
SEQADV 6CDT ALA A 1086 UNP Q9UM73 EXPRESSION TAG
SEQADV 6CDT HIS A 1087 UNP Q9UM73 EXPRESSION TAG
SEQADV 6CDT HIS A 1088 UNP Q9UM73 EXPRESSION TAG
SEQADV 6CDT HIS A 1089 UNP Q9UM73 EXPRESSION TAG
SEQADV 6CDT HIS A 1090 UNP Q9UM73 EXPRESSION TAG
SEQADV 6CDT HIS A 1091 UNP Q9UM73 EXPRESSION TAG
SEQADV 6CDT HIS A 1092 UNP Q9UM73 EXPRESSION TAG
SEQRES 1 A 327 MET ALA HIS HIS HIS HIS HIS HIS ASN PRO ASN TYR CYS
SEQRES 2 A 327 PHE ALA GLY LYS THR SER SER ILE SER ASP LEU LYS GLU
SEQRES 3 A 327 VAL PRO ARG LYS ASN ILE THR LEU ILE ARG GLY LEU GLY
SEQRES 4 A 327 HIS GLY ALA PHE GLY GLU VAL TYR GLU GLY GLN VAL SER
SEQRES 5 A 327 GLY MET PRO ASN ASP PRO SER PRO LEU GLN VAL ALA VAL
SEQRES 6 A 327 LYS THR LEU PRO GLU VAL CYS SER GLU GLN ASP GLU LEU
SEQRES 7 A 327 ASP PHE LEU MET GLU ALA LEU ILE ILE SER LYS PHE ASN
SEQRES 8 A 327 HIS GLN ASN ILE VAL ARG CYS ILE GLY VAL SER LEU GLN
SEQRES 9 A 327 SER LEU PRO ARG PHE ILE LEU LEU GLU LEU MET ALA GLY
SEQRES 10 A 327 GLY ASP LEU LYS SER PHE LEU ARG GLU THR ARG PRO ARG
SEQRES 11 A 327 PRO SER GLN PRO SER SER LEU ALA MET LEU ASP LEU LEU
SEQRES 12 A 327 HIS VAL ALA ARG ASP ILE ALA CYS GLY CYS GLN TYR LEU
SEQRES 13 A 327 GLU GLU ASN HIS PHE ILE HIS ARG ASP ILE ALA ALA ARG
SEQRES 14 A 327 ASN CYS LEU LEU THR CYS PRO GLY PRO GLY ARG VAL ALA
SEQRES 15 A 327 LYS ILE GLY ASP PHE GLY MET ALA ARG ASP ILE TYR ARG
SEQRES 16 A 327 ALA SER TYR TYR ARG LYS GLY GLY CYS ALA MET LEU PRO
SEQRES 17 A 327 VAL LYS TRP MET PRO PRO GLU ALA PHE MET GLU GLY ILE
SEQRES 18 A 327 PHE THR SER LYS THR ASP THR TRP SER PHE GLY VAL LEU
SEQRES 19 A 327 LEU TRP GLU ILE PHE SER LEU GLY TYR MET PRO TYR PRO
SEQRES 20 A 327 SER LYS SER ASN GLN GLU VAL LEU GLU PHE VAL THR SER
SEQRES 21 A 327 GLY GLY ARG MET ASP PRO PRO LYS ASN CYS PRO GLY PRO
SEQRES 22 A 327 VAL TYR ARG ILE MET THR GLN CYS TRP GLN HIS GLN PRO
SEQRES 23 A 327 GLU ASP ARG PRO ASN PHE ALA ILE ILE LEU GLU ARG ILE
SEQRES 24 A 327 GLU TYR CYS THR GLN ASP PRO ASP VAL ILE ASN THR ALA
SEQRES 25 A 327 LEU PRO ILE GLU TYR GLY PRO LEU VAL GLU GLU GLU GLU
SEQRES 26 A 327 LYS VAL
FORMUL 2 HOH *276(H2 O)
HELIX 1 AA1 SER A 1106 LEU A 1108 5 3
HELIX 2 AA2 PRO A 1112 ILE A 1116 5 5
HELIX 3 AA3 SER A 1157 PHE A 1174 1 18
HELIX 4 AA4 LEU A 1204 THR A 1211 1 8
HELIX 5 AA5 ALA A 1222 ASN A 1243 1 22
HELIX 6 AA6 ALA A 1251 ARG A 1253 5 3
HELIX 7 AA7 PHE A 1271 ARG A 1279 1 9
HELIX 8 AA8 GLY A 1287 LEU A 1291 5 5
HELIX 9 AA9 PRO A 1292 MET A 1296 5 5
HELIX 10 AB1 PRO A 1297 GLY A 1304 1 8
HELIX 11 AB2 THR A 1307 SER A 1324 1 18
HELIX 12 AB3 SER A 1334 SER A 1344 1 11
HELIX 13 AB4 PRO A 1355 TRP A 1366 1 12
HELIX 14 AB5 GLN A 1369 ARG A 1373 5 5
HELIX 15 AB6 ASN A 1375 ASP A 1389 1 15
HELIX 16 AB7 ASP A 1389 ASN A 1394 1 6
SHEET 1 AA1 2 ASN A1095 PHE A1098 0
SHEET 2 AA1 2 LYS A1101 SER A1104 -1 O SER A1103 N TYR A1096
SHEET 1 AA2 5 THR A1117 GLY A1123 0
SHEET 2 AA2 5 VAL A1130 GLN A1134 -1 O GLU A1132 N ILE A1119
SHEET 3 AA2 5 GLN A1146 THR A1151 -1 O VAL A1147 N GLY A1133
SHEET 4 AA2 5 PHE A1193 GLU A1197 -1 O LEU A1196 N ALA A1148
SHEET 5 AA2 5 CYS A1182 SER A1186 -1 N GLY A1184 O LEU A1195
SHEET 1 AA3 3 GLY A1202 ASP A1203 0
SHEET 2 AA3 3 CYS A1255 LEU A1257 -1 O LEU A1257 N GLY A1202
SHEET 3 AA3 3 ALA A1266 ILE A1268 -1 O LYS A1267 N LEU A1256
CISPEP 1 LEU A 1190 PRO A 1191 0 -3.20
CRYST1 52.028 57.472 104.729 90.00 90.00 90.00 P 21 21 21 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 0.019220 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009548 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
