HEADER TRANSFERASE 14-MAR-05 1X03
TITLE CRYSTAL STRUCTURE OF ENDOPHILIN BAR DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SH3-CONTAINING GRB2-LIKE PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ENDOPHILIN BAR DOMAIN;
COMPND 5 SYNONYM: ENDOPHILIN A1, SH3 DOMAIN PROTEIN 2A, ENDOPHILIN 1, EEN-B1;
COMPND 6 EC: 2.3.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P3
KEYWDS BAR DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MASUDA,S.TAKEDA,M.SONE,Y.KAMIOKA,H.MORI,N.MOCHIZUKI
REVDAT 4 13-JUL-11 1X03 1 VERSN
REVDAT 3 24-FEB-09 1X03 1 VERSN
REVDAT 2 11-JUL-06 1X03 1 JRNL
REVDAT 1 02-MAY-06 1X03 0
JRNL AUTH M.MASUDA,S.TAKEDA,M.SONE,T.OHKI,H.MORI,Y.KAMIOKA,N.MOCHIZUKI
JRNL TITL ENDOPHILIN BAR DOMAIN DRIVES MEMBRANE CURVATURE BY TWO NEWLY
JRNL TITL 2 IDENTIFIED STRUCTURE-BASED MECHANISMS
JRNL REF EMBO J. V. 25 2889 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16763557
JRNL DOI 10.1038/SJ.EMBOJ.7601176
REMARK 2
REMARK 2 RESOLUTION. 3.10 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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 14449
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) : 0.236
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 738
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4230
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 73
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 : 1698
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.80
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) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : 0.66
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) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.65
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.03
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 : NULL
REMARK 3 BSOL : NULL
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 1X03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAR-05.
REMARK 100 THE RCSB ID CODE IS RCSB024210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-04; 27-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 90; 90
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; SPRING-8
REMARK 200 BEAMLINE : BL45PX; BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797; 0.9793, 0.9794, 0.9817,
REMARK 200 0.9817
REMARK 200 MONOCHROMATOR : DIAMOND; SI 111
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER; ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14464
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, ETHYLENE GLYCOL, GLYCEROL,
REMARK 280 BENZAMIZINE/HCL, HEPES, DTT, PH 7.4, MICRODIALYSIS, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 63.71200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 63.71200
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.81750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.71200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.90875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.71200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.72625
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 63.71200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.71200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.81750
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 63.71200
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 74.72625
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 63.71200
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 24.90875
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED BY THE TWO
REMARK 300 FOLD AXIS.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 127.42400
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 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 GLY A -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MSE A 1
REMARK 465 SER A 2
REMARK 465 VAL A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLN A 9
REMARK 465 PHE A 10
REMARK 465 HIS A 11
REMARK 465 LYS A 12
REMARK 465 ALA A 13
REMARK 465 THR A 14
REMARK 465 GLN A 15
REMARK 465 LYS A 16
REMARK 465 VAL A 17
REMARK 465 SER A 18
REMARK 465 GLU A 19
REMARK 465 LYS A 20
REMARK 465 VAL A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 ALA A 24
REMARK 465 GLU A 25
REMARK 465 ASN A 72
REMARK 465 THR A 73
REMARK 465 MSE A 74
REMARK 465 SER A 75
REMARK 465 LYS A 76
REMARK 465 ILE A 77
REMARK 465 ARG A 78
REMARK 465 GLY A 79
REMARK 465 GLN A 80
REMARK 465 GLU A 81
REMARK 465 LYS A 82
REMARK 465 GLY A 83
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 NH1 ARG A 184 OE2 GLU A 188 2.14
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 MSE A 70 -57.46 -134.05
REMARK 500 ARG A 102 -71.14 -67.18
REMARK 500 CYS A 108 -160.05 -74.79
REMARK 500 PHE A 139 -50.18 -131.14
REMARK 500 LYS A 149 -99.76 -93.96
REMARK 500 ARG A 174 56.26 -101.65
REMARK 500 MSE A 207 20.16 -79.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X04 RELATED DB: PDB
REMARK 900 ENDOPHILIN BAR DOMAIN (APPENDAGE-LESS MUTANT)
DBREF 1X03 A 1 247 UNP Q99962 SH3G2_HUMAN 1 247
SEQADV 1X03 GLY A -4 UNP Q99962 LINKER
SEQADV 1X03 PRO A -3 UNP Q99962 LINKER
SEQADV 1X03 LEU A -2 UNP Q99962 LINKER
SEQADV 1X03 GLY A -1 UNP Q99962 LINKER
SEQADV 1X03 SER A 0 UNP Q99962 LINKER
SEQADV 1X03 MSE A 1 UNP Q99962 MET 1 MODIFIED RESIDUE
SEQADV 1X03 MSE A 36 UNP Q99962 MET 36 MODIFIED RESIDUE
SEQADV 1X03 MSE A 48 UNP Q99962 MET 48 MODIFIED RESIDUE
SEQADV 1X03 MSE A 51 UNP Q99962 MET 51 MODIFIED RESIDUE
SEQADV 1X03 MSE A 70 UNP Q99962 MET 70 MODIFIED RESIDUE
SEQADV 1X03 MSE A 74 UNP Q99962 MET 74 MODIFIED RESIDUE
SEQADV 1X03 MSE A 97 UNP Q99962 MET 97 MODIFIED RESIDUE
SEQADV 1X03 MSE A 121 UNP Q99962 MET 121 MODIFIED RESIDUE
SEQADV 1X03 MSE A 201 UNP Q99962 MET 201 MODIFIED RESIDUE
SEQADV 1X03 MSE A 207 UNP Q99962 MET 207 MODIFIED RESIDUE
SEQRES 1 A 252 GLY PRO LEU GLY SER MSE SER VAL ALA GLY LEU LYS LYS
SEQRES 2 A 252 GLN PHE HIS LYS ALA THR GLN LYS VAL SER GLU LYS VAL
SEQRES 3 A 252 GLY GLY ALA GLU GLY THR LYS LEU ASP ASP ASP PHE LYS
SEQRES 4 A 252 GLU MSE GLU ARG LYS VAL ASP VAL THR SER ARG ALA VAL
SEQRES 5 A 252 MSE GLU ILE MSE THR LYS THR ILE GLU TYR LEU GLN PRO
SEQRES 6 A 252 ASN PRO ALA SER ARG ALA LYS LEU SER MSE ILE ASN THR
SEQRES 7 A 252 MSE SER LYS ILE ARG GLY GLN GLU LYS GLY PRO GLY TYR
SEQRES 8 A 252 PRO GLN ALA GLU ALA LEU LEU ALA GLU ALA MSE LEU LYS
SEQRES 9 A 252 PHE GLY ARG GLU LEU GLY ASP ASP CYS ASN PHE GLY PRO
SEQRES 10 A 252 ALA LEU GLY GLU VAL GLY GLU ALA MSE ARG GLU LEU SER
SEQRES 11 A 252 GLU VAL LYS ASP SER LEU ASP ILE GLU VAL LYS GLN ASN
SEQRES 12 A 252 PHE ILE ASP PRO LEU GLN ASN LEU HIS ASP LYS ASP LEU
SEQRES 13 A 252 ARG GLU ILE GLN HIS HIS LEU LYS LYS LEU GLU GLY ARG
SEQRES 14 A 252 ARG LEU ASP PHE ASP TYR LYS LYS LYS ARG GLN GLY LYS
SEQRES 15 A 252 ILE PRO ASP GLU GLU LEU ARG GLN ALA LEU GLU LYS PHE
SEQRES 16 A 252 ASP GLU SER LYS GLU ILE ALA GLU SER SER MSE PHE ASN
SEQRES 17 A 252 LEU LEU GLU MSE ASP ILE GLU GLN VAL SER GLN LEU SER
SEQRES 18 A 252 ALA LEU VAL GLN ALA GLN LEU GLU TYR HIS LYS GLN ALA
SEQRES 19 A 252 VAL GLN ILE LEU GLN GLN VAL THR VAL ARG LEU GLU GLU
SEQRES 20 A 252 ARG ILE ARG GLN ALA
MODRES 1X03 MSE A 36 MET SELENOMETHIONINE
MODRES 1X03 MSE A 48 MET SELENOMETHIONINE
MODRES 1X03 MSE A 51 MET SELENOMETHIONINE
MODRES 1X03 MSE A 70 MET SELENOMETHIONINE
MODRES 1X03 MSE A 97 MET SELENOMETHIONINE
MODRES 1X03 MSE A 121 MET SELENOMETHIONINE
MODRES 1X03 MSE A 201 MET SELENOMETHIONINE
MODRES 1X03 MSE A 207 MET SELENOMETHIONINE
HET MSE A 36 8
HET MSE A 48 8
HET MSE A 51 8
HET MSE A 70 8
HET MSE A 97 8
HET MSE A 121 8
HET MSE A 201 8
HET MSE A 207 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
HELIX 1 1 ASP A 30 GLN A 59 1 30
HELIX 2 2 SER A 64 SER A 69 1 6
HELIX 3 3 GLN A 88 GLY A 105 1 18
HELIX 4 4 ASN A 109 PHE A 139 1 31
HELIX 5 5 PHE A 139 LYS A 149 1 11
HELIX 6 6 LYS A 149 ARG A 174 1 26
HELIX 7 7 PRO A 179 MSE A 207 1 29
HELIX 8 8 ASP A 208 ARG A 245 1 38
LINK C GLU A 35 N MSE A 36 1555 1555 1.33
LINK C MSE A 36 N GLU A 37 1555 1555 1.33
LINK C VAL A 47 N MSE A 48 1555 1555 1.33
LINK C MSE A 48 N GLU A 49 1555 1555 1.33
LINK C ILE A 50 N MSE A 51 1555 1555 1.33
LINK C MSE A 51 N THR A 52 1555 1555 1.33
LINK C SER A 69 N MSE A 70 1555 1555 1.33
LINK C MSE A 70 N ILE A 71 1555 1555 1.33
LINK C ALA A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N LEU A 98 1555 1555 1.33
LINK C ALA A 120 N MSE A 121 1555 1555 1.33
LINK C MSE A 121 N ARG A 122 1555 1555 1.33
LINK C SER A 200 N MSE A 201 1555 1555 1.33
LINK C MSE A 201 N PHE A 202 1555 1555 1.33
LINK C GLU A 206 N MSE A 207 1555 1555 1.33
LINK C MSE A 207 N ASP A 208 1555 1555 1.33
CRYST1 127.424 127.424 99.635 90.00 90.00 90.00 I 41 8
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 0.007848 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010037 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
