HEADER TRANSLATION 07-OCT-13 3WJ9
TITLE CRYSTAL STRUCTURE OF THE EUKARYOTIC INITIATION FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 2A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 2-412;
COMPND 5 SYNONYM: EIF-2A;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 284812;
SOURCE 5 STRAIN: 972 / ATCC 24843;
SOURCE 6 GENE: SPBC4B4.04;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28C
KEYWDS BETA-PROPELLER, TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KASHIWAGI,T.ITO,S.YOKOYAMA
REVDAT 2 24-AUG-22 3WJ9 1 JRNL SEQADV LINK
REVDAT 1 12-MAR-14 3WJ9 0
JRNL AUTH K.KASHIWAGI,T.ITO,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF THE EUKARYOTIC TRANSLATION INITIATION
JRNL TITL 2 FACTOR 2A FROM SCHIZOSACCHAROMYCES POMBE.
JRNL REF J STRUCT FUNCT GENOMICS V. 15 125 2014
JRNL REFN ISSN 1570-0267
JRNL PMID 24569939
JRNL DOI 10.1007/S10969-014-9177-Y
REMARK 2
REMARK 2 RESOLUTION. 2.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 47722
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2397
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 21.6328 - 6.3934 0.92 2787 146 0.2085 0.2196
REMARK 3 2 6.3934 - 5.0965 0.94 2719 162 0.2109 0.2448
REMARK 3 3 5.0965 - 4.4587 0.95 2699 146 0.1645 0.1890
REMARK 3 4 4.4587 - 4.0539 0.95 2660 145 0.1933 0.2179
REMARK 3 5 4.0539 - 3.7650 0.95 2704 131 0.2131 0.2280
REMARK 3 6 3.7650 - 3.5440 0.95 2683 137 0.2390 0.2418
REMARK 3 7 3.5440 - 3.3672 0.95 2637 144 0.2433 0.2569
REMARK 3 8 3.3672 - 3.2211 0.96 2663 122 0.2823 0.2966
REMARK 3 9 3.2211 - 3.0975 0.94 2620 158 0.2951 0.2923
REMARK 3 10 3.0975 - 2.9909 0.95 2633 153 0.3017 0.3155
REMARK 3 11 2.9909 - 2.8976 0.96 2663 123 0.3193 0.3539
REMARK 3 12 2.8976 - 2.8150 0.95 2617 152 0.3316 0.3706
REMARK 3 13 2.8150 - 2.7410 0.95 2632 127 0.3189 0.3864
REMARK 3 14 2.7410 - 2.6742 0.95 2640 129 0.3324 0.3570
REMARK 3 15 2.6742 - 2.6136 0.95 2615 144 0.3513 0.3622
REMARK 3 16 2.6136 - 2.5580 0.95 2639 132 0.3599 0.3850
REMARK 3 17 2.5580 - 2.5069 0.95 2628 141 0.3709 0.3899
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.32
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 6438
REMARK 3 ANGLE : 0.923 8749
REMARK 3 CHIRALITY : 0.040 945
REMARK 3 PLANARITY : 0.005 1143
REMARK 3 DIHEDRAL : 14.279 2333
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3WJ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000096404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47788
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 22.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 49.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 22.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.86100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD, MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHARP, PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 8000, 0.1M MAGNESIUM ACETATE,
REMARK 280 0.1M SODIUM ACETATE, PH 4.3, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.79567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 179.59133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 179.59133
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 89.79567
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 1
REMARK 465 SER A 2
REMARK 465 THR A 235
REMARK 465 GLU A 236
REMARK 465 VAL A 237
REMARK 465 ASN A 249
REMARK 465 LEU A 250
REMARK 465 TYR A 251
REMARK 465 LEU A 252
REMARK 465 LEU A 253
REMARK 465 GLY A 254
REMARK 465 ILE A 255
REMARK 465 CYS A 261
REMARK 465 ARG A 262
REMARK 465 VAL A 263
REMARK 465 ASP A 264
REMARK 465 VAL B 237
REMARK 465 ASP B 238
REMARK 465 LYS B 239
REMARK 465 SER B 240
REMARK 465 ASN B 241
REMARK 465 LEU B 250
REMARK 465 TYR B 251
REMARK 465 LEU B 252
REMARK 465 LEU B 253
REMARK 465 GLY B 254
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 TYR B 245 CB - CA - C ANGL. DEV. = -12.8 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 TYR B 244 -160.67 -174.42
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3WJ9 A 2 412 UNP O74965 EIF2A_SCHPO 2 412
DBREF 3WJ9 B 2 412 UNP O74965 EIF2A_SCHPO 2 412
SEQADV 3WJ9 SER A 1 UNP O74965 EXPRESSION TAG
SEQADV 3WJ9 SER B 1 UNP O74965 EXPRESSION TAG
SEQRES 1 A 412 SER SER GLN LYS SER GLN PHE ALA TYR ARG SER SER LYS
SEQRES 2 A 412 SER ILE GLY LEU VAL ASN ALA SER GLU ASN TYR ALA SER
SEQRES 3 A 412 PRO PRO LYS PHE GLU ALA ILE SER GLU PRO ALA ARG ASN
SEQRES 4 A 412 ALA CYS TYR SER PRO ASN GLY LYS LEU PHE ALA TYR ALA
SEQRES 5 A 412 THR ALA THR GLN VAL VAL ILE ASN ASP THR GLU SER GLY
SEQRES 6 A 412 ALA LYS LEU THR GLN LEU PRO ALA ALA ASN THR TYR GLU
SEQRES 7 A 412 LEU GLY PHE SER PRO LEU GLY LYS TYR LEU SER THR TRP
SEQRES 8 A 412 GLU ARG PRO GLY LYS GLU ALA ASP GLY THR PRO LYS GLN
SEQRES 9 A 412 ASN MSE LYS VAL TRP ASN THR GLU THR GLY GLN LEU VAL
SEQRES 10 A 412 PHE SER PHE VAL GLN ARG ASN GLN THR GLY TRP ASN LEU
SEQRES 11 A 412 GLN TYR THR CYS ASP GLU SER LEU ALA ALA ARG LEU VAL
SEQRES 12 A 412 THR ASN GLU VAL HIS PHE TYR GLU THR GLY ASN MSE SER
SEQRES 13 A 412 LYS GLY PRO ILE ALA LYS LEU ARG VAL GLU GLY ILE SER
SEQRES 14 A 412 ASP PHE ALA LEU SER PRO GLY GLN ASN HIS ALA VAL ALA
SEQRES 15 A 412 VAL PHE ILE PRO GLU LYS LYS GLY ALA PRO ALA SER VAL
SEQRES 16 A 412 ARG THR TYR SER ILE PRO ASN PHE ASN SER PRO LEU SER
SEQRES 17 A 412 GLN LYS THR PHE PHE LYS ALA ASP LYS VAL GLN PHE LYS
SEQRES 18 A 412 TRP ASN ALA LEU GLY THR SER LEU LEU VAL LEU THR GLN
SEQRES 19 A 412 THR GLU VAL ASP LYS SER ASN LYS ASN TYR TYR GLY GLU
SEQRES 20 A 412 THR ASN LEU TYR LEU LEU GLY ILE THR GLY GLN PHE ASP
SEQRES 21 A 412 CYS ARG VAL ASP LEU ASP ARG GLU GLY PRO ILE HIS ASP
SEQRES 22 A 412 VAL CYS TRP ASN ALA ASP SER LYS GLU PHE GLY ILE VAL
SEQRES 23 A 412 TYR GLY TYR MSE PRO ALA LYS THR ALA ILE PHE ASP ASN
SEQRES 24 A 412 ARG ALA ASN VAL VAL SER ILE ILE PRO PRO ALA PRO ARG
SEQRES 25 A 412 ASN THR LEU ILE PHE SER PRO ASN SER ARG TYR ILE LEU
SEQRES 26 A 412 LEU ALA GLY PHE GLY ASN LEU GLN GLY SER ILE ASP ILE
SEQRES 27 A 412 PHE ASP ALA ALA ASN ASN MSE LYS LYS ILE THR THR VAL
SEQRES 28 A 412 GLU ALA ALA ASN CYS THR TYR CYS GLU PHE SER PRO ASP
SEQRES 29 A 412 SER GLN PHE LEU LEU THR ALA VAL THR SER PRO ARG LEU
SEQRES 30 A 412 ARG VAL ASP ASN SER ILE LYS ILE TRP HIS ILE THR GLY
SEQRES 31 A 412 ALA PRO MSE PHE TYR GLU GLU PHE ASN GLU LEU TYR GLN
SEQRES 32 A 412 ALA PHE TRP ARG PRO ARG PRO LEU ASN
SEQRES 1 B 412 SER SER GLN LYS SER GLN PHE ALA TYR ARG SER SER LYS
SEQRES 2 B 412 SER ILE GLY LEU VAL ASN ALA SER GLU ASN TYR ALA SER
SEQRES 3 B 412 PRO PRO LYS PHE GLU ALA ILE SER GLU PRO ALA ARG ASN
SEQRES 4 B 412 ALA CYS TYR SER PRO ASN GLY LYS LEU PHE ALA TYR ALA
SEQRES 5 B 412 THR ALA THR GLN VAL VAL ILE ASN ASP THR GLU SER GLY
SEQRES 6 B 412 ALA LYS LEU THR GLN LEU PRO ALA ALA ASN THR TYR GLU
SEQRES 7 B 412 LEU GLY PHE SER PRO LEU GLY LYS TYR LEU SER THR TRP
SEQRES 8 B 412 GLU ARG PRO GLY LYS GLU ALA ASP GLY THR PRO LYS GLN
SEQRES 9 B 412 ASN MSE LYS VAL TRP ASN THR GLU THR GLY GLN LEU VAL
SEQRES 10 B 412 PHE SER PHE VAL GLN ARG ASN GLN THR GLY TRP ASN LEU
SEQRES 11 B 412 GLN TYR THR CYS ASP GLU SER LEU ALA ALA ARG LEU VAL
SEQRES 12 B 412 THR ASN GLU VAL HIS PHE TYR GLU THR GLY ASN MSE SER
SEQRES 13 B 412 LYS GLY PRO ILE ALA LYS LEU ARG VAL GLU GLY ILE SER
SEQRES 14 B 412 ASP PHE ALA LEU SER PRO GLY GLN ASN HIS ALA VAL ALA
SEQRES 15 B 412 VAL PHE ILE PRO GLU LYS LYS GLY ALA PRO ALA SER VAL
SEQRES 16 B 412 ARG THR TYR SER ILE PRO ASN PHE ASN SER PRO LEU SER
SEQRES 17 B 412 GLN LYS THR PHE PHE LYS ALA ASP LYS VAL GLN PHE LYS
SEQRES 18 B 412 TRP ASN ALA LEU GLY THR SER LEU LEU VAL LEU THR GLN
SEQRES 19 B 412 THR GLU VAL ASP LYS SER ASN LYS ASN TYR TYR GLY GLU
SEQRES 20 B 412 THR ASN LEU TYR LEU LEU GLY ILE THR GLY GLN PHE ASP
SEQRES 21 B 412 CYS ARG VAL ASP LEU ASP ARG GLU GLY PRO ILE HIS ASP
SEQRES 22 B 412 VAL CYS TRP ASN ALA ASP SER LYS GLU PHE GLY ILE VAL
SEQRES 23 B 412 TYR GLY TYR MSE PRO ALA LYS THR ALA ILE PHE ASP ASN
SEQRES 24 B 412 ARG ALA ASN VAL VAL SER ILE ILE PRO PRO ALA PRO ARG
SEQRES 25 B 412 ASN THR LEU ILE PHE SER PRO ASN SER ARG TYR ILE LEU
SEQRES 26 B 412 LEU ALA GLY PHE GLY ASN LEU GLN GLY SER ILE ASP ILE
SEQRES 27 B 412 PHE ASP ALA ALA ASN ASN MSE LYS LYS ILE THR THR VAL
SEQRES 28 B 412 GLU ALA ALA ASN CYS THR TYR CYS GLU PHE SER PRO ASP
SEQRES 29 B 412 SER GLN PHE LEU LEU THR ALA VAL THR SER PRO ARG LEU
SEQRES 30 B 412 ARG VAL ASP ASN SER ILE LYS ILE TRP HIS ILE THR GLY
SEQRES 31 B 412 ALA PRO MSE PHE TYR GLU GLU PHE ASN GLU LEU TYR GLN
SEQRES 32 B 412 ALA PHE TRP ARG PRO ARG PRO LEU ASN
MODRES 3WJ9 MSE A 106 MET SELENOMETHIONINE
MODRES 3WJ9 MSE A 155 MET SELENOMETHIONINE
MODRES 3WJ9 MSE A 290 MET SELENOMETHIONINE
MODRES 3WJ9 MSE A 345 MET SELENOMETHIONINE
MODRES 3WJ9 MSE A 393 MET SELENOMETHIONINE
MODRES 3WJ9 MSE B 106 MET SELENOMETHIONINE
MODRES 3WJ9 MSE B 155 MET SELENOMETHIONINE
MODRES 3WJ9 MSE B 290 MET SELENOMETHIONINE
MODRES 3WJ9 MSE B 345 MET SELENOMETHIONINE
MODRES 3WJ9 MSE B 393 MET SELENOMETHIONINE
HET MSE A 106 8
HET MSE A 155 8
HET MSE A 290 8
HET MSE A 345 8
HET MSE A 393 8
HET MSE B 106 8
HET MSE B 155 8
HET MSE B 290 8
HET MSE B 345 8
HET MSE B 393 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 3 HOH *61(H2 O)
HELIX 1 1 SER A 21 ASN A 23 5 3
SHEET 1 A 3 ILE A 15 ASN A 19 0
SHEET 2 A 3 GLN A 6 SER A 11 -1 N PHE A 7 O VAL A 18
SHEET 3 A 3 LEU A 401 TRP A 406 -1 O PHE A 405 N ALA A 8
SHEET 1 B 4 ALA A 37 TYR A 42 0
SHEET 2 B 4 LEU A 48 THR A 53 -1 O ALA A 52 N ARG A 38
SHEET 3 B 4 VAL A 57 ASP A 61 -1 O ASN A 60 N PHE A 49
SHEET 4 B 4 LYS A 67 LEU A 71 -1 O LEU A 68 N ILE A 59
SHEET 1 C 4 THR A 76 PHE A 81 0
SHEET 2 C 4 TYR A 87 GLU A 92 -1 O SER A 89 N GLY A 80
SHEET 3 C 4 MSE A 106 ASN A 110 -1 O TRP A 109 N LEU A 88
SHEET 4 C 4 LEU A 116 PHE A 120 -1 O PHE A 120 N MSE A 106
SHEET 1 D 4 GLN A 131 TYR A 132 0
SHEET 2 D 4 LEU A 138 VAL A 143 -1 O ALA A 140 N GLN A 131
SHEET 3 D 4 GLU A 146 GLU A 151 -1 O TYR A 150 N ALA A 139
SHEET 4 D 4 ALA A 161 LYS A 162 -1 O ALA A 161 N PHE A 149
SHEET 1 E 4 ASP A 170 LEU A 173 0
SHEET 2 E 4 ALA A 180 ILE A 185 -1 O ALA A 182 N ALA A 172
SHEET 3 E 4 ALA A 193 SER A 199 -1 O ARG A 196 N VAL A 183
SHEET 4 E 4 PRO A 206 PHE A 212 -1 O PHE A 212 N ALA A 193
SHEET 1 F 3 PHE A 220 TRP A 222 0
SHEET 2 F 3 SER A 228 THR A 233 -1 O LEU A 230 N LYS A 221
SHEET 3 F 3 LYS A 242 GLU A 247 -1 O TYR A 244 N VAL A 231
SHEET 1 G 4 ILE A 271 TRP A 276 0
SHEET 2 G 4 PHE A 283 TYR A 287 -1 O VAL A 286 N HIS A 272
SHEET 3 G 4 ALA A 292 PHE A 297 -1 O PHE A 297 N PHE A 283
SHEET 4 G 4 VAL A 303 ALA A 310 -1 O VAL A 304 N ILE A 296
SHEET 1 H 4 THR A 314 PHE A 317 0
SHEET 2 H 4 TYR A 323 ALA A 327 -1 O LEU A 325 N ILE A 316
SHEET 3 H 4 SER A 335 ASP A 340 -1 O PHE A 339 N ILE A 324
SHEET 4 H 4 LYS A 346 GLU A 352 -1 O VAL A 351 N ILE A 336
SHEET 1 I 8 TYR A 358 PHE A 361 0
SHEET 2 I 8 PHE A 367 VAL A 372 -1 O LEU A 369 N GLU A 360
SHEET 3 I 8 SER A 382 HIS A 387 -1 O TRP A 386 N LEU A 368
SHEET 4 I 8 PRO A 392 GLU A 397 -1 O MSE A 393 N ILE A 385
SHEET 5 I 8 PRO B 392 GLU B 397 -1 O GLU B 397 N MSE A 393
SHEET 6 I 8 SER B 382 HIS B 387 -1 N ILE B 385 O MSE B 393
SHEET 7 I 8 PHE B 367 VAL B 372 -1 N THR B 370 O LYS B 384
SHEET 8 I 8 TYR B 358 PHE B 361 -1 N GLU B 360 O LEU B 369
SHEET 1 J 3 ILE B 15 ASN B 19 0
SHEET 2 J 3 GLN B 6 SER B 11 -1 N PHE B 7 O VAL B 18
SHEET 3 J 3 LEU B 401 TRP B 406 -1 O PHE B 405 N ALA B 8
SHEET 1 K 4 ASN B 39 TYR B 42 0
SHEET 2 K 4 LEU B 48 ALA B 52 -1 O ALA B 50 N CYS B 41
SHEET 3 K 4 VAL B 57 ASP B 61 -1 O VAL B 58 N TYR B 51
SHEET 4 K 4 LYS B 67 LEU B 71 -1 O LEU B 71 N VAL B 57
SHEET 1 L 4 THR B 76 PHE B 81 0
SHEET 2 L 4 TYR B 87 GLU B 92 -1 O SER B 89 N GLY B 80
SHEET 3 L 4 MSE B 106 ASN B 110 -1 O TRP B 109 N LEU B 88
SHEET 4 L 4 LEU B 116 PHE B 120 -1 O PHE B 118 N VAL B 108
SHEET 1 M 4 GLN B 131 TYR B 132 0
SHEET 2 M 4 LEU B 138 VAL B 143 -1 O ALA B 140 N GLN B 131
SHEET 3 M 4 GLU B 146 GLU B 151 -1 O TYR B 150 N ALA B 139
SHEET 4 M 4 ALA B 161 LYS B 162 -1 O ALA B 161 N PHE B 149
SHEET 1 N 4 ASP B 170 LEU B 173 0
SHEET 2 N 4 ALA B 180 ILE B 185 -1 O PHE B 184 N ASP B 170
SHEET 3 N 4 SER B 194 SER B 199 -1 O SER B 194 N ILE B 185
SHEET 4 N 4 SER B 208 LYS B 210 -1 O LYS B 210 N VAL B 195
SHEET 1 O 2 LEU B 230 LEU B 232 0
SHEET 2 O 2 ASN B 243 TYR B 245 -1 O TYR B 244 N VAL B 231
SHEET 1 P 4 ILE B 271 TRP B 276 0
SHEET 2 P 4 PHE B 283 TYR B 287 -1 O GLY B 284 N CYS B 275
SHEET 3 P 4 ALA B 292 PHE B 297 -1 O LYS B 293 N TYR B 287
SHEET 4 P 4 VAL B 303 ALA B 310 -1 O SER B 305 N ILE B 296
SHEET 1 Q 4 THR B 314 PHE B 317 0
SHEET 2 Q 4 TYR B 323 ALA B 327 -1 O LEU B 325 N ILE B 316
SHEET 3 Q 4 ILE B 336 ASP B 340 -1 O ASP B 337 N LEU B 326
SHEET 4 Q 4 LYS B 346 VAL B 351 -1 O THR B 349 N ILE B 338
LINK C ASN A 105 N MSE A 106 1555 1555 1.33
LINK C MSE A 106 N LYS A 107 1555 1555 1.33
LINK C ASN A 154 N MSE A 155 1555 1555 1.33
LINK C MSE A 155 N SER A 156 1555 1555 1.33
LINK C TYR A 289 N MSE A 290 1555 1555 1.33
LINK C MSE A 290 N PRO A 291 1555 1555 1.33
LINK C ASN A 344 N MSE A 345 1555 1555 1.32
LINK C MSE A 345 N LYS A 346 1555 1555 1.33
LINK C PRO A 392 N MSE A 393 1555 1555 1.33
LINK C MSE A 393 N PHE A 394 1555 1555 1.33
LINK C ASN B 105 N MSE B 106 1555 1555 1.33
LINK C MSE B 106 N LYS B 107 1555 1555 1.33
LINK C ASN B 154 N MSE B 155 1555 1555 1.32
LINK C MSE B 155 N SER B 156 1555 1555 1.33
LINK C TYR B 289 N MSE B 290 1555 1555 1.33
LINK C MSE B 290 N PRO B 291 1555 1555 1.33
LINK C ASN B 344 N MSE B 345 1555 1555 1.33
LINK C MSE B 345 N LYS B 346 1555 1555 1.33
LINK C PRO B 392 N MSE B 393 1555 1555 1.33
LINK C MSE B 393 N PHE B 394 1555 1555 1.33
CISPEP 1 MSE A 290 PRO A 291 0 4.02
CISPEP 2 SER A 374 PRO A 375 0 1.36
CISPEP 3 GLY B 246 GLU B 247 0 5.98
CISPEP 4 MSE B 290 PRO B 291 0 3.57
CISPEP 5 SER B 374 PRO B 375 0 -1.90
CRYST1 93.443 93.443 269.387 90.00 90.00 120.00 P 31 2 1 12
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 0.010702 0.006179 0.000000 0.00000
SCALE2 0.000000 0.012357 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003712 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
