HEADER TRANSCRIPTION 16-SEP-09 3JV9
TITLE THE STRUCTURE OF A REDUCED FORM OF OXYR FROM N. MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR, LYSR FAMILY;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 88-306;
COMPND 5 SYNONYM: OXYR;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 122586;
SOURCE 4 STRAIN: MC58;
SOURCE 5 GENE: NMB0173;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: OPPF3291
KEYWDS LYSR-TYPE TRANSCRIPTIONAL REGULATOR, LTTR, REDOX, STRUCTURAL
KEYWDS 2 GENOMICS, OPPF, OXFORD PROTEIN PRODUCTION FACILITY, DNA-BINDING,
KEYWDS 3 TRANSCRIPTION, TRANSCRIPTION REGULATION, OPPF3291
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SAINSBURY,J.REN,D.I.STUART,R.J.OWENS,OXFORD PROTEIN PRODUCTION
AUTHOR 2 FACILITY (OPPF)
REVDAT 1 16-JUN-10 3JV9 0
JRNL AUTH S.SAINSBURY,J.REN,J.E.NETTLESHIP,N.J.SAUNDERS,D.I.STUART,
JRNL AUTH 2 R.J.OWENS
JRNL TITL THE STRUCTURE OF A REDUCED FORM OF OXYR FROM NEISSERIA
JRNL TITL 2 MENINGITIDIS
JRNL REF BMC STRUCT.BIOL. V. 10 10 2010
JRNL REFN ESSN 1472-6807
JRNL PMID 20478059
JRNL DOI 10.1186/1472-6807-10-10
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_129)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 32077
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1617
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 29.8001 - 5.1418 1.00 3188 173 0.2124 0.2747
REMARK 3 2 5.1418 - 4.0845 1.00 3201 152 0.1687 0.2273
REMARK 3 3 4.0845 - 3.5692 1.00 3136 209 0.1832 0.2388
REMARK 3 4 3.5692 - 3.2433 1.00 3220 166 0.2029 0.2336
REMARK 3 5 3.2433 - 3.0111 1.00 3193 159 0.2120 0.2844
REMARK 3 6 3.0111 - 2.8337 1.00 3188 173 0.2420 0.2931
REMARK 3 7 2.8337 - 2.6919 1.00 3195 167 0.2687 0.3268
REMARK 3 8 2.6919 - 2.5747 0.99 3132 175 0.3211 0.4334
REMARK 3 9 2.5747 - 2.4757 0.90 2889 128 0.3558 0.4491
REMARK 3 10 2.4757 - 2.3903 0.67 2118 115 0.3763 0.4942
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 : 0.34
REMARK 3 B_SOL : 61.49
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 36.17900
REMARK 3 B22 (A**2) : -19.40200
REMARK 3 B33 (A**2) : -16.77700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 10.30500
REMARK 3 B23 (A**2) : -0.00000
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 : 0.009 3316
REMARK 3 ANGLE : 1.331 4500
REMARK 3 CHIRALITY : 0.082 534
REMARK 3 PLANARITY : 0.006 577
REMARK 3 DIHEDRAL : 17.983 1242
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain 'A' and (resseq 95:182 or resseq
REMARK 3 185:212 or resseq 229:310 ) and (name N or
REMARK 3 name C or name O or name CA) and (not
REMARK 3 element H) and (not element D)
REMARK 3 SELECTION : chain 'B' and (resseq 95:182 or resseq
REMARK 3 185:212 or resseq 229:310 ) and (name N or
REMARK 3 name C or name O or name CA) and (not
REMARK 3 element H) and (not element D)
REMARK 3 ATOM PAIRS NUMBER : 756
REMARK 3 RMSD : 0.285
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ANOMALOUS SCATTERER GROUPS DETAILS.
REMARK 3 NUMBER OF ANOMALOUS SCATTERER GROUPS : 1
REMARK 3 ANOMALOUS SCATTERER GROUP : 1
REMARK 3 SELECTION: NAME SE
REMARK 3 FP : -3.9200
REMARK 3 FDP : 5.8667
REMARK 4
REMARK 4 3JV9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB055202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-06
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 : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785, 0.9070
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16661
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.55400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: 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 (%): 44.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M CALCIUM ACETATE,
REMARK 280 0.2MM TCEP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
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 28.03750
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 GLU A 88
REMARK 465 LEU A 89
REMARK 465 ASP A 306
REMARK 465 GLU B 88
REMARK 465 LEU B 89
REMARK 465 SER B 209
REMARK 465 GLU B 210
REMARK 465 LEU B 211
REMARK 465 ALA B 212
REMARK 465 ALA B 213
REMARK 465 LYS B 214
REMARK 465 GLN B 215
REMARK 465 ARG B 216
REMARK 465 ILE B 217
REMARK 465 GLN B 218
REMARK 465 GLY B 219
REMARK 465 LEU B 220
REMARK 465 ASP B 306
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 ALA A 117 62.32 -151.45
REMARK 500 PRO A 118 3.68 -66.25
REMARK 500 LEU A 160 -56.45 -126.17
REMARK 500 ASP A 179 -109.67 -58.10
REMARK 500 PRO A 183 -61.40 -95.64
REMARK 500 ARG A 184 11.49 -172.71
REMARK 500 MSE A 185 29.52 -73.42
REMARK 500 SER A 209 -30.41 -153.99
REMARK 500 ILE A 217 -87.26 -63.77
REMARK 500 LEU A 220 -0.08 80.92
REMARK 500 THR A 221 -41.46 -153.82
REMARK 500 ALA A 241 -168.47 -171.70
REMARK 500 ALA B 117 53.47 -154.07
REMARK 500 ASN B 127 -178.23 178.57
REMARK 500 PHE B 175 -9.83 -58.91
REMARK 500 ASP B 179 -76.97 -68.99
REMARK 500 PRO B 183 -79.36 -118.43
REMARK 500 ARG B 184 28.61 -147.53
REMARK 500 THR B 195 159.20 -48.88
REMARK 500 THR B 223 108.27 -37.32
REMARK 500 ALA B 241 -165.93 -179.41
REMARK 500 GLN B 297 21.65 80.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 78
DBREF 3JV9 A 88 306 UNP Q9K1H8 Q9K1H8_NEIMB 88 306
DBREF 3JV9 B 88 306 UNP Q9K1H8 Q9K1H8_NEIMB 88 306
SEQRES 1 A 219 GLU LEU GLU GLY ALA PHE LYS LEU GLY LEU ILE PHE THR
SEQRES 2 A 219 VAL ALA PRO TYR LEU LEU PRO LYS LEU ILE VAL SER LEU
SEQRES 3 A 219 ARG ARG THR ALA PRO LYS MSE PRO LEU MSE LEU GLU GLU
SEQRES 4 A 219 ASN TYR THR HIS THR LEU THR GLU SER LEU LYS ARG GLY
SEQRES 5 A 219 ASP VAL ASP ALA ILE ILE VAL ALA GLU PRO PHE GLN GLU
SEQRES 6 A 219 PRO GLY ILE VAL THR GLU PRO LEU TYR ASP GLU PRO PHE
SEQRES 7 A 219 PHE VAL ILE VAL PRO LYS GLY HIS SER PHE GLU GLU LEU
SEQRES 8 A 219 ASP ALA VAL SER PRO ARG MSE LEU GLY GLU GLU GLN VAL
SEQRES 9 A 219 LEU LEU LEU THR GLU GLY ASN CYS MSE ARG ASP GLN VAL
SEQRES 10 A 219 LEU SER SER CYS SER GLU LEU ALA ALA LYS GLN ARG ILE
SEQRES 11 A 219 GLN GLY LEU THR ASN THR LEU GLN GLY SER SER ILE ASN
SEQRES 12 A 219 THR ILE ARG HIS MSE VAL ALA SER GLY LEU ALA ILE SER
SEQRES 13 A 219 VAL LEU PRO ALA THR ALA LEU THR GLU ASN ASP HIS MSE
SEQRES 14 A 219 LEU PHE SER ILE ILE PRO PHE GLU GLY THR PRO PRO SER
SEQRES 15 A 219 ARG ARG VAL VAL LEU ALA TYR ARG ARG ASN PHE VAL ARG
SEQRES 16 A 219 PRO LYS ALA LEU SER ALA MSE LYS ALA ALA ILE MSE GLN
SEQRES 17 A 219 SER GLN LEU HIS GLY VAL SER PHE ILE CYS ASP
SEQRES 1 B 219 GLU LEU GLU GLY ALA PHE LYS LEU GLY LEU ILE PHE THR
SEQRES 2 B 219 VAL ALA PRO TYR LEU LEU PRO LYS LEU ILE VAL SER LEU
SEQRES 3 B 219 ARG ARG THR ALA PRO LYS MSE PRO LEU MSE LEU GLU GLU
SEQRES 4 B 219 ASN TYR THR HIS THR LEU THR GLU SER LEU LYS ARG GLY
SEQRES 5 B 219 ASP VAL ASP ALA ILE ILE VAL ALA GLU PRO PHE GLN GLU
SEQRES 6 B 219 PRO GLY ILE VAL THR GLU PRO LEU TYR ASP GLU PRO PHE
SEQRES 7 B 219 PHE VAL ILE VAL PRO LYS GLY HIS SER PHE GLU GLU LEU
SEQRES 8 B 219 ASP ALA VAL SER PRO ARG MSE LEU GLY GLU GLU GLN VAL
SEQRES 9 B 219 LEU LEU LEU THR GLU GLY ASN CYS MSE ARG ASP GLN VAL
SEQRES 10 B 219 LEU SER SER CYS SER GLU LEU ALA ALA LYS GLN ARG ILE
SEQRES 11 B 219 GLN GLY LEU THR ASN THR LEU GLN GLY SER SER ILE ASN
SEQRES 12 B 219 THR ILE ARG HIS MSE VAL ALA SER GLY LEU ALA ILE SER
SEQRES 13 B 219 VAL LEU PRO ALA THR ALA LEU THR GLU ASN ASP HIS MSE
SEQRES 14 B 219 LEU PHE SER ILE ILE PRO PHE GLU GLY THR PRO PRO SER
SEQRES 15 B 219 ARG ARG VAL VAL LEU ALA TYR ARG ARG ASN PHE VAL ARG
SEQRES 16 B 219 PRO LYS ALA LEU SER ALA MSE LYS ALA ALA ILE MSE GLN
SEQRES 17 B 219 SER GLN LEU HIS GLY VAL SER PHE ILE CYS ASP
MODRES 3JV9 MSE A 120 MET SELENOMETHIONINE
MODRES 3JV9 MSE A 123 MET SELENOMETHIONINE
MODRES 3JV9 MSE A 185 MET SELENOMETHIONINE
MODRES 3JV9 MSE A 200 MET SELENOMETHIONINE
MODRES 3JV9 MSE A 235 MET SELENOMETHIONINE
MODRES 3JV9 MSE A 256 MET SELENOMETHIONINE
MODRES 3JV9 MSE A 289 MET SELENOMETHIONINE
MODRES 3JV9 MSE A 294 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 120 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 123 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 185 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 200 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 235 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 256 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 289 MET SELENOMETHIONINE
MODRES 3JV9 MSE B 294 MET SELENOMETHIONINE
HET MSE A 120 8
HET MSE A 123 8
HET MSE A 185 8
HET MSE A 200 8
HET MSE A 235 8
HET MSE A 256 8
HET MSE A 289 8
HET MSE A 294 8
HET MSE B 120 8
HET MSE B 123 8
HET MSE B 185 8
HET MSE B 200 8
HET MSE B 235 8
HET MSE B 256 8
HET MSE B 289 8
HET MSE B 294 8
HET CL A 307 1
HET CL B 78 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *95(H2 O)
HELIX 1 1 VAL A 101 ALA A 117 1 17
HELIX 2 2 TYR A 128 ARG A 138 1 11
HELIX 3 3 HIS A 173 GLU A 177 5 5
HELIX 4 4 ASN A 198 CYS A 208 1 11
HELIX 5 5 LEU A 211 GLY A 219 1 9
HELIX 6 6 SER A 228 GLY A 239 1 12
HELIX 7 7 THR A 248 LEU A 250 5 3
HELIX 8 8 ARG A 282 GLN A 295 1 14
HELIX 9 9 VAL B 101 ALA B 117 1 17
HELIX 10 10 TYR B 128 ARG B 138 1 11
HELIX 11 11 HIS B 173 LEU B 178 5 6
HELIX 12 12 ARG B 184 GLU B 189 5 6
HELIX 13 13 ASN B 198 SER B 206 1 9
HELIX 14 14 SER B 228 SER B 238 1 11
HELIX 15 15 THR B 248 LEU B 250 5 3
HELIX 16 16 THR B 251 MSE B 256 5 6
HELIX 17 17 ARG B 282 GLN B 295 1 14
SHEET 1 A 6 LEU A 122 ASN A 127 0
SHEET 2 A 6 PHE A 93 ILE A 98 1 N LEU A 95 O MSE A 123
SHEET 3 A 6 ALA A 143 ALA A 147 1 O ILE A 145 N GLY A 96
SHEET 4 A 6 SER A 269 ARG A 277 -1 O VAL A 273 N VAL A 146
SHEET 5 A 6 ILE A 155 PRO A 170 -1 N VAL A 156 O TYR A 276
SHEET 6 A 6 PHE A 258 ILE A 261 -1 O ILE A 261 N VAL A 167
SHEET 1 B 5 GLN A 225 GLY A 226 0
SHEET 2 B 5 VAL A 191 LEU A 194 1 N LEU A 193 O GLY A 226
SHEET 3 B 5 ILE A 242 PRO A 246 1 O ILE A 242 N LEU A 192
SHEET 4 B 5 ILE A 155 PRO A 170 -1 N PHE A 166 O LEU A 245
SHEET 5 B 5 SER A 302 PHE A 303 -1 O SER A 302 N ASP A 162
SHEET 1 C 6 LEU B 122 ASN B 127 0
SHEET 2 C 6 PHE B 93 ILE B 98 1 N LEU B 95 O MSE B 123
SHEET 3 C 6 ALA B 143 ALA B 147 1 O ILE B 145 N GLY B 96
SHEET 4 C 6 SER B 269 ARG B 277 -1 O ALA B 275 N ILE B 144
SHEET 5 C 6 ILE B 155 PRO B 170 -1 N VAL B 156 O TYR B 276
SHEET 6 C 6 PHE B 258 PRO B 262 -1 O ILE B 261 N VAL B 167
SHEET 1 D 5 GLN B 225 GLY B 226 0
SHEET 2 D 5 VAL B 191 LEU B 194 1 N LEU B 193 O GLY B 226
SHEET 3 D 5 ILE B 242 PRO B 246 1 O ILE B 242 N LEU B 192
SHEET 4 D 5 ILE B 155 PRO B 170 -1 N ILE B 168 O SER B 243
SHEET 5 D 5 SER B 302 PHE B 303 -1 O SER B 302 N ASP B 162
LINK C LYS A 119 N MSE A 120 1555 1555 1.32
LINK C MSE A 120 N PRO A 121 1555 1555 1.34
LINK C LEU A 122 N MSE A 123 1555 1555 1.33
LINK C MSE A 123 N LEU A 124 1555 1555 1.33
LINK C ARG A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N LEU A 186 1555 1555 1.33
LINK C CYS A 199 N MSE A 200 1555 1555 1.33
LINK C MSE A 200 N ARG A 201 1555 1555 1.33
LINK C HIS A 234 N MSE A 235 1555 1555 1.33
LINK C MSE A 235 N VAL A 236 1555 1555 1.33
LINK C HIS A 255 N MSE A 256 1555 1555 1.33
LINK C MSE A 256 N LEU A 257 1555 1555 1.33
LINK C ALA A 288 N MSE A 289 1555 1555 1.34
LINK C MSE A 289 N LYS A 290 1555 1555 1.32
LINK C ILE A 293 N MSE A 294 1555 1555 1.33
LINK C MSE A 294 N GLN A 295 1555 1555 1.33
LINK C LYS B 119 N MSE B 120 1555 1555 1.32
LINK C MSE B 120 N PRO B 121 1555 1555 1.34
LINK C LEU B 122 N MSE B 123 1555 1555 1.33
LINK C MSE B 123 N LEU B 124 1555 1555 1.33
LINK C ARG B 184 N MSE B 185 1555 1555 1.33
LINK C MSE B 185 N LEU B 186 1555 1555 1.33
LINK C CYS B 199 N MSE B 200 1555 1555 1.33
LINK C MSE B 200 N ARG B 201 1555 1555 1.33
LINK C HIS B 234 N MSE B 235 1555 1555 1.32
LINK C MSE B 235 N VAL B 236 1555 1555 1.33
LINK C HIS B 255 N MSE B 256 1555 1555 1.33
LINK C MSE B 256 N LEU B 257 1555 1555 1.33
LINK C ALA B 288 N MSE B 289 1555 1555 1.33
LINK C MSE B 289 N LYS B 290 1555 1555 1.33
LINK C ILE B 293 N MSE B 294 1555 1555 1.32
LINK C MSE B 294 N GLN B 295 1555 1555 1.33
CISPEP 1 GLU A 148 PRO A 149 0 2.89
CISPEP 2 GLU B 148 PRO B 149 0 -4.77
SITE 1 AC1 3 THR A 129 HIS A 130 GLY A 197
SITE 1 AC2 2 SER B 228 ILE B 229
CRYST1 49.813 56.075 81.247 90.00 104.91 90.00 P 1 21 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 0.020075 0.000000 0.005345 0.00000
SCALE2 0.000000 0.017833 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012737 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
