HEADER METAL TRANSPORT 19-APR-16 5JG7
TITLE CRYSTAL STRUCTURE OF PUTATIVE PERIPLASMIC BINDING PROTEIN FROM
TITLE 2 SALMONELLA TYPHIMURIUM LT2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUR REGULATED SALMONELLA IRON TRANSPORTER;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 28-187;
COMPND 5 SYNONYM: PERIPLASMIC BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 /
SOURCE 3 ATCC 700720);
SOURCE 4 ORGANISM_TAXID: 99287;
SOURCE 5 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 6 GENE: SITA, STM2861;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS STRUCTURAL GENOMICS, CSGID, PERIPLASMIC BINDING PROTEIN, CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHANG,M.ZHOU,S.SHATSMAN,A.JOACHIMIAK,W.F.ANDERSON,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 20-JUL-16 5JG7 1 REMARK
REVDAT 1 27-APR-16 5JG7 0
JRNL AUTH C.CHANG,M.ZHOU,S.SHATSMAN,A.JOACHIMIAK,W.F.ANDERSON
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE PERIPLASMIC BINDING PROTEIN
JRNL TITL 2 FROM SALMONELLA TYPHIMURIUM LT2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_2328
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 35880
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1828
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 30.9895 - 3.9935 0.98 2895 193 0.1809 0.2209
REMARK 3 2 3.9935 - 3.1708 1.00 2856 145 0.1712 0.1881
REMARK 3 3 3.1708 - 2.7703 0.99 2772 170 0.1786 0.2077
REMARK 3 4 2.7703 - 2.5171 0.99 2788 150 0.1762 0.2064
REMARK 3 5 2.5171 - 2.3368 1.00 2755 152 0.1585 0.2173
REMARK 3 6 2.3368 - 2.1990 0.99 2756 149 0.1536 0.2214
REMARK 3 7 2.1990 - 2.0889 0.98 2723 127 0.1567 0.2160
REMARK 3 8 2.0889 - 1.9980 0.99 2739 142 0.1624 0.2093
REMARK 3 9 1.9980 - 1.9211 0.98 2733 131 0.1733 0.2100
REMARK 3 10 1.9211 - 1.8548 0.96 2647 138 0.1717 0.2308
REMARK 3 11 1.8548 - 1.7968 0.89 2443 125 0.1774 0.2229
REMARK 3 12 1.7968 - 1.7455 0.76 2102 111 0.1863 0.2448
REMARK 3 13 1.7455 - 1.6995 0.67 1843 95 0.2083 0.2565
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.01
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 : 0.006 2409
REMARK 3 ANGLE : 0.734 3268
REMARK 3 CHIRALITY : 0.050 359
REMARK 3 PLANARITY : 0.004 428
REMARK 3 DIHEDRAL : 15.713 1472
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 5JG7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220528.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37084
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 96.8
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M PROLINE, 0.1 M HEPES, 10% W/V
REMARK 280 PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 22.02850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.52450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.29100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.52450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.02850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.29100
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 ALA A 61
REMARK 465 THR A 118
REMARK 465 GLU A 119
REMARK 465 GLY A 120
REMARK 465 PRO A 121
REMARK 465 TYR A 122
REMARK 465 ASN A 123
REMARK 465 GLY A 124
REMARK 465 LYS A 125
REMARK 465 PRO A 126
REMARK 465 ASN A 127
REMARK 465 PRO A 128
REMARK 465 GLU B 62
REMARK 465 ILE B 63
REMARK 465 HIS B 64
REMARK 465 GLU B 65
REMARK 465 GLY B 116
REMARK 465 ILE B 117
REMARK 465 THR B 118
REMARK 465 GLU B 119
REMARK 465 GLY B 120
REMARK 465 PRO B 121
REMARK 465 TYR B 122
REMARK 465 ASN B 123
REMARK 465 GLY B 124
REMARK 465 LYS B 125
REMARK 465 PRO B 126
REMARK 465 ASN B 127
REMARK 465 PRO B 128
REMARK 465 HIS B 129
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 62 CG CD OE1 OE2
REMARK 470 ILE A 63 CG1 CG2 CD1
REMARK 470 HIS A 64 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 65 CG CD OE1 OE2
REMARK 470 ARG A 91 CG CD NE CZ NH1 NH2
REMARK 470 MSE A 115 CG SE CE
REMARK 470 HIS A 129 CG ND1 CD2 CE1 NE2
REMARK 470 TYR B 66 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 ARG B 91 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 OD1 ASP A 187 O HOH A 301 2.11
REMARK 500 NH2 ARG A 171 O HOH A 302 2.16
REMARK 500 O HOH A 343 O HOH B 381 2.17
REMARK 500 O HOH A 321 O HOH A 430 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 305 O HOH B 359 1455 2.16
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 GOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP01840 RELATED DB: TARGETTRACK
DBREF 5JG7 A 28 187 UNP Q7CPX8 Q7CPX8_SALTY 28 187
DBREF 5JG7 B 28 187 UNP Q7CPX8 Q7CPX8_SALTY 28 187
SEQRES 1 A 160 GLU LYS PHE LYS VAL ILE THR THR PHE THR VAL ILE ALA
SEQRES 2 A 160 ASP MSE ALA LYS ASN VAL ALA GLY ASP ALA ALA GLU VAL
SEQRES 3 A 160 SER SER ILE THR LYS PRO GLY ALA GLU ILE HIS GLU TYR
SEQRES 4 A 160 GLN PRO THR PRO GLY ASP ILE LYS ARG ALA GLN GLY ALA
SEQRES 5 A 160 GLN LEU ILE LEU ALA ASN GLY LEU ASN LEU GLU ARG TRP
SEQRES 6 A 160 PHE ALA ARG PHE TYR GLN HIS LEU SER GLY VAL PRO GLU
SEQRES 7 A 160 VAL VAL VAL SER THR GLY VAL LYS PRO MSE GLY ILE THR
SEQRES 8 A 160 GLU GLY PRO TYR ASN GLY LYS PRO ASN PRO HIS ALA TRP
SEQRES 9 A 160 MSE SER ALA GLU ASN ALA LEU ILE TYR VAL ASP ASN ILE
SEQRES 10 A 160 ARG ASP ALA LEU VAL LYS TYR ASP PRO ASP ASN ALA GLN
SEQRES 11 A 160 ILE TYR LYS GLN ASN ALA GLU ARG TYR LYS ALA LYS ILE
SEQRES 12 A 160 ARG GLN MSE ALA ASP PRO LEU ARG ALA GLU LEU GLU LYS
SEQRES 13 A 160 ILE PRO ALA ASP
SEQRES 1 B 160 GLU LYS PHE LYS VAL ILE THR THR PHE THR VAL ILE ALA
SEQRES 2 B 160 ASP MSE ALA LYS ASN VAL ALA GLY ASP ALA ALA GLU VAL
SEQRES 3 B 160 SER SER ILE THR LYS PRO GLY ALA GLU ILE HIS GLU TYR
SEQRES 4 B 160 GLN PRO THR PRO GLY ASP ILE LYS ARG ALA GLN GLY ALA
SEQRES 5 B 160 GLN LEU ILE LEU ALA ASN GLY LEU ASN LEU GLU ARG TRP
SEQRES 6 B 160 PHE ALA ARG PHE TYR GLN HIS LEU SER GLY VAL PRO GLU
SEQRES 7 B 160 VAL VAL VAL SER THR GLY VAL LYS PRO MSE GLY ILE THR
SEQRES 8 B 160 GLU GLY PRO TYR ASN GLY LYS PRO ASN PRO HIS ALA TRP
SEQRES 9 B 160 MSE SER ALA GLU ASN ALA LEU ILE TYR VAL ASP ASN ILE
SEQRES 10 B 160 ARG ASP ALA LEU VAL LYS TYR ASP PRO ASP ASN ALA GLN
SEQRES 11 B 160 ILE TYR LYS GLN ASN ALA GLU ARG TYR LYS ALA LYS ILE
SEQRES 12 B 160 ARG GLN MSE ALA ASP PRO LEU ARG ALA GLU LEU GLU LYS
SEQRES 13 B 160 ILE PRO ALA ASP
MODRES 5JG7 MSE A 42 MET MODIFIED RESIDUE
MODRES 5JG7 MSE A 115 MET MODIFIED RESIDUE
MODRES 5JG7 MSE A 132 MET MODIFIED RESIDUE
MODRES 5JG7 MSE A 173 MET MODIFIED RESIDUE
MODRES 5JG7 MSE B 42 MET MODIFIED RESIDUE
MODRES 5JG7 MSE B 115 MET MODIFIED RESIDUE
MODRES 5JG7 MSE B 132 MET MODIFIED RESIDUE
MODRES 5JG7 MSE B 173 MET MODIFIED RESIDUE
HET MSE A 42 8
HET MSE A 115 5
HET MSE A 132 8
HET MSE A 173 16
HET MSE B 42 8
HET MSE B 115 8
HET MSE B 132 8
HET MSE B 173 16
HET GOL A 201 12
HET GOL A 202 6
HET GOL B 201 12
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 HOH *234(H2 O)
HELIX 1 AA1 PHE A 36 GLY A 48 1 13
HELIX 2 AA2 THR A 69 GLN A 77 1 9
HELIX 3 AA3 GLY A 86 LEU A 89 5 4
HELIX 4 AA4 GLU A 90 TYR A 97 1 8
HELIX 5 AA5 GLN A 98 SER A 101 5 4
HELIX 6 AA6 ALA A 130 ASP A 152 1 23
HELIX 7 AA7 ASN A 155 ASP A 175 1 21
HELIX 8 AA8 ASP A 175 LYS A 183 1 9
HELIX 9 AA9 PHE B 36 GLY B 48 1 13
HELIX 10 AB1 THR B 69 GLN B 77 1 9
HELIX 11 AB2 GLY B 86 LEU B 89 5 4
HELIX 12 AB3 GLU B 90 TYR B 97 1 8
HELIX 13 AB4 GLN B 98 SER B 101 5 4
HELIX 14 AB5 SER B 133 ASP B 152 1 20
HELIX 15 AB6 ASN B 155 ASP B 175 1 21
HELIX 16 AB7 ASP B 175 LYS B 183 1 9
SHEET 1 AA1 4 ALA A 51 SER A 55 0
SHEET 2 AA1 4 PHE A 30 THR A 34 1 N PHE A 30 O GLU A 52
SHEET 3 AA1 4 LEU A 81 ALA A 84 1 O LEU A 81 N ILE A 33
SHEET 4 AA1 4 GLU B 105 VAL B 107 1 O VAL B 106 N ALA A 84
SHEET 1 AA2 4 GLU A 105 VAL A 107 0
SHEET 2 AA2 4 LEU B 81 ALA B 84 1 O ILE B 82 N VAL A 106
SHEET 3 AA2 4 PHE B 30 THR B 34 1 N ILE B 33 O LEU B 81
SHEET 4 AA2 4 ALA B 51 SER B 55 1 O GLU B 52 N PHE B 30
LINK C ASP A 41 N MSE A 42 1555 1555 1.33
LINK C MSE A 42 N ALA A 43 1555 1555 1.34
LINK C PRO A 114 N MSE A 115 1555 1555 1.33
LINK C MSE A 115 N GLY A 116 1555 1555 1.33
LINK C ATRP A 131 N MSE A 132 1555 1555 1.33
LINK C BTRP A 131 N MSE A 132 1555 1555 1.33
LINK C MSE A 132 N SER A 133 1555 1555 1.34
LINK C AGLN A 172 N AMSE A 173 1555 1555 1.33
LINK C BGLN A 172 N BMSE A 173 1555 1555 1.33
LINK C AMSE A 173 N ALA A 174 1555 1555 1.33
LINK C BMSE A 173 N ALA A 174 1555 1555 1.33
LINK C ASP B 41 N MSE B 42 1555 1555 1.33
LINK C MSE B 42 N ALA B 43 1555 1555 1.34
LINK C PRO B 114 N MSE B 115 1555 1555 1.33
LINK C TRP B 131 N MSE B 132 1555 1555 1.33
LINK C MSE B 132 N SER B 133 1555 1555 1.33
LINK C GLN B 172 N AMSE B 173 1555 1555 1.33
LINK C GLN B 172 N BMSE B 173 1555 1555 1.33
LINK C AMSE B 173 N ALA B 174 1555 1555 1.33
LINK C BMSE B 173 N ALA B 174 1555 1555 1.33
SITE 1 AC1 12 ASN A 85 GLY A 86 LEU A 87 GLU A 105
SITE 2 AC1 12 HOH A 303 HOH A 306 HOH A 307 HOH A 352
SITE 3 AC1 12 ASN B 85 GLY B 86 LEU B 87 GLU B 105
SITE 1 AC2 7 THR A 110 TYR A 151 HOH A 311 HOH A 324
SITE 2 AC2 7 HOH A 436 PRO B 104 GLU B 105
SITE 1 AC3 9 PRO A 104 GLU A 105 VAL B 106 VAL B 107
SITE 2 AC3 9 THR B 110 TYR B 151 HOH B 303 HOH B 306
SITE 3 AC3 9 HOH B 315
CRYST1 44.057 84.582 91.049 90.00 90.00 90.00 P 21 21 21 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 0.022698 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011823 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010983 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
