| content |
HEADER OXIDOREDUCTASE 12-JAN-21 7LD8
TITLE CRYSTAL STRUCTURE OF PUTATIVE NON-HEME BROMOPEROXIDASE BPOC FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS H37RV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE NON-HEME BROMOPEROXIDASE BPOC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MYTUD.00095.B.B1;
COMPND 5 EC: 1.11.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: BPOC, RV0554;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MYTUD.00095.B.B1
KEYWDS SSGCID, PUTATIVE NON-HEME BROMOPEROXIDASE, BPOC, STRUCTURAL GENOMICS,
KEYWDS 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,SEATTLE
AUTHOR 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 20-JAN-21 7LD8 0
JRNL AUTH N.D.DEBOUVER,D.M.DRANOW,D.D.LORIMER,P.S.HORANYI,T.E.EDWARDS
JRNL TITL CRYSTAL STRUCTURE OF ACETYL-COENZYME A SYNTHETASE SYNTHETASE
JRNL TITL 2 FROM COCCIDIOIDES IMMITIS IN COMPLEX WITH PRX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19RC4-4035
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 38201
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.410
REMARK 3 FREE R VALUE TEST SET COUNT : 2068
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 43.3700 - 3.7000 0.99 2658 148 0.1347 0.1502
REMARK 3 2 3.7000 - 2.9400 0.99 2531 144 0.1349 0.1698
REMARK 3 3 2.9400 - 2.5700 0.99 2484 123 0.1467 0.1909
REMARK 3 4 2.5600 - 2.3300 0.99 2467 140 0.1429 0.1927
REMARK 3 5 2.3300 - 2.1600 0.99 2440 126 0.1303 0.1780
REMARK 3 6 2.1600 - 2.0400 0.98 2413 166 0.1315 0.1772
REMARK 3 7 2.0400 - 1.9300 0.98 2408 144 0.1305 0.2091
REMARK 3 8 1.9300 - 1.8500 0.98 2409 144 0.1230 0.1836
REMARK 3 9 1.8500 - 1.7800 0.98 2404 133 0.1302 0.1752
REMARK 3 10 1.7800 - 1.7200 0.97 2355 132 0.1281 0.1705
REMARK 3 11 1.7200 - 1.6600 0.97 2361 150 0.1234 0.2057
REMARK 3 12 1.6600 - 1.6200 0.97 2380 129 0.1229 0.1984
REMARK 3 13 1.6200 - 1.5700 0.97 2365 130 0.1178 0.1700
REMARK 3 14 1.5700 - 1.5300 0.97 2358 145 0.1280 0.1949
REMARK 3 15 1.5300 - 1.5000 0.87 2100 114 0.1392 0.2324
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) : 0.115
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.126
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.03
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 2172
REMARK 3 ANGLE : 0.760 2976
REMARK 3 CHIRALITY : 0.054 332
REMARK 3 PLANARITY : 0.008 397
REMARK 3 DIHEDRAL : 11.107 797
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 7LD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1000254102.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38202
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 97.3
REMARK 200 DATA REDUNDANCY : 7.164
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.18
REMARK 200 R MERGE FOR SHELL (I) : 0.32300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: 3HSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MYTUD.00095.B.B1.PW38899[BARCODE:
REMARK 280 318836D7, PUCKID: NEU1-3, CRYO: 20% EG, CONCENTRATION: 18 MG/ML]
REMARK 280 100 MM SODIUM CITRATE/CITRIC ACID PH 5.5, 20% (W/V) PEG 3000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 24.27500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.27500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.75000
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: 4000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 0.00000
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 MET A -6
REMARK 465 ALA A -5
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 HIS A -4 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 137 CG CD OE1 NE2
REMARK 470 MET A 172 CG SD CE
REMARK 470 GLN A 190 CG CD OE1 NE2
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 143 O HOH A 401 2.18
REMARK 500 ND2 ASN A 229 O HOH A 402 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 A 406 O HOH A 406 2555 2.02
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 SER A 88 -117.97 57.03
REMARK 500 SER A 88 -119.83 55.58
REMARK 500 PRO A 189 109.90 -59.92
REMARK 500 LEU A 241 39.87 -94.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 224 O
REMARK 620 2 LEU A 227 O 84.0
REMARK 620 3 GLY A 230 O 94.8 104.3
REMARK 620 4 HOH A 480 O 101.7 88.2 160.2
REMARK 620 5 HOH A 591 O 171.1 92.3 78.3 86.2
REMARK 620 6 HOH A 653 O 86.0 168.6 81.9 88.5 98.4
REMARK 620 N 1 2 3 4 5
DBREF 7LD8 A 3 263 UNP P9WNH1 BPOC_MYCTU 2 262
SEQADV 7LD8 MET A -6 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 ALA A -5 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 HIS A -4 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 HIS A -3 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 HIS A -2 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 HIS A -1 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 HIS A 0 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 MET A 1 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 VAL A 2 UNP P9WNH1 EXPRESSION TAG
SEQADV 7LD8 TYR A 192 UNP P9WNH1 ASN 191 CONFLICT
SEQRES 1 A 270 MET ALA HIS HIS HIS HIS HIS MET VAL ILE ASN LEU ALA
SEQRES 2 A 270 TYR ASP ASP ASN GLY THR GLY ASP PRO VAL VAL PHE ILE
SEQRES 3 A 270 ALA GLY ARG GLY GLY ALA GLY ARG THR TRP HIS PRO HIS
SEQRES 4 A 270 GLN VAL PRO ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE
SEQRES 5 A 270 THR PHE ASP ASN ARG GLY ILE GLY ALA THR GLU ASN ALA
SEQRES 6 A 270 GLU GLY PHE THR THR GLN THR MET VAL ALA ASP THR ALA
SEQRES 7 A 270 ALA LEU ILE GLU THR LEU ASP ILE ALA PRO ALA ARG VAL
SEQRES 8 A 270 VAL GLY VAL SER MET GLY ALA PHE ILE ALA GLN GLU LEU
SEQRES 9 A 270 MET VAL VAL ALA PRO GLU LEU VAL SER SER ALA VAL LEU
SEQRES 10 A 270 MET ALA THR ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE
SEQRES 11 A 270 PHE ASN LYS ALA GLU ALA GLU LEU TYR ASP SER GLY VAL
SEQRES 12 A 270 GLN LEU PRO PRO THR TYR ASP ALA ARG ALA ARG LEU LEU
SEQRES 13 A 270 GLU ASN PHE SER ARG LYS THR LEU ASN ASP ASP VAL ALA
SEQRES 14 A 270 VAL GLY ASP TRP ILE ALA MET PHE SER MET TRP PRO ILE
SEQRES 15 A 270 LYS SER THR PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA
SEQRES 16 A 270 PRO GLN THR TYR ARG LEU PRO ALA TYR ARG ASN ILE ALA
SEQRES 17 A 270 ALA PRO VAL LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL
SEQRES 18 A 270 THR PRO PRO TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU
SEQRES 19 A 270 PRO ASN GLY ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS
SEQRES 20 A 270 LEU GLY PHE PHE GLU ARG PRO GLU ALA VAL ASN THR ALA
SEQRES 21 A 270 MET LEU LYS PHE PHE ALA SER VAL LYS ALA
HET EDO A 301 4
HET NA A 302 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO C2 H6 O2
FORMUL 3 NA NA 1+
FORMUL 4 HOH *350(H2 O)
HELIX 1 AA1 ALA A 25 HIS A 30 5 6
HELIX 2 AA2 GLN A 33 ALA A 40 1 8
HELIX 3 AA3 ILE A 52 GLU A 56 5 5
HELIX 4 AA4 THR A 62 LEU A 77 1 16
HELIX 5 AA5 SER A 88 ALA A 101 1 14
HELIX 6 AA6 ASP A 118 GLY A 135 1 18
HELIX 7 AA7 PRO A 139 PHE A 152 1 14
HELIX 8 AA8 SER A 153 ASN A 158 1 6
HELIX 9 AA9 ASP A 159 TRP A 173 1 15
HELIX 10 AB1 THR A 178 ASP A 186 1 9
HELIX 11 AB2 ARG A 193 ARG A 198 1 6
HELIX 12 AB3 PRO A 216 LEU A 227 1 12
HELIX 13 AB4 LEU A 241 ARG A 246 1 6
HELIX 14 AB5 ARG A 246 VAL A 261 1 16
SHEET 1 AA1 7 TYR A 7 ASN A 10 0
SHEET 2 AA1 7 ARG A 43 PHE A 47 -1 O CYS A 44 N ASN A 10
SHEET 3 AA1 7 PRO A 15 ILE A 19 1 N VAL A 16 O ILE A 45
SHEET 4 AA1 7 ALA A 82 VAL A 87 1 O ARG A 83 N VAL A 17
SHEET 5 AA1 7 VAL A 105 MET A 111 1 O MET A 111 N GLY A 86
SHEET 6 AA1 7 VAL A 204 PHE A 209 1 O LEU A 205 N LEU A 110
SHEET 7 AA1 7 GLY A 230 ILE A 235 1 O ARG A 231 N VAL A 206
LINK O ALA A 224 NA NA A 302 1555 1555 2.29
LINK O LEU A 227 NA NA A 302 1555 1555 2.44
LINK O GLY A 230 NA NA A 302 1555 1555 2.44
LINK NA NA A 302 O HOH A 480 1555 1555 2.49
LINK NA NA A 302 O HOH A 591 1555 1555 2.44
LINK NA NA A 302 O HOH A 653 1555 1555 2.50
CISPEP 1 ALA A 80 PRO A 81 0 -4.04
CRYST1 48.550 113.500 43.370 90.00 90.00 90.00 P 21 21 2 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 0.020597 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008811 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023057 0.00000
TER 2108 ALA A 263
MASTER 296 0 2 14 7 0 0 6 2397 1 12 21
END |