| content |
HEADER HYDROLASE 04-JAN-21 7BFR
TITLE THERMOGUTTA TERRIFONTIS ESTERASE 2 PHOSPHORYLATED BY PARAOXON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ESTERASE EST2;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOGUTTA TERRIFONTIS;
SOURCE 3 ORGANISM_TAXID: 1331910;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS NERVE AGENT, CONJUGATE, ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.B.BRAZZOLOTTO,J.BZDRENGA,F.NACHON
REVDAT 1 10-FEB-21 7BFR 0
JRNL AUTH J.BZDRENGA,E.TRENET,F.CHANTEGREIL,K.BERNAL,F.NACHON,
JRNL AUTH 2 X.BRAZZOLOTTO
JRNL TITL A THERMOPHILIC BACTERIAL ESTERASE FOR SCAVENGING NERVE
JRNL TITL 2 AGENTS: A KINETIC, BIOPHYSICAL AND STRUCTURAL STUDY.
JRNL REF MOLECULES V. 26 2021
JRNL REFN ESSN 1420-3049
JRNL PMID 33513869
JRNL DOI 10.3390/MOLECULES26030657
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19_4092
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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 19233
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 961
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 36.7400 - 3.8000 1.00 2790 147 0.1449 0.1627
REMARK 3 2 3.8000 - 3.0200 1.00 2679 141 0.1616 0.2170
REMARK 3 3 3.0200 - 2.6400 1.00 2645 140 0.1827 0.2341
REMARK 3 4 2.6400 - 2.4000 1.00 2620 138 0.1708 0.2506
REMARK 3 5 2.4000 - 2.2300 1.00 2621 138 0.1645 0.2073
REMARK 3 6 2.2300 - 2.0900 0.99 2613 136 0.1641 0.2253
REMARK 3 7 2.0900 - 1.9900 0.90 2304 121 0.1701 0.2568
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) : 0.189
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.701
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.33
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 : 0.009 2102
REMARK 3 ANGLE : 1.054 2850
REMARK 3 CHIRALITY : 0.066 299
REMARK 3 PLANARITY : 0.010 379
REMARK 3 DIHEDRAL : 5.849 292
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3834 11.7107 15.9284
REMARK 3 T TENSOR
REMARK 3 T11: 0.1598 T22: 0.1611
REMARK 3 T33: 0.1641 T12: 0.0132
REMARK 3 T13: -0.0043 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.0062 L22: 1.2658
REMARK 3 L33: 0.5009 L12: 0.2937
REMARK 3 L13: 0.1347 L23: -0.1236
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: 0.0709 S13: -0.0324
REMARK 3 S21: 0.1070 S22: -0.0022 S23: -0.1819
REMARK 3 S31: 0.0424 S32: 0.0380 S33: 0.0003
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 7BFR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1292113290.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-20
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 36.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 7BFN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 7.5, 25% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 26.76000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.98500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.98500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.76000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.82000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 0
REMARK 465 ALA A 1
REMARK 465 GLU A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 4
REMARK 465 ARG A 168
REMARK 465 GLU A 169
REMARK 465 GLY A 170
REMARK 465 LEU A 171
REMARK 465 LYS A 172
REMARK 465 ASP A 173
REMARK 465 HIS A 174
REMARK 465 VAL A 175
REMARK 465 PRO A 176
REMARK 465 ARG A 177
REMARK 465 GLN A 178
REMARK 465 ASP A 179
REMARK 465 TRP A 180
REMARK 465 GLU A 181
REMARK 465 GLU A 182
REMARK 465 ARG A 183
REMARK 465 LEU A 184
REMARK 465 GLY A 282
REMARK 465 GLU A 283
REMARK 465 SER A 284
REMARK 465 GLN A 285
REMARK 465 PRO A 286
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 O HOH A 414 O HOH A 565 2.02
REMARK 500 OE1 GLN A 118 O HOH A 401 2.07
REMARK 500 OD2 ASP A 24 O HOH A 402 2.09
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 ASP A 24 54.28 38.55
REMARK 500 ASN A 25 18.71 56.98
REMARK 500 SER A 57 -159.78 -146.86
REMARK 500 MIR A 126 -119.74 55.61
REMARK 500 ASP A 140 -147.16 64.06
REMARK 500 ASN A 161 70.36 17.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 614 DISTANCE = 5.84 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7BFN RELATED DB: PDB
REMARK 900 APO FORM OF SAME PROTEIN
DBREF1 7BFR A 1 286 UNP A0A0X1KHD1_9BACT
DBREF2 7BFR A A0A0X1KHD1 1 286
SEQADV 7BFR GLY A 0 UNP A0A0X1KHD EXPRESSION TAG
SEQRES 1 A 287 GLY ALA GLU VAL GLY ARG LEU ARG TYR PRO PRO GLU MET
SEQRES 2 A 287 PRO GLY ALA GLU VAL LYS VAL TYR LYS LYS VAL ASP ASN
SEQRES 3 A 287 VAL ASP LEU LYS LEU TYR ILE TYR LYS PRO ALA ASP TRP
SEQRES 4 A 287 LYS PRO ALA ASP ARG ARG SER ALA ILE VAL PHE PHE PHE
SEQRES 5 A 287 GLY GLY GLY TRP GLN SER GLY SER PRO ALA GLN PHE ARG
SEQRES 6 A 287 PRO GLN CYS GLU TYR PHE ALA GLY ARG GLY MET VAL ALA
SEQRES 7 A 287 MET ALA ALA ASP TYR ARG VAL GLY SER ARG HIS ASN VAL
SEQRES 8 A 287 LYS VAL ALA ASP CYS VAL ALA ASP ALA LYS SER ALA ILE
SEQRES 9 A 287 ARG TRP VAL ARG GLN HIS ALA ALA GLU LEU GLY VAL ASP
SEQRES 10 A 287 PRO GLN LYS ILE VAL ALA SER GLY GLY MIR ALA GLY GLY
SEQRES 11 A 287 HIS LEU ALA ALA CYS THR VAL MET VAL PRO ASP LEU GLU
SEQRES 12 A 287 ALA PRO GLU GLU ASP HIS THR ILE SER SER GLN ALA ASN
SEQRES 13 A 287 ALA ALA ILE LEU PHE ASN PRO VAL LEU ILE LEU SER ARG
SEQRES 14 A 287 GLU GLY LEU LYS ASP HIS VAL PRO ARG GLN ASP TRP GLU
SEQRES 15 A 287 GLU ARG LEU ARG GLU ARG LEU GLY THR GLU PRO LYS ALA
SEQRES 16 A 287 VAL SER PRO TYR HIS HIS ILE ARG ALA GLY LEU PRO PRO
SEQRES 17 A 287 MET ILE ILE PHE HIS GLY THR ALA ASP ASN THR VAL PRO
SEQRES 18 A 287 PHE GLU THR ILE ARG LEU PHE ALA GLU ALA MET LYS LYS
SEQRES 19 A 287 ALA GLY ASN ARG CYS GLU LEU VAL PRO PHE GLU GLY ALA
SEQRES 20 A 287 ALA HIS GLY PHE PHE ASN PHE GLY ARG GLY ASP ASN LEU
SEQRES 21 A 287 ALA TYR GLN LYS THR LEU GLU LEU ALA ASP GLU PHE LEU
SEQRES 22 A 287 VAL GLU ILE GLY PHE LEU ALA PRO LYS GLY GLU SER GLN
SEQRES 23 A 287 PRO
MODRES 7BFR MIR A 126 SER MODIFIED RESIDUE
HET MIR A 126 12
HET CO3 A 301 4
HETNAM MIR MONOETHYLPHOSPHORYLSERINE
HETNAM CO3 CARBONATE ION
HETSYN MIR O-[(S)-ETHOXY(HYDROXY)PHOSPHORYL]-L-SERINE
FORMUL 1 MIR C5 H12 N O6 P
FORMUL 2 CO3 C O3 2-
FORMUL 3 HOH *214(H2 O)
HELIX 1 AA1 SER A 59 GLN A 62 5 4
HELIX 2 AA2 PHE A 63 ARG A 73 1 11
HELIX 3 AA3 LYS A 91 HIS A 109 1 19
HELIX 4 AA4 HIS A 109 GLY A 114 1 6
HELIX 5 AA5 MIR A 126 VAL A 138 1 13
HELIX 6 AA6 GLU A 191 ILE A 201 5 11
HELIX 7 AA7 PRO A 220 ALA A 234 1 15
HELIX 8 AA8 ASN A 258 ILE A 275 1 18
SHEET 1 AA1 8 GLU A 16 VAL A 23 0
SHEET 2 AA1 8 VAL A 26 TYR A 33 -1 O ILE A 32 N GLU A 16
SHEET 3 AA1 8 VAL A 76 ALA A 80 -1 O ALA A 77 N TYR A 33
SHEET 4 AA1 8 ARG A 44 PHE A 50 1 N PHE A 49 O MET A 78
SHEET 5 AA1 8 VAL A 115 GLY A 125 1 O ASP A 116 N ARG A 44
SHEET 6 AA1 8 ALA A 156 PHE A 160 1 O PHE A 160 N GLY A 124
SHEET 7 AA1 8 MET A 208 GLY A 213 1 O ILE A 209 N LEU A 159
SHEET 8 AA1 8 CYS A 238 PHE A 243 1 O VAL A 241 N ILE A 210
LINK C GLY A 125 N MIR A 126 1555 1555 1.34
LINK C MIR A 126 N ALA A 127 1555 1555 1.34
CISPEP 1 TYR A 8 PRO A 9 0 5.02
CRYST1 53.520 67.640 75.970 90.00 90.00 90.00 P 21 21 21 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 0.018685 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014784 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013163 0.00000
TER 2044 LYS A 281
MASTER 299 0 2 8 8 0 0 6 2235 1 18 23
END |