| content |
HEADER HYDROLASE/HYDROLASE INHIBITOR 07-JUL-16 5KRE
TITLE COVALENT INHIBITOR OF LYPLAL1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOPHOSPHOLIPASE-LIKE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.2.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LYPLAL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LYPLAL1, SERINE HYDROLASE, COVALENT INHIBITOR, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PANDIT
REVDAT 1 20-JUL-16 5KRE 0
JRNL AUTH K.AHN,M.F.BROWN,M.BOEHM,J.CALLOWAY,Y.CHE,J.M.CHEN,K.FENNELL,
JRNL AUTH 2 K.F.GEOGHEGAN,A.M.GILBERT,J.A.GUTIERREZ,A.S.KALGUTKAR,
JRNL AUTH 3 A.LANBA,C.LIMBERAKIS,T.V.MAGEE,I.O'DOHERTY,R.OLIVER,B.PABST,
JRNL AUTH 4 J.PANDIT,K.PARRIS,J.A.PFEFFERKORN,T.P.ROLPH,R.PATEL,
JRNL AUTH 5 B.SCHUFF,V.SHANMUGASUNDARAM,J.T.STARR,A.H.VARGHESE,N.B.VERA,
JRNL AUTH 6 C.VERNOCHET,J.YAN
JRNL TITL DISCOVERY OF A SELECTIVE COVALENT INHIBITOR OF
JRNL TITL 2 LYSOPHOSPHOLIPASE-LIKE 1 (LYPLAL1) AS A TOOL TO EVALUATE THE
JRNL TITL 3 ROLE OF THIS SERINE HYDROLASE IN METABOLISM.
JRNL REF ACS CHEM.BIOL. 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 27391855
JRNL DOI 10.1021/ACSCHEMBIO.6B00266
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 15450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.670
REMARK 3 FREE R VALUE TEST SET COUNT : 1030
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.29
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2657
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1708
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2467
REMARK 3 BIN R VALUE (WORKING SET) : 0.1683
REMARK 3 BIN FREE R VALUE : 0.2035
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.15
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 190
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.07440
REMARK 3 B22 (A**2) : 8.04500
REMARK 3 B33 (A**2) : -5.97060
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.191
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.180
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.155
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.167
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.151
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1848 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2514 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 636 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 39 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 278 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1848 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 236 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2293 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.04
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.10
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.18
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5KRE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222647.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15495
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30200
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: 3U0V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 22% PEG 3350 AND 100MM
REMARK 280 AMMONIUM NITRATE, PROTEIN BUFFER: 20MM TRIS PH 8.0, 30MM NACL,
REMARK 280 1MM TCEP, 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 23.70500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.99000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.99000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.70500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.72000
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 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 -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 GLY A 6
REMARK 465 SER A 7
REMARK 465 GLU A 232
REMARK 465 MET A 233
REMARK 465 GLU A 234
REMARK 465 LYS A 235
REMARK 465 GLN A 236
REMARK 465 LYS A 237
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 124 -117.06 53.61
REMARK 500 TYR A 210 -141.73 -103.33
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 553 DISTANCE = 5.85 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6WG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 302
DBREF 5KRE A 1 237 UNP Q5VWZ2 LYPL1_HUMAN 1 237
SEQADV 5KRE GLY A -1 UNP Q5VWZ2 EXPRESSION TAG
SEQADV 5KRE PRO A 0 UNP Q5VWZ2 EXPRESSION TAG
SEQADV 5KRE MET A 131 UNP Q5VWZ2 ILE 131 VARIANT
SEQRES 1 A 239 GLY PRO MET ALA ALA ALA SER GLY SER VAL LEU GLN ARG
SEQRES 2 A 239 CYS ILE VAL SER PRO ALA GLY ARG HIS SER ALA SER LEU
SEQRES 3 A 239 ILE PHE LEU HIS GLY SER GLY ASP SER GLY GLN GLY LEU
SEQRES 4 A 239 ARG MET TRP ILE LYS GLN VAL LEU ASN GLN ASP LEU THR
SEQRES 5 A 239 PHE GLN HIS ILE LYS ILE ILE TYR PRO THR ALA PRO PRO
SEQRES 6 A 239 ARG SER TYR THR PRO MET LYS GLY GLY ILE SER ASN VAL
SEQRES 7 A 239 TRP PHE ASP ARG PHE LYS ILE THR ASN ASP CYS PRO GLU
SEQRES 8 A 239 HIS LEU GLU SER ILE ASP VAL MET CYS GLN VAL LEU THR
SEQRES 9 A 239 ASP LEU ILE ASP GLU GLU VAL LYS SER GLY ILE LYS LYS
SEQRES 10 A 239 ASN ARG ILE LEU ILE GLY GLY PHE SER MET GLY GLY CYS
SEQRES 11 A 239 MET ALA MET HIS LEU ALA TYR ARG ASN HIS GLN ASP VAL
SEQRES 12 A 239 ALA GLY VAL PHE ALA LEU SER SER PHE LEU ASN LYS ALA
SEQRES 13 A 239 SER ALA VAL TYR GLN ALA LEU GLN LYS SER ASN GLY VAL
SEQRES 14 A 239 LEU PRO GLU LEU PHE GLN CYS HIS GLY THR ALA ASP GLU
SEQRES 15 A 239 LEU VAL LEU HIS SER TRP ALA GLU GLU THR ASN SER MET
SEQRES 16 A 239 LEU LYS SER LEU GLY VAL THR THR LYS PHE HIS SER PHE
SEQRES 17 A 239 PRO ASN VAL TYR HIS GLU LEU SER LYS THR GLU LEU ASP
SEQRES 18 A 239 ILE LEU LYS LEU TRP ILE LEU THR LYS LEU PRO GLY GLU
SEQRES 19 A 239 MET GLU LYS GLN LYS
HET 6WG A 301 28
HET NO3 A 302 4
HETNAM 6WG (2~{R})-2-PHENYLPIPERIDINE-1-CARBALDEHYDE
HETNAM NO3 NITRATE ION
FORMUL 2 6WG C12 H15 N O
FORMUL 3 NO3 N O3 1-
FORMUL 4 HOH *153(H2 O)
HELIX 1 AA1 SER A 33 ASN A 46 1 14
HELIX 2 AA2 THR A 67 LYS A 70 5 4
HELIX 3 AA3 HIS A 90 SER A 111 1 22
HELIX 4 AA4 LYS A 114 ASN A 116 5 3
HELIX 5 AA5 SER A 124 ASN A 137 1 14
HELIX 6 AA6 SER A 155 LYS A 163 1 9
HELIX 7 AA7 LEU A 183 LEU A 197 1 15
HELIX 8 AA8 SER A 214 LEU A 229 1 16
SHEET 1 AA1 7 ARG A 11 VAL A 14 0
SHEET 2 AA1 7 ILE A 54 PRO A 59 -1 O ILE A 56 N VAL A 14
SHEET 3 AA1 7 ALA A 22 LEU A 27 1 N LEU A 24 O ILE A 57
SHEET 4 AA1 7 ILE A 118 PHE A 123 1 O GLY A 121 N LEU A 27
SHEET 5 AA1 7 GLY A 143 LEU A 147 1 O LEU A 147 N GLY A 122
SHEET 6 AA1 7 LEU A 171 GLY A 176 1 O PHE A 172 N VAL A 144
SHEET 7 AA1 7 THR A 201 PHE A 206 1 O PHE A 206 N HIS A 175
SHEET 1 AA2 2 PRO A 63 SER A 65 0
SHEET 2 AA2 2 ILE A 73 ASN A 75 -1 O SER A 74 N ARG A 64
LINK OG SER A 124 C12 6WG A 301 1555 1555 1.42
SITE 1 AC1 10 SER A 30 TYR A 66 ARG A 80 ILE A 83
SITE 2 AC1 10 SER A 124 MET A 125 LEU A 181 VAL A 182
SITE 3 AC1 10 NO3 A 302 HOH A 427
SITE 1 AC2 9 ARG A 80 SER A 124 MET A 125 CYS A 128
SITE 2 AC2 9 SER A 148 SER A 149 PHE A 150 VAL A 182
SITE 3 AC2 9 6WG A 301
CRYST1 47.410 61.440 75.980 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 0.021093 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016276 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013161 0.00000
TER 1772 GLY A 231
MASTER 277 0 2 8 9 0 6 6 1926 1 33 19
END |