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HEADER LUMINESCENT PROTEIN 21-MAY-21 7OME
TITLE AZACOELENTERAZINE-BOUND RENILLA-TYPE ENGINEERED ANCESTRAL LUCIFERASE
TITLE 2 VARIANT (ANCFT7)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENILLA-TYPE ENGINEERED ANCESTRAL LUCIFERASE VARIANT
COMPND 3 (ANCFT7);
COMPND 4 CHAIN: A;
COMPND 5 EC: 1.13.12.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOLUMINSCENCE, AZACOELENTERAZINE-BOUND ENZYME, LUMINESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHENKMAYEROVA,Y.L.JANIN,M.MAREK
REVDAT 1 01-JUN-22 7OME 0
JRNL AUTH A.SCHENKMAYEROVA,Y.JANIN,J.DAMBORSKY,M.MAREK
JRNL TITL STRUCTURAL AND CHEMICAL BASIS OF THE RENILLA-TYPE
JRNL TITL 2 BIOLUMINESCENCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 44198
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 2130
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 39.4410 - 3.7008 1.00 3008 169 0.1582 0.1796
REMARK 3 2 3.7008 - 2.9378 1.00 2887 151 0.1581 0.1828
REMARK 3 3 2.9378 - 2.5665 1.00 2850 137 0.1751 0.2020
REMARK 3 4 2.5665 - 2.3319 1.00 2835 150 0.1646 0.1785
REMARK 3 5 2.3319 - 2.1647 1.00 2821 142 0.1469 0.1992
REMARK 3 6 2.1647 - 2.0371 1.00 2812 141 0.1569 0.1771
REMARK 3 7 2.0371 - 1.9351 1.00 2808 151 0.1608 0.1688
REMARK 3 8 1.9351 - 1.8509 1.00 2782 150 0.1632 0.1792
REMARK 3 9 1.8509 - 1.7796 1.00 2789 137 0.1722 0.1959
REMARK 3 10 1.7796 - 1.7182 1.00 2783 150 0.1703 0.1976
REMARK 3 11 1.7182 - 1.6645 1.00 2800 137 0.1768 0.1871
REMARK 3 12 1.6645 - 1.6169 1.00 2806 118 0.1840 0.2203
REMARK 3 13 1.6169 - 1.5743 1.00 2790 135 0.2001 0.2031
REMARK 3 14 1.5743 - 1.5359 0.98 2716 122 0.2323 0.2589
REMARK 3 15 1.5359 - 1.5010 0.92 2581 140 0.2709 0.2829
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.67
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 12:306 OR RESID 401:401 OR
REMARK 3 RESID 501:711 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.121 1.040 -13.350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0642 T22: 0.0665
REMARK 3 T33: 0.0743 T12: 0.0000
REMARK 3 T13: -0.0004 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.9514 L22: 1.0875
REMARK 3 L33: 0.8281 L12: 0.1559
REMARK 3 L13: -0.1787 L23: -0.4426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0051 S12: -0.0541 S13: 0.0091
REMARK 3 S21: -0.0408 S22: -0.0168 S23: -0.0111
REMARK 3 S31: 0.0647 S32: 0.0128 S33: 0.0059
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 7OME COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1292116013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44303
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 43.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 11.50
REMARK 200 R MERGE (I) : 0.21100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7000
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) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 1.49500
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: 2PSJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG1500, SPG BUFFER, PH 9, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 21.53800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.04800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.24350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.04800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.53800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.24350
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11800 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
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 LEU A 27 -124.29 49.70
REMARK 500 SER A 29 -149.86 -142.35
REMARK 500 ASP A 37 77.65 -152.84
REMARK 500 PRO A 52 47.40 -108.35
REMARK 500 THR A 53 -159.84 -100.89
REMARK 500 ASP A 118 -135.28 52.89
REMARK 500 GLU A 142 55.99 39.95
REMARK 500 GLU A 149 -87.79 -96.40
REMARK 500 LYS A 228 63.11 -120.00
REMARK 500 PHE A 259 -68.22 -122.60
REMARK 500 LEU A 282 -137.50 -102.84
REMARK 500 PHE A 284 59.92 -92.55
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 VK8 A 401
DBREF 7OME A 1 312 PDB 7OME 7OME 1 312
SEQRES 1 A 312 MET VAL SER ALA SER GLN ARG THR THR SER THR ALA THR
SEQRES 2 A 312 GLY ASP GLU TRP TRP ALA LYS CYS LYS GLN VAL ASP VAL
SEQRES 3 A 312 LEU ASP SER GLU MET SER TYR TYR ASP SER ASP PRO GLY
SEQRES 4 A 312 LYS HIS LYS ASN THR VAL ILE PHE LEU HIS GLY ASN PRO
SEQRES 5 A 312 THR SER SER TYR LEU TRP ARG ASN VAL ILE PRO HIS VAL
SEQRES 6 A 312 GLU PRO LEU ALA ARG CYS LEU ALA PRO ASP LEU ILE GLY
SEQRES 7 A 312 MET GLY LYS SER GLY LYS LEU PRO ASN HIS SER TYR ARG
SEQRES 8 A 312 PHE VAL ASP HIS TYR ARG TYR LEU SER ALA TRP PHE ASP
SEQRES 9 A 312 SER VAL ASN LEU PRO GLU LYS VAL THR ILE VAL CYS HIS
SEQRES 10 A 312 ASP TRP GLY SER GLY LEU GLY PHE HIS TRP CYS ASN GLU
SEQRES 11 A 312 HIS ARG ASP ARG VAL LYS GLY ILE VAL HIS MET GLU SER
SEQRES 12 A 312 VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO ASP
SEQRES 13 A 312 ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU ALA GLY
SEQRES 14 A 312 GLU GLU MET VAL LEU LYS LYS ASN PHE PHE ILE GLU ARG
SEQRES 15 A 312 LEU LEU PRO SER SER ILE MET ARG LYS LEU SER GLU GLU
SEQRES 16 A 312 GLU MET ASP ALA TYR ARG GLU PRO PHE VAL GLU PRO GLY
SEQRES 17 A 312 GLU SER ARG ARG PRO THR LEU THR TRP PRO ARG GLU ILE
SEQRES 18 A 312 PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL ILE GLU ILE
SEQRES 19 A 312 VAL LYS SER TYR ASN LYS TRP LEU SER THR SER LYS ASP
SEQRES 20 A 312 ILE PRO LYS LEU PHE ILE ASN ALA ASP PRO GLY PHE PHE
SEQRES 21 A 312 SER ASN ALA ILE LYS LYS VAL THR LYS ASN TRP PRO ASN
SEQRES 22 A 312 GLN LYS THR VAL THR VAL LYS GLY LEU HIS PHE LEU GLN
SEQRES 23 A 312 GLU ASP SER PRO GLU GLU ILE GLY GLU ALA ILE ALA ASP
SEQRES 24 A 312 PHE LEU ASN GLU LEU THR LYS HIS HIS HIS HIS HIS HIS
HET VK8 A 401 32
HETNAM VK8 6-(4-HYDROXYPHENYL)-2-[(4-HYDROXYPHENYL)METHYL]-8-
HETNAM 2 VK8 (PHENYLMETHYL)-[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-3-ONE
FORMUL 2 VK8 C25 H20 N4 O3
FORMUL 3 HOH *211(H2 O)
HELIX 1 AA1 THR A 13 LYS A 20 1 8
HELIX 2 AA2 SER A 54 ARG A 59 5 6
HELIX 3 AA3 VAL A 61 VAL A 65 5 5
HELIX 4 AA4 ARG A 91 ASP A 104 1 14
HELIX 5 AA5 ASP A 118 HIS A 131 1 14
HELIX 6 AA6 ILE A 157 SER A 166 1 10
HELIX 7 AA7 GLU A 167 LYS A 175 1 9
HELIX 8 AA8 ASN A 177 ARG A 182 1 6
HELIX 9 AA9 ARG A 182 SER A 187 1 6
HELIX 10 AB1 SER A 193 GLU A 202 1 10
HELIX 11 AB2 PRO A 203 VAL A 205 5 3
HELIX 12 AB3 GLY A 208 SER A 210 5 3
HELIX 13 AB4 ARG A 211 GLU A 220 1 10
HELIX 14 AB5 LYS A 228 SER A 243 1 16
HELIX 15 AB6 PHE A 260 THR A 268 1 9
HELIX 16 AB7 PHE A 284 ASP A 288 5 5
HELIX 17 AB8 SER A 289 LEU A 304 1 16
SHEET 1 AA1 8 LYS A 22 VAL A 26 0
SHEET 2 AA1 8 SER A 29 ASP A 35 -1 O TYR A 33 N LYS A 22
SHEET 3 AA1 8 ARG A 70 PRO A 74 -1 O ALA A 73 N TYR A 34
SHEET 4 AA1 8 THR A 44 LEU A 48 1 N VAL A 45 O ARG A 70
SHEET 5 AA1 8 VAL A 112 HIS A 117 1 O VAL A 115 N ILE A 46
SHEET 6 AA1 8 VAL A 135 MET A 141 1 O VAL A 139 N ILE A 114
SHEET 7 AA1 8 LYS A 250 PRO A 257 1 O ILE A 253 N HIS A 140
SHEET 8 AA1 8 GLN A 274 GLY A 281 1 O LYS A 275 N PHE A 252
CISPEP 1 ASN A 51 PRO A 52 0 2.61
CISPEP 2 ASP A 256 PRO A 257 0 5.31
SITE 1 AC1 16 ASP A 118 TRP A 119 GLU A 142 SER A 143
SITE 2 AC1 16 VAL A 144 TRP A 154 ASP A 160 PHE A 178
SITE 3 AC1 16 LEU A 183 SER A 187 PRO A 218 PHE A 260
SITE 4 AC1 16 PHE A 284 HOH A 598 HOH A 603 HOH A 655
CRYST1 43.076 64.487 98.096 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 0.023215 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010194 0.00000
TER 2423 LYS A 306
MASTER 280 0 1 17 8 0 4 6 2639 1 32 24
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