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HEADER LUMINESCENT PROTEIN 24-MAY-21 7OMR
TITLE CRYSTAL STRUCTURE OF COELENTERAMIDE-BOUND RENILLA RENIFORMIS
TITLE 2 LUCIFERASE RLUC8-D162A VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COELENTERAZINE H 2-MONOOXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RENILLA-LUCIFERIN 2-MONOOXYGENASE,RENILLA-TYPE LUCIFERASE;
COMPND 5 EC: 1.13.12.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;
SOURCE 3 ORGANISM_COMMON: SEA PANSY;
SOURCE 4 ORGANISM_TAXID: 6136;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOLUMINSCENCE, COELENTERAMIDE-BOUND ENZYME, LUMINESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHENKMAYEROVA,M.MAREK
REVDAT 1 01-JUN-22 7OMR 0
JRNL AUTH A.SCHENKMAYEROVA,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 1.19.2-4158
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) : 46.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54626
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2763
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 46.1870 - 4.0718 1.00 2785 160 0.1701 0.1695
REMARK 3 2 4.0718 - 3.2322 1.00 2658 145 0.1423 0.1297
REMARK 3 3 3.2322 - 2.8237 1.00 2640 136 0.1559 0.1947
REMARK 3 4 2.8237 - 2.5655 1.00 2644 122 0.1582 0.1624
REMARK 3 5 2.5655 - 2.3817 1.00 2613 132 0.1579 0.1858
REMARK 3 6 2.3817 - 2.2413 1.00 2583 156 0.1606 0.1641
REMARK 3 7 2.2413 - 2.1290 1.00 2609 130 0.1664 0.2070
REMARK 3 8 2.1290 - 2.0363 1.00 2592 135 0.1687 0.2034
REMARK 3 9 2.0363 - 1.9579 1.00 2543 155 0.1755 0.2275
REMARK 3 10 1.9579 - 1.8904 1.00 2569 158 0.1772 0.2171
REMARK 3 11 1.8904 - 1.8313 1.00 2574 137 0.1844 0.2261
REMARK 3 12 1.8313 - 1.7789 1.00 2574 136 0.1884 0.2273
REMARK 3 13 1.7789 - 1.7321 1.00 2579 132 0.1915 0.1994
REMARK 3 14 1.7321 - 1.6898 1.00 2550 136 0.1896 0.2310
REMARK 3 15 1.6898 - 1.6514 1.00 2583 127 0.2046 0.2366
REMARK 3 16 1.6514 - 1.6163 1.00 2560 133 0.2198 0.2815
REMARK 3 17 1.6163 - 1.5839 1.00 2566 152 0.2327 0.2615
REMARK 3 18 1.5839 - 1.5540 1.00 2577 112 0.2420 0.2507
REMARK 3 19 1.5540 - 1.5263 1.00 2539 134 0.2617 0.2725
REMARK 3 20 1.5263 - 1.5004 0.98 2525 135 0.3045 0.3354
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) : 20.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.99
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 : 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 7OMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1292116056.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
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) : 0.9999
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 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54685
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 46.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.8000
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 11.90
REMARK 200 R MERGE FOR SHELL (I) : 2.14100
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 (%): 46.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, POTASSIUM PHOSPHATE,
REMARK 280 GLYCEROL, PH 8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 28.22250
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.17300
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.22250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.17300
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: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 GLN A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
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 30 -119.37 51.94
REMARK 500 SER A 32 -147.55 -147.23
REMARK 500 GLU A 40 -50.32 71.81
REMARK 500 ALA A 54 -16.68 76.99
REMARK 500 THR A 55 -160.93 -114.67
REMARK 500 ASP A 120 -130.33 57.34
REMARK 500 HIS A 133 59.67 -142.16
REMARK 500 LEU A 284 -85.92 -103.85
REMARK 500 ALA A 291 52.74 -142.21
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 CEI A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
DBREF 7OMR A 1 311 UNP P27652 LUCI_RENRE 1 311
SEQADV 7OMR THR A 55 UNP P27652 ALA 55 CONFLICT
SEQADV 7OMR ALA A 124 UNP P27652 CYS 124 CONFLICT
SEQADV 7OMR ALA A 130 UNP P27652 SER 130 CONFLICT
SEQADV 7OMR ARG A 136 UNP P27652 LYS 136 CONFLICT
SEQADV 7OMR MET A 143 UNP P27652 ALA 143 CONFLICT
SEQADV 7OMR ALA A 162 UNP P27652 ASP 162 ENGINEERED MUTATION
SEQADV 7OMR VAL A 185 UNP P27652 MET 185 CONFLICT
SEQADV 7OMR LEU A 253 UNP P27652 MET 253 CONFLICT
SEQADV 7OMR LEU A 287 UNP P27652 SER 287 CONFLICT
SEQADV 7OMR HIS A 312 UNP P27652 EXPRESSION TAG
SEQADV 7OMR HIS A 313 UNP P27652 EXPRESSION TAG
SEQADV 7OMR HIS A 314 UNP P27652 EXPRESSION TAG
SEQADV 7OMR HIS A 315 UNP P27652 EXPRESSION TAG
SEQADV 7OMR HIS A 316 UNP P27652 EXPRESSION TAG
SEQADV 7OMR HIS A 317 UNP P27652 EXPRESSION TAG
SEQRES 1 A 317 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 A 317 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 A 317 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 A 317 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 A 317 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 A 317 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 A 317 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 A 317 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 A 317 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 A 317 GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 A 317 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 A 317 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 A 317 PRO ASP ILE GLU GLU ALA ILE ALA LEU ILE LYS SER GLU
SEQRES 14 A 317 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 A 317 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 A 317 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 A 317 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 A 317 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 A 317 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 A 317 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 A 317 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 A 317 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 A 317 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 A 317 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN HIS
SEQRES 25 A 317 HIS HIS HIS HIS HIS
HET CEI A 401 31
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HETNAM CEI N-[3-BENZYL-5-(4-HYDROXYPHENYL)PYRAZIN-2-YL]-2-(4-
HETNAM 2 CEI HYDROXYPHENYL)ACETAMIDE
HETNAM GOL GLYCEROL
HETSYN CEI COELENTERAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CEI C25 H21 N3 O3
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 7 HOH *343(H2 O)
HELIX 1 AA1 GLU A 9 ARG A 13 5 5
HELIX 2 AA2 THR A 16 ARG A 23 1 8
HELIX 3 AA3 SER A 56 ARG A 61 5 6
HELIX 4 AA4 VAL A 63 ILE A 67 5 5
HELIX 5 AA5 ARG A 93 GLU A 106 1 14
HELIX 6 AA6 ASP A 120 HIS A 133 1 14
HELIX 7 AA7 GLU A 151 GLU A 155 5 5
HELIX 8 AA8 TRP A 156 LYS A 167 1 12
HELIX 9 AA9 SER A 168 GLU A 177 1 10
HELIX 10 AB1 ASN A 179 THR A 184 1 6
HELIX 11 AB2 THR A 184 LYS A 189 1 6
HELIX 12 AB3 GLU A 195 GLU A 204 1 10
HELIX 13 AB4 PRO A 205 LYS A 207 5 3
HELIX 14 AB5 GLY A 210 VAL A 212 5 3
HELIX 15 AB6 ARG A 213 GLU A 222 1 10
HELIX 16 AB7 LYS A 230 ALA A 246 1 17
HELIX 17 AB8 SER A 263 LYS A 271 1 9
HELIX 18 AB9 PHE A 286 ASP A 290 5 5
HELIX 19 AC1 ALA A 291 GLU A 310 1 20
SHEET 1 AA1 8 LYS A 25 VAL A 29 0
SHEET 2 AA1 8 SER A 32 ASP A 38 -1 O TYR A 36 N LYS A 25
SHEET 3 AA1 8 ARG A 72 PRO A 76 -1 O ILE A 75 N TYR A 37
SHEET 4 AA1 8 ALA A 46 LEU A 50 1 N VAL A 47 O ARG A 72
SHEET 5 AA1 8 ILE A 114 HIS A 119 1 O VAL A 117 N LEU A 50
SHEET 6 AA1 8 ILE A 137 MET A 143 1 O LYS A 138 N ILE A 114
SHEET 7 AA1 8 LYS A 252 PRO A 259 1 O LEU A 253 N HIS A 142
SHEET 8 AA1 8 THR A 276 GLY A 283 1 O VAL A 279 N GLU A 256
CISPEP 1 ASP A 258 PRO A 259 0 9.59
SITE 1 AC1 12 SER A 145 VAL A 146 VAL A 147 ASP A 148
SITE 2 AC1 12 ILE A 150 TRP A 156 ASP A 158 ILE A 159
SITE 3 AC1 12 ALA A 162 ILE A 223 PHE A 262 ALA A 265
SITE 1 AC2 9 PRO A 18 ASP A 31 GLY A 88 ASN A 89
SITE 2 AC2 9 GLU A 197 HOH A 535 HOH A 568 HOH A 621
SITE 3 AC2 9 HOH A 653
SITE 1 AC3 10 ARG A 11 LYS A 12 ARG A 13 MET A 14
SITE 2 AC3 10 GLN A 19 ASP A 31 SER A 32 PHE A 33
SITE 3 AC3 10 HOH A 502 HOH A 707
SITE 1 AC4 4 ASN A 89 SER A 91 ARG A 93 ASP A 96
SITE 1 AC5 6 TRP A 153 GLU A 277 SER A 301 PHE A 302
SITE 2 AC5 6 ARG A 305 HOH A 697
CRYST1 56.445 74.166 80.346 90.00 90.00 90.00 P 21 2 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 0.017716 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013483 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012446 0.00000
TER 2563 GLU A 310
MASTER 274 0 5 19 8 0 12 6 2927 1 55 25
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