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HEADER LUMINESCENT PROTEIN 24-MAY-21 7OMO
TITLE CRYSTAL STRUCTURE OF COELENTERAMINE-BOUND RENILLA RENIFORMIS
TITLE 2 LUCIFERASE RLUC8-D120A VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENILLA RENIFORMIS LUCIFERASE RLUC8-D120A VARIANT;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;
SOURCE 3 ORGANISM_TAXID: 6136;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 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 7OMO 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. 1.45 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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 111416
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 5471
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 10.0000 - 4.5073 1.00 3579 187 0.1620 0.1684
REMARK 3 2 4.5073 - 3.5780 1.00 3550 192 0.1409 0.1541
REMARK 3 3 3.5780 - 3.1258 1.00 3535 197 0.1499 0.1562
REMARK 3 4 3.1258 - 2.8401 1.00 3541 189 0.1614 0.1831
REMARK 3 5 2.8401 - 2.6365 1.00 3550 165 0.1599 0.1794
REMARK 3 6 2.6365 - 2.4811 1.00 3560 151 0.1677 0.1985
REMARK 3 7 2.4811 - 2.3568 1.00 3543 168 0.1617 0.1884
REMARK 3 8 2.3568 - 2.2542 1.00 3540 186 0.1583 0.1843
REMARK 3 9 2.2542 - 2.1675 1.00 3567 172 0.1571 0.1571
REMARK 3 10 2.1675 - 2.0927 1.00 3528 175 0.1608 0.1883
REMARK 3 11 2.0927 - 2.0272 1.00 3507 190 0.1585 0.1994
REMARK 3 12 2.0272 - 1.9693 1.00 3530 180 0.1573 0.1884
REMARK 3 13 1.9693 - 1.9174 1.00 3516 207 0.1610 0.1803
REMARK 3 14 1.9174 - 1.8707 1.00 3537 178 0.1662 0.1766
REMARK 3 15 1.8707 - 1.8281 1.00 3540 186 0.1635 0.2108
REMARK 3 16 1.8281 - 1.7892 1.00 3518 180 0.1689 0.2133
REMARK 3 17 1.7892 - 1.7534 1.00 3527 174 0.1674 0.1945
REMARK 3 18 1.7534 - 1.7203 1.00 3547 213 0.1692 0.1769
REMARK 3 19 1.7203 - 1.6896 1.00 3449 187 0.1696 0.1768
REMARK 3 20 1.6896 - 1.6610 1.00 3576 195 0.1726 0.1945
REMARK 3 21 1.6610 - 1.6342 1.00 3463 180 0.1789 0.1930
REMARK 3 22 1.6342 - 1.6090 1.00 3606 163 0.1866 0.2036
REMARK 3 23 1.6090 - 1.5854 1.00 3444 181 0.1915 0.2399
REMARK 3 24 1.5854 - 1.5630 1.00 3594 182 0.1985 0.2400
REMARK 3 25 1.5630 - 1.5419 1.00 3445 177 0.2056 0.2098
REMARK 3 26 1.5419 - 1.5219 1.00 3587 207 0.2094 0.2139
REMARK 3 27 1.5219 - 1.5029 1.00 3495 174 0.2140 0.2180
REMARK 3 28 1.5029 - 1.4848 1.00 3525 184 0.2207 0.2682
REMARK 3 29 1.4848 - 1.4675 1.00 3576 173 0.2404 0.2659
REMARK 3 30 1.4675 - 1.4510 1.00 3470 178 0.2598 0.2776
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) : 18.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.92
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 5207
REMARK 3 ANGLE : 0.786 7053
REMARK 3 CHIRALITY : 0.080 727
REMARK 3 PLANARITY : 0.005 927
REMARK 3 DIHEDRAL : 5.277 3175
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 7OMO 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_1292116051.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.9990
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 : 111521
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 46.751
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.86100
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: 2SPJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, MAGNESIUM CHLORIDE, BIS-TRIS,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 69.98600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 THR A 2
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 465 MET B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 VAL B 5
REMARK 465 TYR B 6
REMARK 465 ASP B 7
REMARK 465 PRO B 8
REMARK 465 GLU B 9
REMARK 465 GLN B 10
REMARK 465 ASP B 158
REMARK 465 ILE B 159
REMARK 465 GLU B 160
REMARK 465 GLU B 161
REMARK 465 GLU B 310
REMARK 465 GLN B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 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 -127.48 52.91
REMARK 500 SER A 32 -147.02 -146.75
REMARK 500 GLU A 40 -52.00 73.36
REMARK 500 ALA A 54 -16.58 76.23
REMARK 500 THR A 55 -164.97 -115.67
REMARK 500 ALA A 120 -126.37 57.28
REMARK 500 GLU A 151 -66.19 -104.86
REMARK 500 PHE A 261 -63.34 -128.07
REMARK 500 LEU A 284 -111.70 -109.73
REMARK 500 ALA A 291 53.03 -141.72
REMARK 500 LEU B 30 -121.02 51.77
REMARK 500 SER B 32 -147.29 -149.12
REMARK 500 GLU B 40 -51.68 72.47
REMARK 500 ALA B 54 -13.98 78.13
REMARK 500 THR B 55 -161.76 -117.41
REMARK 500 ALA B 120 -128.60 57.12
REMARK 500 LEU B 284 -114.66 -110.44
REMARK 500 ALA B 291 50.82 -144.99
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 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 9 OE1
REMARK 620 2 HOH A 522 O 90.1
REMARK 620 3 HOH A 526 O 86.3 95.9
REMARK 620 4 HOH A 536 O 178.8 89.4 92.7
REMARK 620 5 HOH B 561 O 89.7 91.8 171.3 91.3
REMARK 620 6 HOH B 640 O 89.9 179.9 84.2 90.6 88.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 518 O
REMARK 620 2 HOH A 527 O 91.7
REMARK 620 3 HOH A 560 O 92.3 88.2
REMARK 620 4 HOH B 505 O 95.1 171.9 87.2
REMARK 620 5 HOH B 523 O 177.6 86.6 89.3 86.8
REMARK 620 N 1 2 3 4
DBREF 7OMO A 1 317 PDB 7OMO 7OMO 1 317
DBREF 7OMO B 1 317 PDB 7OMO 7OMO 1 317
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 ALA 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 ASP 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
SEQRES 1 B 317 MET THR SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG
SEQRES 2 B 317 MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN
SEQRES 3 B 317 MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER
SEQRES 4 B 317 GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY
SEQRES 5 B 317 ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO
SEQRES 6 B 317 HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU
SEQRES 7 B 317 ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER
SEQRES 8 B 317 TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP
SEQRES 9 B 317 PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL
SEQRES 10 B 317 GLY HIS ALA TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA
SEQRES 11 B 317 TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET
SEQRES 12 B 317 GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP
SEQRES 13 B 317 PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU
SEQRES 14 B 317 GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL
SEQRES 15 B 317 GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU
SEQRES 16 B 317 PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU
SEQRES 17 B 317 LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 18 B 317 GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL
SEQRES 19 B 317 GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER
SEQRES 20 B 317 ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY
SEQRES 21 B 317 PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE
SEQRES 22 B 317 PRO ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE
SEQRES 23 B 317 LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE
SEQRES 24 B 317 LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN HIS
SEQRES 25 B 317 HIS HIS HIS HIS HIS
HET VKB A 401 21
HET MG A 402 1
HET MG A 403 1
HET CL A 404 1
HET GOL A 405 6
HET GOL A 406 6
HET GOL A 407 6
HET CL B 401 1
HET GOL B 402 6
HETNAM VKB 4-[5-AZANYL-6-(PHENYLMETHYL)PYRAZIN-2-YL]PHENOL
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 VKB C17 H15 N3 O
FORMUL 4 MG 2(MG 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 12 HOH *463(H2 O)
HELIX 1 AA1 ASP A 7 MET A 14 1 8
HELIX 2 AA2 THR A 16 ALA A 22 1 7
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 ALA A 120 HIS A 133 1 14
HELIX 7 AA7 ASP A 158 SER A 168 1 11
HELIX 8 AA8 SER A 168 GLU A 177 1 10
HELIX 9 AA9 ASN A 179 THR A 184 1 6
HELIX 10 AB1 THR A 184 LYS A 189 1 6
HELIX 11 AB2 GLU A 195 GLU A 204 1 10
HELIX 12 AB3 PRO A 205 LYS A 207 5 3
HELIX 13 AB4 GLY A 210 VAL A 212 5 3
HELIX 14 AB5 ARG A 213 GLU A 222 1 10
HELIX 15 AB6 LYS A 230 ALA A 246 1 17
HELIX 16 AB7 PHE A 262 LYS A 272 1 11
HELIX 17 AB8 PHE A 286 ASP A 290 5 5
HELIX 18 AB9 ALA A 291 GLU A 310 1 20
HELIX 19 AC1 THR B 16 ARG B 23 1 8
HELIX 20 AC2 SER B 56 ARG B 61 5 6
HELIX 21 AC3 VAL B 63 ILE B 67 5 5
HELIX 22 AC4 ARG B 93 GLU B 106 1 14
HELIX 23 AC5 ALA B 120 HIS B 133 1 14
HELIX 24 AC6 ILE B 163 SER B 168 1 6
HELIX 25 AC7 GLU B 169 GLU B 177 1 9
HELIX 26 AC8 ASN B 179 THR B 184 1 6
HELIX 27 AC9 THR B 184 LYS B 189 1 6
HELIX 28 AD1 GLU B 195 GLU B 204 1 10
HELIX 29 AD2 PRO B 205 LYS B 207 5 3
HELIX 30 AD3 GLY B 210 VAL B 212 5 3
HELIX 31 AD4 ARG B 213 GLU B 222 1 10
HELIX 32 AD5 LYS B 230 SER B 247 1 18
HELIX 33 AD6 PHE B 262 LYS B 271 1 10
HELIX 34 AD7 PHE B 286 ASP B 290 5 5
HELIX 35 AD8 ALA B 291 ASN B 309 1 19
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 ILE A 115 N ILE A 48
SHEET 6 AA1 8 ILE A 137 MET A 143 1 O VAL A 141 N PHE A 116
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
SHEET 1 AA2 8 LYS B 25 VAL B 29 0
SHEET 2 AA2 8 SER B 32 ASP B 38 -1 O TYR B 36 N LYS B 25
SHEET 3 AA2 8 ARG B 72 PRO B 76 -1 O ILE B 75 N TYR B 37
SHEET 4 AA2 8 ALA B 46 LEU B 50 1 N VAL B 47 O ARG B 72
SHEET 5 AA2 8 ILE B 114 HIS B 119 1 O ILE B 115 N ILE B 48
SHEET 6 AA2 8 ILE B 137 MET B 143 1 O VAL B 141 N PHE B 116
SHEET 7 AA2 8 LYS B 252 PRO B 259 1 O LEU B 253 N HIS B 142
SHEET 8 AA2 8 THR B 276 GLY B 283 1 O VAL B 279 N GLU B 256
LINK OE1 GLU A 9 MG MG A 402 1555 1555 2.05
LINK MG MG A 402 O HOH A 522 1555 1554 2.02
LINK MG MG A 402 O HOH A 526 1555 1554 2.16
LINK MG MG A 402 O HOH A 536 1555 1554 2.09
LINK MG MG A 402 O HOH B 561 1555 1554 2.09
LINK MG MG A 402 O HOH B 640 1555 1554 2.13
LINK MG MG A 403 O HOH A 518 1555 1555 2.24
LINK MG MG A 403 O HOH A 527 1555 1555 2.05
LINK MG MG A 403 O HOH A 560 1555 1555 2.08
LINK MG MG A 403 O HOH B 505 1555 1454 2.00
LINK MG MG A 403 O HOH B 523 1555 1454 2.00
CISPEP 1 ASP A 258 PRO A 259 0 6.05
CISPEP 2 ASP B 258 PRO B 259 0 6.91
CRYST1 49.315 139.972 50.623 90.00 112.56 90.00 P 1 21 1 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 0.020278 0.000000 0.008422 0.00000
SCALE2 0.000000 0.007144 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021390 0.00000
TER 2567 GLU A 310
TER 5015 ASN B 309
MASTER 313 0 9 35 16 0 0 6 5446 2 51 50
END |