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HEADER LUMINESCENT PROTEIN 10-APR-20 6YN2
TITLE CRYSTAL STRUCTURE OF RENILLA RENIFORMIS LUCIFERASE VARIANT RLUC8-
TITLE 2 W121F/E144Q IN COMPLEX WITH A COELENTERAMIDE (THE POSTCATALYTIC
TITLE 3 ENZYME-PRODUCT COMPLEX)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COELENTERAZINE H 2-MONOOXYGENASE;
COMPND 3 CHAIN: A, B;
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 J.DAMBORSKY,M.MAREK
REVDAT 1 21-APR-21 6YN2 0
JRNL AUTH M.MAREK,J.DAMBORSKY
JRNL TITL STRUCTURAL BASIS OF THE RENILLA-TYPE BIOLUMINESCENCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14-3260-000
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 82682
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 4176
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 44.5280 - 5.9006 1.00 2782 157 0.1701 0.1780
REMARK 3 2 5.9006 - 4.6852 1.00 2699 140 0.1502 0.1879
REMARK 3 3 4.6852 - 4.0934 1.00 2654 161 0.1221 0.1480
REMARK 3 4 4.0934 - 3.7193 1.00 2644 138 0.1334 0.1549
REMARK 3 5 3.7193 - 3.4529 1.00 2649 151 0.1594 0.1677
REMARK 3 6 3.4529 - 3.2493 1.00 2631 126 0.1669 0.1992
REMARK 3 7 3.2493 - 3.0867 1.00 2610 163 0.1832 0.1969
REMARK 3 8 3.0867 - 2.9523 1.00 2589 166 0.1819 0.1819
REMARK 3 9 2.9523 - 2.8387 1.00 2613 158 0.1840 0.1956
REMARK 3 10 2.8387 - 2.7407 1.00 2617 126 0.1791 0.2177
REMARK 3 11 2.7407 - 2.6551 1.00 2632 148 0.1808 0.2362
REMARK 3 12 2.6551 - 2.5792 1.00 2593 150 0.1897 0.2155
REMARK 3 13 2.5792 - 2.5113 1.00 2605 159 0.1807 0.2199
REMARK 3 14 2.5113 - 2.4500 1.00 2563 154 0.1810 0.2343
REMARK 3 15 2.4500 - 2.3943 1.00 2622 145 0.1832 0.2130
REMARK 3 16 2.3943 - 2.3434 1.00 2606 143 0.1768 0.2463
REMARK 3 17 2.3434 - 2.2965 1.00 2595 129 0.1754 0.1754
REMARK 3 18 2.2965 - 2.2532 1.00 2637 104 0.1738 0.2283
REMARK 3 19 2.2532 - 2.2129 1.00 2593 141 0.1814 0.2166
REMARK 3 20 2.2129 - 2.1754 1.00 2622 146 0.1836 0.2121
REMARK 3 21 2.1754 - 2.1403 1.00 2598 122 0.1956 0.2149
REMARK 3 22 2.1403 - 2.1074 1.00 2598 120 0.1982 0.2659
REMARK 3 23 2.1074 - 2.0764 1.00 2595 136 0.2137 0.2606
REMARK 3 24 2.0764 - 2.0472 1.00 2644 127 0.2230 0.2524
REMARK 3 25 2.0472 - 2.0195 1.00 2599 116 0.2311 0.2484
REMARK 3 26 2.0195 - 1.9933 1.00 2566 151 0.2355 0.2589
REMARK 3 27 1.9933 - 1.9683 1.00 2552 162 0.2455 0.2541
REMARK 3 28 1.9683 - 1.9446 1.00 2646 106 0.2603 0.3151
REMARK 3 29 1.9446 - 1.9220 1.00 2629 111 0.2694 0.2825
REMARK 3 30 1.9220 - 1.9004 0.98 2523 120 0.3039 0.3396
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.54
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 6YN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1292107896.
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 : 4.5
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) : 0.99987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82701
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 12.40
REMARK 200 R MERGE FOR SHELL (I) : 1.80000
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 (%): 65.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAHPO4/K2HPO4, SODIUM ACETATE, PH 4.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.5K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 56.38250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.53850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.01500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.38250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.53850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.01500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.38250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.53850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.01500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.38250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.53850
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 71.01500
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 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 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 -128.88 52.21
REMARK 500 SER A 32 -149.62 -136.43
REMARK 500 GLU A 40 -54.52 70.54
REMARK 500 ALA A 54 -11.85 73.44
REMARK 500 THR A 55 -162.61 -113.96
REMARK 500 ASP A 120 -136.14 61.07
REMARK 500 GLN A 144 55.79 39.84
REMARK 500 TRP A 153 34.13 -99.01
REMARK 500 ASP A 158 99.32 -64.32
REMARK 500 LEU A 284 -118.01 -114.56
REMARK 500 LEU B 30 -125.60 49.91
REMARK 500 SER B 32 -146.32 -146.65
REMARK 500 GLU B 40 -52.55 76.64
REMARK 500 ALA B 54 -14.32 72.15
REMARK 500 THR B 55 -161.38 -111.24
REMARK 500 ASP B 120 -136.83 61.13
REMARK 500 TRP B 153 34.92 -99.48
REMARK 500 LEU B 284 -114.79 -109.04
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 K B 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 26 O
REMARK 620 2 TRP B 21 O 49.7
REMARK 620 3 CYS B 24 O 49.3 1.8
REMARK 620 4 HOH B 510 O 50.6 3.0 1.6
REMARK 620 5 HOH B 623 O 51.1 2.1 1.8 1.5
REMARK 620 6 HOH B 673 O 51.9 2.3 3.3 3.4 1.9
REMARK 620 7 HOH B 720 O 52.8 3.1 4.0 3.8 2.3 0.9
REMARK 620 N 1 2 3 4 5 6
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 ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CEI B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 403
DBREF 6YN2 A 1 311 UNP P27652 LUCI_RENRE 1 311
DBREF 6YN2 B 1 311 UNP P27652 LUCI_RENRE 1 311
SEQADV 6YN2 THR A 55 UNP P27652 ALA 55 CONFLICT
SEQADV 6YN2 PHE A 121 UNP P27652 TRP 121 ENGINEERED MUTATION
SEQADV 6YN2 ALA A 124 UNP P27652 CYS 124 CONFLICT
SEQADV 6YN2 ALA A 130 UNP P27652 SER 130 CONFLICT
SEQADV 6YN2 ARG A 136 UNP P27652 LYS 136 CONFLICT
SEQADV 6YN2 MET A 143 UNP P27652 ALA 143 CONFLICT
SEQADV 6YN2 GLN A 144 UNP P27652 GLU 144 ENGINEERED MUTATION
SEQADV 6YN2 VAL A 185 UNP P27652 MET 185 CONFLICT
SEQADV 6YN2 LEU A 253 UNP P27652 MET 253 CONFLICT
SEQADV 6YN2 LEU A 287 UNP P27652 SER 287 CONFLICT
SEQADV 6YN2 HIS A 312 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS A 313 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS A 314 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS A 315 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS A 316 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS A 317 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 THR B 55 UNP P27652 ALA 55 CONFLICT
SEQADV 6YN2 PHE B 121 UNP P27652 TRP 121 ENGINEERED MUTATION
SEQADV 6YN2 ALA B 124 UNP P27652 CYS 124 CONFLICT
SEQADV 6YN2 ALA B 130 UNP P27652 SER 130 CONFLICT
SEQADV 6YN2 ARG B 136 UNP P27652 LYS 136 CONFLICT
SEQADV 6YN2 MET B 143 UNP P27652 ALA 143 CONFLICT
SEQADV 6YN2 GLN B 144 UNP P27652 GLU 144 ENGINEERED MUTATION
SEQADV 6YN2 VAL B 185 UNP P27652 MET 185 CONFLICT
SEQADV 6YN2 LEU B 253 UNP P27652 MET 253 CONFLICT
SEQADV 6YN2 LEU B 287 UNP P27652 SER 287 CONFLICT
SEQADV 6YN2 HIS B 312 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS B 313 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS B 314 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS B 315 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS B 316 UNP P27652 EXPRESSION TAG
SEQADV 6YN2 HIS B 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 PHE 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 GLN 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 ASP PHE 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 GLN 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 CEI A 401 31
HET ACT A 402 4
HET GOL B 401 6
HET CEI B 402 31
HET K B 403 1
HETNAM CEI N-[3-BENZYL-5-(4-HYDROXYPHENYL)PYRAZIN-2-YL]-2-(4-
HETNAM 2 CEI HYDROXYPHENYL)ACETAMIDE
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETNAM K POTASSIUM ION
HETSYN CEI COELENTERAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CEI 2(C25 H21 N3 O3)
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 GOL C3 H8 O3
FORMUL 7 K K 1+
FORMUL 8 HOH *507(H2 O)
HELIX 1 AA1 GLU A 9 MET A 14 1 6
HELIX 2 AA2 THR A 16 CYS A 24 1 9
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 ILE A 159 SER A 168 1 10
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 271 1 10
HELIX 17 AB8 PHE A 286 ASP A 290 5 5
HELIX 18 AB9 ALA A 291 GLN A 311 1 21
HELIX 19 AC1 GLN B 10 MET B 14 5 5
HELIX 20 AC2 THR B 16 ALA B 22 1 7
HELIX 21 AC3 SER B 56 ARG B 61 5 6
HELIX 22 AC4 VAL B 63 ILE B 67 5 5
HELIX 23 AC5 ARG B 93 GLU B 106 1 14
HELIX 24 AC6 PHE B 121 HIS B 133 1 13
HELIX 25 AC7 ILE B 159 SER B 168 1 10
HELIX 26 AC8 SER B 168 GLU B 177 1 10
HELIX 27 AC9 ASN B 179 THR B 184 1 6
HELIX 28 AD1 THR B 184 LYS B 189 1 6
HELIX 29 AD2 GLU B 195 GLU B 204 1 10
HELIX 30 AD3 PRO B 205 LYS B 207 5 3
HELIX 31 AD4 GLY B 210 VAL B 212 5 3
HELIX 32 AD5 ARG B 213 GLU B 222 1 10
HELIX 33 AD6 LYS B 230 ALA B 246 1 17
HELIX 34 AD7 PHE B 262 LYS B 271 1 10
HELIX 35 AD8 PHE B 286 ASP B 290 5 5
HELIX 36 AD9 ALA B 291 GLU B 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 SER A 145 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 ASP B 120 1 O VAL B 117 N LEU B 50
SHEET 6 AA2 8 ILE B 137 SER B 145 1 O LYS B 138 N ILE B 114
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 O GLN A 26 K K B 403 1555 8444 2.63
LINK O TRP B 21 K K B 403 1555 1555 2.64
LINK O CYS B 24 K K B 403 1555 1555 2.79
LINK K K B 403 O HOH B 510 1555 1555 2.73
LINK K K B 403 O HOH B 623 1555 1555 3.46
LINK K K B 403 O HOH B 673 1555 1555 2.64
LINK K K B 403 O HOH B 720 1555 1555 3.18
CISPEP 1 ASP A 258 PRO A 259 0 6.65
CISPEP 2 ASP B 258 PRO B 259 0 4.53
SITE 1 AC1 15 ASP A 120 GLN A 144 SER A 145 VAL A 146
SITE 2 AC1 15 VAL A 147 ASP A 148 TRP A 156 ILE A 159
SITE 3 AC1 15 ILE A 223 PRO A 224 PHE A 262 ILE A 266
SITE 4 AC1 15 HIS A 285 HOH A 609 ASP B 162
SITE 1 AC2 5 ASN A 53 ASP A 120 PHE A 181 HIS A 285
SITE 2 AC2 5 HOH A 552
SITE 1 AC3 10 ASP A 31 LYS A 86 HOH A 520 SER B 32
SITE 2 AC3 10 LYS B 86 HOH B 517 HOH B 534 HOH B 589
SITE 3 AC3 10 HOH B 630 HOH B 678
SITE 1 AC4 16 ASP A 162 ASP B 120 GLN B 144 SER B 145
SITE 2 AC4 16 VAL B 146 VAL B 147 ASP B 148 TRP B 156
SITE 3 AC4 16 ILE B 159 ASP B 162 PRO B 224 PHE B 262
SITE 4 AC4 16 ILE B 266 HIS B 285 HOH B 538 HOH B 575
SITE 1 AC5 5 GLN A 26 TRP B 21 CYS B 24 HOH B 510
SITE 2 AC5 5 HOH B 673
CRYST1 112.765 131.077 142.030 90.00 90.00 90.00 I 2 2 2 16
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 0.008868 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007041 0.00000
TER 2553 GLN A 311
TER 5094 GLU B 310
MASTER 333 0 5 36 16 0 15 6 5647 2 80 50
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