HEADER TRANSPORT PROTEIN 29-FEB-16 5IHH
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH LUTEOLIN-MEO
TITLE 2 AT 1.35 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATTR,PREALBUMIN,TBPA;
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: TTR, PALB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA BARREL, WILD TYPE HUMAN TTR, TRANSTHYRETIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BEGUM,L.NILSSON,A.OLOFSSON,A.E.SAUER-ERIKSSON
REVDAT 2 10-JAN-24 5IHH 1 LINK
REVDAT 1 20-APR-16 5IHH 0
JRNL AUTH L.NILSSON,A.LARSSON,A.BEGUM,I.IAKOVLEVA,M.CARLSSON,
JRNL AUTH 2 K.BRANNSTROM,A.E.SAUER-ERIKSSON,A.OLOFSSON
JRNL TITL MODIFICATIONS OF THE 7-HYDROXYL GROUP OF THE TRANSTHYRETIN
JRNL TITL 2 LIGAND LUTEOLIN PROVIDE MECHANISTIC INSIGHTS INTO ITS
JRNL TITL 3 BINDING PROPERTIES AND HIGH PLASMA SPECIFICITY.
JRNL REF PLOS ONE V. 11 53112 2016
JRNL REFN ESSN 1932-6203
JRNL PMID 27050398
JRNL DOI 10.1371/JOURNAL.PONE.0153112
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 52589
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2595
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 42.9968 - 3.6017 1.00 2833 146 0.1596 0.1720
REMARK 3 2 3.6017 - 2.8590 1.00 2706 137 0.1410 0.1853
REMARK 3 3 2.8590 - 2.4976 1.00 2661 145 0.1481 0.1722
REMARK 3 4 2.4976 - 2.2693 1.00 2652 143 0.1389 0.1380
REMARK 3 5 2.2693 - 2.1066 1.00 2625 157 0.1202 0.1461
REMARK 3 6 2.1066 - 1.9824 1.00 2630 139 0.1222 0.1578
REMARK 3 7 1.9824 - 1.8831 1.00 2618 134 0.1232 0.1559
REMARK 3 8 1.8831 - 1.8012 1.00 2623 151 0.1250 0.1581
REMARK 3 9 1.8012 - 1.7318 1.00 2621 121 0.1282 0.1558
REMARK 3 10 1.7318 - 1.6721 1.00 2589 141 0.1252 0.1717
REMARK 3 11 1.6721 - 1.6198 1.00 2636 131 0.1169 0.1441
REMARK 3 12 1.6198 - 1.5735 1.00 2629 120 0.1150 0.1458
REMARK 3 13 1.5735 - 1.5320 1.00 2590 118 0.1223 0.1719
REMARK 3 14 1.5320 - 1.4947 1.00 2641 139 0.1317 0.1766
REMARK 3 15 1.4947 - 1.4607 1.00 2606 118 0.1351 0.1718
REMARK 3 16 1.4607 - 1.4296 1.00 2567 144 0.1423 0.1780
REMARK 3 17 1.4296 - 1.4010 1.00 2604 135 0.1590 0.2157
REMARK 3 18 1.4010 - 1.3746 1.00 2565 139 0.1687 0.2124
REMARK 3 19 1.3746 - 1.3500 1.00 2598 137 0.1652 0.2083
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.009 2073
REMARK 3 ANGLE : 0.968 2856
REMARK 3 CHIRALITY : 0.084 311
REMARK 3 PLANARITY : 0.008 370
REMARK 3 DIHEDRAL : 13.878 725
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 5IHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52635
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 43.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.61700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 1F41
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED TTRWT WAS DIALYZED AGAINST 10
REMARK 280 MM SODIUMPHOSPHATE BUFFER WITH 100 MM KCL PH 7.6 AND
REMARK 280 CONCENTRATED TO 5 MG PER ML. 7MEOLUT WAS ADDED AT 5 X MOLAR
REMARK 280 EXCESS TO THE PROTEIN. THE RESERVOIR CONTAINED 1.3 TO 1.6 M
REMARK 280 SODIUM CITRATE AND 3.5 PERCENT GLYCEROL AT PH 5.5. DROP SIZE 3
REMARK 280 PLUS 3 MICROLITER, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
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 21.44300
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.97500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 21.44300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.97500
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 42.88600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 C06 6B5 A 201 LIES ON A SPECIAL POSITION.
REMARK 375 C08 6B5 A 201 LIES ON A SPECIAL POSITION.
REMARK 375 C11 6B5 A 201 LIES ON A SPECIAL POSITION.
REMARK 375 O12 6B5 A 201 LIES ON A SPECIAL POSITION.
REMARK 375 C06 6B5 B 201 LIES ON A SPECIAL POSITION.
REMARK 375 C08 6B5 B 201 LIES ON A SPECIAL POSITION.
REMARK 375 C11 6B5 B 201 LIES ON A SPECIAL POSITION.
REMARK 375 O12 6B5 B 201 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 305 LIES ON A SPECIAL POSITION.
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 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLU A 7
REMARK 465 SER A 8
REMARK 465 LYS A 9
REMARK 465 LYS A 126
REMARK 465 GLU A 127
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 7
REMARK 465 SER B 8
REMARK 465 LYS B 9
REMARK 465 PRO B 125
REMARK 465 LYS B 126
REMARK 465 GLU B 127
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HZ2 LYS A 15 O HOH A 305 1.57
REMARK 500 HD1 HIS B 90 O HOH B 302 1.58
REMARK 500 O HOH A 302 O HOH A 347 1.96
REMARK 500 O HOH A 302 O HOH A 318 1.98
REMARK 500 O HOH B 364 O HOH B 389 2.14
REMARK 500 O HOH A 437 O HOH A 442 2.15
REMARK 500 O HOH B 354 O HOH B 372 2.18
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 NA A 202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 99 O
REMARK 620 2 ASP A 99 O 0.4
REMARK 620 3 HOH A 314 O 96.0 95.8
REMARK 620 4 HOH A 315 O 75.9 76.3 94.2
REMARK 620 5 HOH A 380 O 149.3 149.7 89.5 73.7
REMARK 620 6 HOH A 385 O 105.5 105.1 79.7 173.8 105.1
REMARK 620 7 HOH A 405 O 82.1 82.1 166.8 97.9 98.8 88.3
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 6B5 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6B5 B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EN3 RELATED DB: PDB
REMARK 900 THE 5EN3 CONTAINS THE SAME PROTEIN COMPLEXED WITH 7-CL-LUTEOLIN
REMARK 900 RELATED ID: 4QXV RELATED DB: PDB
REMARK 900 THE 4QXV CONTAINS THE SAME PROTEIN COMPLEXED WITH LUTEOLIN
DBREF 5IHH A 1 127 UNP P02766 TTHY_HUMAN 21 147
DBREF 5IHH B 1 127 UNP P02766 TTHY_HUMAN 21 147
SEQRES 1 A 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 A 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 A 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 A 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 A 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 A 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 A 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 A 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 A 127 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 A 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
SEQRES 1 B 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 B 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 B 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 B 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 B 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 B 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 B 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 B 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 B 127 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 B 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
HET 6B5 A 201 34
HET NA A 202 1
HET 6B5 B 201 34
HETNAM 6B5 2-(3,4-DIHYDROXYPHENYL)-5-HYDROXY-7-METHOXY-4H-1-
HETNAM 2 6B5 CHROMEN-4-ONE
HETNAM NA SODIUM ION
HETSYN 6B5 7,8-DIMETHYLALLOXAZINE; 6,7-DIMETHYLALLOXAZINE
FORMUL 3 6B5 2(C16 H12 O6)
FORMUL 4 NA NA 1+
FORMUL 6 HOH *254(H2 O)
HELIX 1 AA1 ASP A 74 LEU A 82 1 9
HELIX 2 AA2 ASP B 74 LEU B 82 1 9
SHEET 1 AA1 8 SER A 23 PRO A 24 0
SHEET 2 AA1 8 LEU A 12 ASP A 18 -1 N ASP A 18 O SER A 23
SHEET 3 AA1 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA1 8 SER A 115 THR A 123 -1 O SER A 115 N SER A 112
SHEET 5 AA1 8 SER B 115 THR B 123 -1 O THR B 118 N TYR A 116
SHEET 6 AA1 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 AA1 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA1 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 AA2 8 GLU A 54 LEU A 55 0
SHEET 2 AA2 8 LEU A 12 ASP A 18 -1 N VAL A 14 O LEU A 55
SHEET 3 AA2 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA2 8 SER A 115 THR A 123 -1 O SER A 115 N SER A 112
SHEET 5 AA2 8 SER B 115 THR B 123 -1 O THR B 118 N TYR A 116
SHEET 6 AA2 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 AA2 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA2 8 GLU B 54 LEU B 55 -1 O LEU B 55 N VAL B 14
SHEET 1 AA3 8 TRP A 41 LYS A 48 0
SHEET 2 AA3 8 ALA A 29 LYS A 35 -1 N VAL A 32 O ALA A 45
SHEET 3 AA3 8 GLY A 67 ILE A 73 -1 O GLU A 72 N HIS A 31
SHEET 4 AA3 8 HIS A 88 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 5 AA3 8 HIS B 88 ALA B 97 -1 O GLU B 89 N VAL A 94
SHEET 6 AA3 8 GLY B 67 ILE B 73 -1 N ILE B 73 O ALA B 91
SHEET 7 AA3 8 ALA B 29 LYS B 35 -1 N HIS B 31 O GLU B 72
SHEET 8 AA3 8 TRP B 41 LYS B 48 -1 O ALA B 45 N VAL B 32
LINK O AASP A 99 NA NA A 202 1555 1555 2.21
LINK O BASP A 99 NA NA A 202 1555 1555 2.21
LINK NA NA A 202 O HOH A 314 1555 1555 2.30
LINK NA NA A 202 O HOH A 315 1555 1555 2.84
LINK NA NA A 202 O HOH A 380 1555 3454 2.26
LINK NA NA A 202 O HOH A 385 1555 1555 2.22
LINK NA NA A 202 O HOH A 405 1555 1555 2.51
SITE 1 AC1 10 LYS A 15 LEU A 17 THR A 106 ALA A 108
SITE 2 AC1 10 LEU A 110 SER A 117 THR A 119 VAL A 121
SITE 3 AC1 10 HOH A 312 HOH A 409
SITE 1 AC2 6 ASP A 99 HOH A 314 HOH A 315 HOH A 380
SITE 2 AC2 6 HOH A 385 HOH A 405
SITE 1 AC3 10 LYS B 15 LEU B 17 THR B 106 ALA B 108
SITE 2 AC3 10 LEU B 110 SER B 117 THR B 119 VAL B 121
SITE 3 AC3 10 HOH B 305 HOH B 401
CRYST1 42.886 63.834 85.950 90.00 90.00 90.00 P 21 2 21 8
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 0.023318 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011635 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
