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HEADER HYDROLASE 25-JAN-18 6FLD
TITLE CARBAMYLATED T. CALIFORNICA ACETYLCHOLINETERASE BOUND TO UNCHARGED
TITLE 2 HYBRID REACTIVATOR 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: TETRONARCE CALIFORNICA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7787
KEYWDS ACETYLCHOLINESTERASE HYBRID REACTIVATORS ORGANOPHOSPHATE INHIBITION
KEYWDS 2 STRUCTURE-BASED OPTIMIZATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DE LA MORA,G.SANTONI,J.DE SOUZA,J.SUSSMAN,I.SILMAN,R.BAATI,M.WEIK,
AUTHOR 2 F.NACHON
REVDAT 1 29-AUG-18 6FLD 0
JRNL AUTH G.SANTONI,J.DE SOUSA,E.DE LA MORA,J.DIAS,L.JEAN,J.L.SUSSMAN,
JRNL AUTH 2 I.SILMAN,P.Y.RENARD,R.C.D.BROWN,M.WEIK,R.BAATI,F.NACHON
JRNL TITL STRUCTURE-BASED OPTIMIZATION OF NON-QUATERNARY REACTIVATORS
JRNL TITL 2 OF ACETYLCHOLINESTERASE INHIBITED BY ORGANOPHOSPHORUS NERVE
JRNL TITL 3 AGENTS.
JRNL REF J. MED. CHEM. 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30125110
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00592
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.200
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 40520
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
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 37.3230 - 5.7835 1.00 2925 148 0.1651 0.1845
REMARK 3 2 5.7835 - 4.5932 1.00 2814 143 0.1424 0.1475
REMARK 3 3 4.5932 - 4.0133 1.00 2786 148 0.1329 0.1427
REMARK 3 4 4.0133 - 3.6467 1.00 2759 141 0.1541 0.1831
REMARK 3 5 3.6467 - 3.3855 1.00 2768 144 0.1749 0.2426
REMARK 3 6 3.3855 - 3.1861 1.00 2716 139 0.1983 0.2780
REMARK 3 7 3.1861 - 3.0266 1.00 2772 148 0.2169 0.2571
REMARK 3 8 3.0266 - 2.8949 1.00 2733 142 0.2066 0.2375
REMARK 3 9 2.8949 - 2.7835 1.00 2714 139 0.2117 0.2685
REMARK 3 10 2.7835 - 2.6874 1.00 2744 140 0.2196 0.2608
REMARK 3 11 2.6874 - 2.6034 1.00 2712 141 0.2379 0.2987
REMARK 3 12 2.6034 - 2.5290 1.00 2708 138 0.2528 0.2871
REMARK 3 13 2.5290 - 2.4625 1.00 2731 141 0.2765 0.3043
REMARK 3 14 2.4625 - 2.4024 0.97 2646 140 0.3003 0.3645
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.40
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 : 0.012 4489
REMARK 3 ANGLE : 1.049 6096
REMARK 3 CHIRALITY : 0.073 638
REMARK 3 PLANARITY : 0.008 789
REMARK 3 DIHEDRAL : 19.422 1645
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 6FLD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200008535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40520
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 37.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.78000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 200 30 %, MES 100 MM PH 5.4.,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.66000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.32000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.32000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.66000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 171.01500
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 98.73556
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 319.62000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 89 CD OE1 OE2
REMARK 470 LYS A 270 CE NZ
REMARK 470 GLU A 299 CD OE1 OE2
REMARK 470 LYS A 454 CD CE NZ
REMARK 470 SER A 490 OG
REMARK 470 LYS A 491 CE NZ
REMARK 470 LYS A 530 CE NZ
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 SG CYS A 402 SG CYS A 521 1.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 521 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LYS A 11 -5.80 -59.13
REMARK 500 VAL A 22 112.53 -161.50
REMARK 500 SER A 25 -159.90 -153.97
REMARK 500 PHE A 45 -17.83 90.46
REMARK 500 SER A 108 92.93 -162.11
REMARK 500 ASN A 167 8.65 59.84
REMARK 500 BXT A 200 -130.88 58.48
REMARK 500 GLU A 299 -75.10 -110.63
REMARK 500 THR A 303 -164.27 -127.05
REMARK 500 ASN A 382 52.86 -101.70
REMARK 500 VAL A 400 -59.56 -140.61
REMARK 500 ASN A 457 34.92 71.05
REMARK 500 HIS A 486 52.12 36.18
REMARK 500 ARG A 515 66.63 63.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 BXT A 200 26.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PG A 605
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DQ5 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PG A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800 to ASN A 457
DBREF 6FLD A 4 535 UNP P04058 ACES_TETCF 25 556
SEQRES 1 A 532 SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET
SEQRES 2 A 532 GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA
SEQRES 3 A 532 PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN
SEQRES 4 A 532 MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER
SEQRES 5 A 532 GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN
SEQRES 6 A 532 GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER
SEQRES 7 A 532 GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS
SEQRES 8 A 532 LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS
SEQRES 9 A 532 SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE
SEQRES 10 A 532 TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS
SEQRES 11 A 532 TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU
SEQRES 12 A 532 SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS
SEQRES 13 A 532 GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP
SEQRES 14 A 532 GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN
SEQRES 15 A 532 PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY
SEQRES 16 A 532 GLU BXT ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU
SEQRES 17 A 532 SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU
SEQRES 18 A 532 GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER
SEQRES 19 A 532 VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG
SEQRES 20 A 532 ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE
SEQRES 21 A 532 HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP
SEQRES 22 A 532 VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG
SEQRES 23 A 532 PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO
SEQRES 24 A 532 THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS
SEQRES 25 A 532 LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY
SEQRES 26 A 532 SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS
SEQRES 27 A 532 ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET SER
SEQRES 28 A 532 GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY
SEQRES 29 A 532 LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP
SEQRES 30 A 532 ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP
SEQRES 31 A 532 ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS
SEQRES 32 A 532 PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR
SEQRES 33 A 532 LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP
SEQRES 34 A 532 PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU
SEQRES 35 A 532 PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR
SEQRES 36 A 532 THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS
SEQRES 37 A 532 TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU
SEQRES 38 A 532 PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR THR
SEQRES 39 A 532 LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET
SEQRES 40 A 532 LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE
SEQRES 41 A 532 TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR
MODRES 6FLD BXT A 200 SER MODIFIED RESIDUE
HET BXT A 200 12
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET DQ5 A 604 29
HET 1PG A 605 16
HET CL A 606 1
HET CL A 607 1
HET CL A 608 1
HET CL A 609 1
HET CL A 610 1
HET EDO A 611 4
HET EDO A 612 4
HET EDO A 613 4
HETNAM BXT (2~{S})-2-AZANYL-3-[ETHYL(METHYL)CARBAMOYL]OXY-
HETNAM 2 BXT PROPANOIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM DQ5 2-[(~{E})-HYDROXYIMINOMETHYL]-6-[4-(1,2,3,4-
HETNAM 2 DQ5 TETRAHYDROACRIDIN-9-YLAMINO)BUTYL]PYRIDIN-3-OL
HETNAM 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 2 1PG ETHANOL
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 BXT C7 H14 N2 O4
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 5 DQ5 C23 H26 N4 O2
FORMUL 6 1PG C11 H24 O6
FORMUL 7 CL 5(CL 1-)
FORMUL 12 EDO 3(C2 H6 O2)
FORMUL 15 HOH *212(H2 O)
HELIX 1 AA1 VAL A 40 ARG A 44 5 5
HELIX 2 AA2 PHE A 78 MET A 83 1 6
HELIX 3 AA3 LEU A 127 ASN A 131 5 5
HELIX 4 AA4 GLY A 132 GLU A 140 1 9
HELIX 5 AA5 GLY A 151 LEU A 156 1 6
HELIX 6 AA6 ASN A 167 ILE A 184 1 18
HELIX 7 AA7 GLN A 185 PHE A 187 5 3
HELIX 8 AA8 BXT A 200 SER A 212 1 13
HELIX 9 AA9 PRO A 213 PHE A 219 5 7
HELIX 10 AB1 VAL A 238 LEU A 252 1 15
HELIX 11 AB2 SER A 258 LYS A 269 1 12
HELIX 12 AB3 LYS A 270 GLU A 278 1 9
HELIX 13 AB4 TRP A 279 LEU A 282 5 4
HELIX 14 AB5 SER A 304 GLY A 312 1 9
HELIX 15 AB6 GLY A 328 ALA A 336 1 9
HELIX 16 AB7 SER A 348 VAL A 360 1 13
HELIX 17 AB8 ASN A 364 THR A 376 1 13
HELIX 18 AB9 ASN A 383 VAL A 400 1 18
HELIX 19 AC1 VAL A 400 LYS A 413 1 14
HELIX 20 AC2 PRO A 433 GLY A 437 5 5
HELIX 21 AC3 GLU A 443 PHE A 448 1 6
HELIX 22 AC4 GLY A 449 ASN A 457 5 9
HELIX 23 AC5 THR A 459 GLY A 480 1 22
HELIX 24 AC6 ARG A 517 GLN A 526 1 10
HELIX 25 AC7 GLN A 526 ASN A 533 1 8
SHEET 1 AA1 3 LEU A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 MET A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 AA1 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 AA211 THR A 18 PRO A 21 0
SHEET 2 AA211 HIS A 26 PRO A 34 -1 O ALA A 29 N THR A 18
SHEET 3 AA211 TYR A 96 VAL A 101 -1 O ILE A 99 N PHE A 30
SHEET 4 AA211 VAL A 142 SER A 145 -1 O SER A 145 N ASN A 98
SHEET 5 AA211 THR A 109 ILE A 115 1 N MET A 112 O VAL A 144
SHEET 6 AA211 GLY A 189 GLU A 199 1 O ASP A 190 N THR A 109
SHEET 7 AA211 ARG A 221 GLN A 225 1 O ILE A 223 N ILE A 196
SHEET 8 AA211 ILE A 319 ASN A 324 1 O LEU A 320 N ALA A 222
SHEET 9 AA211 THR A 418 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 AA211 LYS A 501 LEU A 505 1 O ILE A 503 N PHE A 422
SHEET 11 AA211 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AA3 2 ASN A 66 CYS A 67 0
SHEET 2 AA3 2 MET A 90 SER A 91 1 O SER A 91 N ASN A 66
SHEET 1 AA4 2 VAL A 236 SER A 237 0
SHEET 2 AA4 2 VAL A 295 ILE A 296 1 O ILE A 296 N VAL A 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.05
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.03
LINK ND2 ASN A 59 C1 NAG A 601 1555 1555 1.46
LINK C GLU A 199 N BXT A 200 1555 1555 1.45
LINK C BXT A 200 N ALA A 201 1555 1555 1.33
LINK ND2 ASN A 416 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 457 C1 NAG A 603 1555 1555 1.45
CISPEP 1 SER A 103 PRO A 104 0 1.34
SITE 1 AC1 10 TYR A 70 TYR A 121 HIS A 181 TRP A 279
SITE 2 AC1 10 SER A 286 TYR A 334 GLY A 335 1PG A 605
SITE 3 AC1 10 HOH A 787 HOH A 815
SITE 1 AC2 10 TRP A 84 GLY A 118 GLU A 199 BXT A 200
SITE 2 AC2 10 PHE A 330 PHE A 331 HIS A 440 DQ5 A 604
SITE 3 AC2 10 HOH A 751 HOH A 805
SITE 1 AC3 3 HIS A 406 HOH A 759 HOH A 911
SITE 1 AC4 4 VAL A 360 PRO A 361 HIS A 362 HOH A 887
SITE 1 AC5 2 ARG A 216 LYS A 316
SITE 1 AC6 2 LEU A 23 TYR A 134
SITE 1 AC7 4 LEU A 494 THR A 496 THR A 497 NAG A 602
SITE 1 AC8 6 GLN A 178 ASP A 217 LEU A 218 PRO A 337
SITE 2 AC8 6 GLY A 338 PHE A 339
SITE 1 AC9 2 SER A 55 VAL A 57
SITE 1 AD1 2 ASN A 59 SER A 61
SITE 1 AD2 3 ASN A 416 EDO A 611 HOH A 745
SITE 1 AD3 1 ASN A 457
CRYST1 114.010 114.010 136.980 90.00 90.00 120.00 P 31 2 1 6
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 0.008771 0.005064 0.000000 0.00000
SCALE2 0.000000 0.010128 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007300 0.00000
TER 4260 THR A 535
MASTER 362 0 14 25 18 0 17 6 4550 1 120 41
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