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HEADER HYDROLASE 28-MAR-18 6G4M
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE BOUND TO UNCHARGED HYBRID
TITLE 2 REACTIVATOR 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS ACETYLCHOLINESTERASE, TABUN, NERVE AGENT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SANTONI,E.DE LA MORA,J.DE SOUZA,I.SILMAN,J.SUSSMAN,R.BAATI,M.WEIK,
AUTHOR 2 F.NACHON
REVDAT 1 29-AUG-18 6G4M 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. 2.63 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) : 2.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 43948
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2221
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 45.9181 - 6.6210 0.99 2792 141 0.2019 0.2551
REMARK 3 2 6.6210 - 5.2577 1.00 2683 145 0.1730 0.2321
REMARK 3 3 5.2577 - 4.5938 1.00 2623 155 0.1396 0.2241
REMARK 3 4 4.5938 - 4.1741 1.00 2642 125 0.1380 0.2116
REMARK 3 5 4.1741 - 3.8751 0.99 2622 127 0.1493 0.2049
REMARK 3 6 3.8751 - 3.6467 1.00 2587 157 0.1595 0.2280
REMARK 3 7 3.6467 - 3.4641 0.99 2622 114 0.1725 0.2531
REMARK 3 8 3.4641 - 3.3134 0.99 2575 144 0.2089 0.2903
REMARK 3 9 3.3134 - 3.1859 1.00 2598 144 0.2204 0.3087
REMARK 3 10 3.1859 - 3.0760 0.99 2585 134 0.2204 0.3419
REMARK 3 11 3.0760 - 2.9798 1.00 2553 153 0.2248 0.2988
REMARK 3 12 2.9798 - 2.8946 0.99 2568 130 0.2317 0.3020
REMARK 3 13 2.8946 - 2.8184 0.99 2589 124 0.2413 0.3130
REMARK 3 14 2.8184 - 2.7497 1.00 2556 144 0.2606 0.3128
REMARK 3 15 2.7497 - 2.6872 0.99 2567 149 0.2643 0.3211
REMARK 3 16 2.6872 - 2.6300 0.99 2565 135 0.2773 0.3799
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.850
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 : 0.008 8943
REMARK 3 ANGLE : 1.038 12153
REMARK 3 CHIRALITY : 0.054 1262
REMARK 3 PLANARITY : 0.006 1568
REMARK 3 DIHEDRAL : 17.598 5241
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 6G4M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009409.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
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 : 43964
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
REMARK 200 RESOLUTION RANGE LOW (A) : 45.911
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.880
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: 1EA5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150MM MES 36% PEG 200, PH 5.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 45.63800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.22800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.22800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.63800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.12000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 2700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 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 ALA A 0
REMARK 465 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ALA B 0
REMARK 465 ASP B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 536
REMARK 465 CYS B 537
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 OE2 GLU A 443 O HOH A 701 1.84
REMARK 500 O PHE B 197 O HOH B 701 1.98
REMARK 500 ND2 ASN A 416 O5 NAG A 603 2.05
REMARK 500 O PHE A 219 O HOH A 702 2.05
REMARK 500 O HOH B 895 O HOH B 899 2.09
REMARK 500 O GLU A 484 OG SER A 487 2.10
REMARK 500 OG SER B 145 O HOH B 702 2.10
REMARK 500 O ASN B 416 O HOH B 703 2.12
REMARK 500 O HOH A 894 O HOH A 933 2.12
REMARK 500 O HOH B 879 O HOH B 951 2.13
REMARK 500 O HOH B 923 O HOH B 938 2.17
REMARK 500 OE2 GLU B 163 O HOH B 704 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 38 C PRO A 39 N 0.118
REMARK 500 GLU B 261 CB GLU B 261 CG -0.154
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 ARG A 517 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 517 NE - CZ - NH2 ANGL. DEV. = 3.6 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 SER A 25 -155.96 -120.70
REMARK 500 PHE A 45 -4.32 76.45
REMARK 500 ALA A 60 62.96 -110.23
REMARK 500 SER A 108 73.06 34.01
REMARK 500 SER A 200 -120.53 60.06
REMARK 500 ASN A 253 58.36 26.04
REMARK 500 GLU A 299 -58.63 -142.93
REMARK 500 THR A 317 -152.32 -158.83
REMARK 500 ASP A 326 60.35 -113.00
REMARK 500 VAL A 360 64.77 -116.85
REMARK 500 ASP A 380 46.84 -161.03
REMARK 500 VAL A 400 -70.85 -124.30
REMARK 500 ASN A 457 31.73 70.60
REMARK 500 PRO A 485 56.40 -96.50
REMARK 500 HIS A 486 -85.73 -159.73
REMARK 500 GLN A 488 -70.15 2.53
REMARK 500 GLU A 489 -116.22 -3.88
REMARK 500 SER A 490 111.97 -170.75
REMARK 500 ARG A 515 67.43 62.43
REMARK 500 PHE B 45 -6.87 76.69
REMARK 500 ALA B 60 51.05 -100.03
REMARK 500 PHE B 155 16.20 -141.06
REMARK 500 LEU B 158 76.54 -116.51
REMARK 500 ALA B 164 76.35 -150.35
REMARK 500 SER B 200 -123.27 57.99
REMARK 500 ARG B 220 -60.26 -96.06
REMARK 500 PRO B 294 155.64 -49.84
REMARK 500 GLU B 299 -72.76 -127.62
REMARK 500 THR B 317 -159.54 -147.53
REMARK 500 ASP B 380 34.88 -171.47
REMARK 500 ASN B 383 98.37 -66.95
REMARK 500 VAL B 400 -70.98 -127.96
REMARK 500 HIS B 440 109.44 -45.78
REMARK 500 PRO B 451 0.69 -65.56
REMARK 500 HIS B 486 55.11 35.93
REMARK 500 ARG B 515 71.59 57.43
REMARK 500 LEU B 516 108.73 -58.17
REMARK 500 GLN B 526 -52.67 -124.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 486 SER A 487 136.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 945 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A 946 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH B 965 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B 966 DISTANCE = 6.23 ANGSTROMS
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DQ5 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DQ5 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DQ5 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800 to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound
REMARK 800 to ASN B 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FLD RELATED DB: PDB
REMARK 900 RELATED ID: 6FQN RELATED DB: PDB
REMARK 900 RELATED ID: 6G17 RELATED DB: PDB
DBREF 6G4M A 0 537 UNP P04058 ACES_TETCF 21 558
DBREF 6G4M B 0 537 UNP P04058 ACES_TETCF 21 558
SEQRES 1 A 538 ALA ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER
SEQRES 2 A 538 GLY LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER
SEQRES 3 A 538 HIS ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 538 PRO VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS
SEQRES 5 A 538 LYS PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO
SEQRES 6 A 538 ASN ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY
SEQRES 7 A 538 PHE SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET
SEQRES 8 A 538 SER GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER
SEQRES 9 A 538 PRO ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR
SEQRES 10 A 538 GLY GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL
SEQRES 11 A 538 TYR ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL
SEQRES 12 A 538 LEU VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE
SEQRES 13 A 538 LEU ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL
SEQRES 14 A 538 GLY LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS
SEQRES 15 A 538 ASP ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL
SEQRES 16 A 538 THR ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY
SEQRES 17 A 538 MET HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG
SEQRES 18 A 538 ARG ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP
SEQRES 19 A 538 ALA SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL
SEQRES 20 A 538 GLU LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP
SEQRES 21 A 538 GLU GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN
SEQRES 22 A 538 GLU LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP
SEQRES 23 A 538 SER ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY
SEQRES 24 A 538 GLU PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER
SEQRES 25 A 538 GLY ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN
SEQRES 26 A 538 LYS ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO
SEQRES 27 A 538 GLY PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU
SEQRES 28 A 538 ASP PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA
SEQRES 29 A 538 ASN ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR
SEQRES 30 A 538 ASP TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP
SEQRES 31 A 538 GLY LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS
SEQRES 32 A 538 PRO LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY
SEQRES 33 A 538 ASN GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER
SEQRES 34 A 538 ASN LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY
SEQRES 35 A 538 TYR GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS
SEQRES 36 A 538 GLU LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG
SEQRES 37 A 538 ARG ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY
SEQRES 38 A 538 ASN PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO
SEQRES 39 A 538 LEU PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN
SEQRES 40 A 538 THR GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN
SEQRES 41 A 538 MET CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU
SEQRES 42 A 538 ASN ALA THR ALA CYS
SEQRES 1 B 538 ALA ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER
SEQRES 2 B 538 GLY LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER
SEQRES 3 B 538 HIS ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 538 PRO VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS
SEQRES 5 B 538 LYS PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO
SEQRES 6 B 538 ASN ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY
SEQRES 7 B 538 PHE SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET
SEQRES 8 B 538 SER GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER
SEQRES 9 B 538 PRO ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR
SEQRES 10 B 538 GLY GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL
SEQRES 11 B 538 TYR ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL
SEQRES 12 B 538 LEU VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE
SEQRES 13 B 538 LEU ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL
SEQRES 14 B 538 GLY LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS
SEQRES 15 B 538 ASP ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL
SEQRES 16 B 538 THR ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY
SEQRES 17 B 538 MET HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG
SEQRES 18 B 538 ARG ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP
SEQRES 19 B 538 ALA SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL
SEQRES 20 B 538 GLU LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP
SEQRES 21 B 538 GLU GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN
SEQRES 22 B 538 GLU LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP
SEQRES 23 B 538 SER ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY
SEQRES 24 B 538 GLU PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER
SEQRES 25 B 538 GLY ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN
SEQRES 26 B 538 LYS ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO
SEQRES 27 B 538 GLY PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU
SEQRES 28 B 538 ASP PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA
SEQRES 29 B 538 ASN ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR
SEQRES 30 B 538 ASP TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP
SEQRES 31 B 538 GLY LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS
SEQRES 32 B 538 PRO LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY
SEQRES 33 B 538 ASN GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER
SEQRES 34 B 538 ASN LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY
SEQRES 35 B 538 TYR GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS
SEQRES 36 B 538 GLU LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG
SEQRES 37 B 538 ARG ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY
SEQRES 38 B 538 ASN PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO
SEQRES 39 B 538 LEU PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN
SEQRES 40 B 538 THR GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN
SEQRES 41 B 538 MET CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU
SEQRES 42 B 538 ASN ALA THR ALA CYS
HET DQ5 A 601 29
HET DQ5 A 602 29
HET NAG A 603 14
HET NAG A 604 14
HET CL A 605 1
HET DQ5 B 601 29
HET DQ5 B 602 29
HET NAG B 603 14
HET NAG B 604 14
HETNAM DQ5 2-[(~{E})-HYDROXYIMINOMETHYL]-6-[4-(1,2,3,4-
HETNAM 2 DQ5 TETRAHYDROACRIDIN-9-YLAMINO)BUTYL]PYRIDIN-3-OL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CL CHLORIDE ION
FORMUL 3 DQ5 4(C23 H26 N4 O2)
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 7 CL CL 1-
FORMUL 12 HOH *512(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 VAL A 150 LEU A 156 1 7
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 SER A 200 SER A 212 1 13
HELIX 9 AA9 PRO A 213 ARG A 216 5 4
HELIX 10 AB1 VAL A 238 ASN A 251 1 14
HELIX 11 AB2 SER A 258 LYS A 269 1 12
HELIX 12 AB3 LYS A 270 TRP A 279 1 10
HELIX 13 AB4 ASN A 280 LEU A 282 5 3
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 GLY A 415 1 16
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 THR A 535 1 10
HELIX 26 AC8 VAL B 40 ARG B 44 5 5
HELIX 27 AC9 PHE B 78 MET B 83 1 6
HELIX 28 AD1 LEU B 127 ASN B 131 5 5
HELIX 29 AD2 GLY B 132 GLU B 140 1 9
HELIX 30 AD3 VAL B 150 LEU B 156 1 7
HELIX 31 AD4 ASN B 167 ILE B 184 1 18
HELIX 32 AD5 GLN B 185 PHE B 187 5 3
HELIX 33 AD6 SER B 200 SER B 212 1 13
HELIX 34 AD7 SER B 212 ASP B 217 1 6
HELIX 35 AD8 VAL B 238 ASN B 251 1 14
HELIX 36 AD9 SER B 258 LYS B 269 1 12
HELIX 37 AE1 LYS B 270 GLU B 278 1 9
HELIX 38 AE2 TRP B 279 LEU B 282 5 4
HELIX 39 AE3 SER B 304 GLY B 312 1 9
HELIX 40 AE4 GLY B 328 ALA B 336 1 9
HELIX 41 AE5 SER B 348 VAL B 360 1 13
HELIX 42 AE6 ASN B 364 THR B 376 1 13
HELIX 43 AE7 ASN B 383 VAL B 400 1 18
HELIX 44 AE8 VAL B 400 LYS B 413 1 14
HELIX 45 AE9 PRO B 433 GLY B 437 5 5
HELIX 46 AF1 GLU B 443 PHE B 448 1 6
HELIX 47 AF2 GLY B 449 ASN B 457 5 9
HELIX 48 AF3 THR B 459 GLY B 480 1 22
HELIX 49 AF4 ARG B 517 GLN B 526 1 10
HELIX 50 AF5 GLN B 526 ALA B 534 1 9
SHEET 1 AA1 3 LEU A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 MET A 16 -1 O GLY A 13 N THR A 10
SHEET 3 AA1 3 VAL A 57 ASN A 59 1 O TRP A 58 N LYS A 14
SHEET 1 AA211 THR A 18 VAL A 22 0
SHEET 2 AA211 SER A 25 PRO A 34 -1 O ILE A 27 N VAL A 20
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 TRP A 114 O VAL A 144
SHEET 6 AA211 GLY A 189 GLU A 199 1 O THR A 195 N VAL A 111
SHEET 7 AA211 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
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 LEU A 505 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 VAL A 236 SER A 237 0
SHEET 2 AA3 2 VAL A 295 ILE A 296 1 O ILE A 296 N VAL A 236
SHEET 1 AA4 3 LEU B 7 THR B 10 0
SHEET 2 AA4 3 GLY B 13 MET B 16 -1 O VAL B 15 N VAL B 8
SHEET 3 AA4 3 VAL B 57 ASN B 59 1 O TRP B 58 N MET B 16
SHEET 1 AA511 THR B 18 VAL B 22 0
SHEET 2 AA511 SER B 25 PRO B 34 -1 O ILE B 27 N VAL B 20
SHEET 3 AA511 TYR B 96 VAL B 101 -1 O LEU B 97 N ILE B 33
SHEET 4 AA511 VAL B 142 SER B 145 -1 O LEU B 143 N TRP B 100
SHEET 5 AA511 THR B 109 ILE B 115 1 N TRP B 114 O VAL B 144
SHEET 6 AA511 GLY B 189 GLU B 199 1 O THR B 195 N VAL B 111
SHEET 7 AA511 ARG B 221 GLN B 225 1 O GLN B 225 N GLY B 198
SHEET 8 AA511 ILE B 319 ASN B 324 1 O LEU B 320 N ALA B 222
SHEET 9 AA511 THR B 418 PHE B 423 1 O PHE B 423 N VAL B 323
SHEET 10 AA511 LYS B 501 LEU B 505 1 O ILE B 503 N PHE B 422
SHEET 11 AA511 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SHEET 1 AA6 2 VAL B 236 SER B 237 0
SHEET 2 AA6 2 VAL B 295 ILE B 296 1 O ILE B 296 N VAL B 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
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.03
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.05
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.03
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.04
LINK ND2 ASN A 59 C1 NAG A 604 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN B 59 C1 NAG B 604 1555 1555 1.45
LINK ND2 ASN B 416 C1 NAG B 603 1555 1555 1.45
CISPEP 1 SER A 103 PRO A 104 0 8.84
CISPEP 2 SER B 103 PRO B 104 0 6.37
SITE 1 AC1 9 TYR A 70 TRP A 279 TYR A 334 GLY A 335
SITE 2 AC1 9 DQ5 A 602 HOH A 755 GLN B 185 PRO B 191
SITE 3 AC1 9 HOH B 918
SITE 1 AC2 16 TRP A 84 GLY A 118 TYR A 121 GLU A 199
SITE 2 AC2 16 SER A 286 ILE A 287 PHE A 288 ARG A 289
SITE 3 AC2 16 PHE A 290 PHE A 330 PHE A 331 TYR A 334
SITE 4 AC2 16 TRP A 432 HIS A 440 TYR A 442 DQ5 A 601
SITE 1 AC3 5 VAL A 246 LEU A 256 ASP A 259 HOH A 831
SITE 2 AC3 5 HOH A 909
SITE 1 AC4 9 GLN A 185 PRO A 191 TYR B 70 TRP B 279
SITE 2 AC4 9 TYR B 334 DQ5 B 602 HOH B 719 HOH B 777
SITE 3 AC4 9 HOH B 843
SITE 1 AC5 17 ASP B 72 TRP B 84 GLY B 118 TYR B 121
SITE 2 AC5 17 GLU B 199 PHE B 288 PHE B 290 PHE B 330
SITE 3 AC5 17 PHE B 331 TYR B 334 TRP B 432 ILE B 439
SITE 4 AC5 17 HIS B 440 TYR B 442 DQ5 B 601 HOH B 718
SITE 5 AC5 17 HOH B 831
SITE 1 AC6 2 ASN A 59 HOH A 804
SITE 1 AC7 2 ASN A 416 HOH A 720
SITE 1 AC8 3 ASN B 59 SER B 61 HOH B 828
SITE 1 AC9 4 ASN B 416 HOH B 715 HOH B 765 HOH B 830
CRYST1 91.276 106.240 150.456 90.00 90.00 90.00 P 21 21 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 0.010956 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009413 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006646 0.00000
TER 4250 THR A 535
TER 8503 THR B 535
MASTER 416 0 9 50 32 0 21 6 9173 2 188 84
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