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HEADER HYDROLASE 11-JUL-18 6H19
TITLE CRYSTAL STRUCTURE OF ETHYL-PARAOXON INHIBITED RECOMBINANT HUMAN BILE
TITLE 2 SALT ACTIVATED LIPASE (AGED FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE SALT-ACTIVATED LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BAL,BILE SALT-STIMULATED LIPASE,BSSL,BUCELIPASE,CARBOXYL
COMPND 5 ESTER LIPASE,CHOLESTEROL ESTERASE,PANCREATIC LYSOPHOSPHOLIPASE,STEROL
COMPND 6 ESTERASE;
COMPND 7 EC: 3.1.1.13,3.1.1.3;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: SPT = SERINE RESIDUE INHIBITED BY ETHYLPARAOXON IN ITS
COMPND 11 AGED FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CEL, BAL;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS LIPASE, ALPHA-BETA HYDROLASE., PARAOXON INHIBITION, AGED FORM,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TOUVREY,X.BRAZZOLOTTO,F.NACHON
REVDAT 1 27-MAR-19 6H19 0
JRNL AUTH C.TOUVREY,C.COURAGEUX,V.GUILLON,R.TERREUX,F.NACHON,
JRNL AUTH 2 X.BRAZZOLOTTO
JRNL TITL X-RAY STRUCTURES OF HUMAN BILE-SALT ACTIVATED LIPASE
JRNL TITL 2 CONJUGATED TO NERVE AGENTS SURROGATES.
JRNL REF TOXICOLOGY V. 411 15 2019
JRNL REFN ISSN 1879-3185
JRNL PMID 30359675
JRNL DOI 10.1016/J.TOX.2018.10.015
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 49021
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2406
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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 : 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 6H19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200010888.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-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 : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49065
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 44.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11960
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.2100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.370
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 (%): 50.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CACODYLATE, ZINC ACETATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 28.06000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.07500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.90500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.07500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.06000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.90500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -314.0 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 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 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 GLU A -5
REMARK 465 ASN A -4
REMARK 465 LEU A -3
REMARK 465 TYR A -2
REMARK 465 PHE A -1
REMARK 465 SER A 422
REMARK 465 ARG A 423
REMARK 465 MET A 424
REMARK 465 PRO A 425
REMARK 465 VAL A 426
REMARK 465 TYR A 427
REMARK 465 PRO A 428
REMARK 465 LYS A 429
REMARK 465 TRP A 430
REMARK 465 VAL A 431
REMARK 465 GLY A 432
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 GLN A 0 CG CD OE1 NE2
REMARK 470 SER A 1 OG
REMARK 470 SDP A 194 C41 C42
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 OD1 ASP A 299 O HOH A 701 2.16
REMARK 500 O HOH A 850 O HOH A 898 2.17
REMARK 500 OE2 GLU A 500 O HOH A 702 2.18
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 SDP A 194 -117.11 58.28
REMARK 500 ASP A 262 117.55 -36.71
REMARK 500 ASP A 294 -85.73 -138.38
REMARK 500 PHE A 393 -58.56 -134.78
REMARK 500 LYS A 409 -86.58 -103.17
REMARK 500 SER A 496 45.93 37.69
REMARK 500 LEU A 514 109.92 -58.01
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 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 48 NE2
REMARK 620 2 ACT A 613 O 102.9
REMARK 620 3 HOH A 722 O 95.2 98.5
REMARK 620 4 ACT A 613 OXT 91.2 63.1 161.5
REMARK 620 5 HOH A 749 O 173.6 81.6 88.6 86.8
REMARK 620 6 HOH A 865 O 92.7 153.2 101.7 95.3 81.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 603 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 77 OD1
REMARK 620 2 GLU A 78 OE2 115.6
REMARK 620 3 ASP A 476 OD2 43.8 74.6
REMARK 620 4 HOH A 708 O 108.4 104.3 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 607 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 97 OD1
REMARK 620 2 ASP A 97 OD2 53.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 604 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 115 NE2
REMARK 620 2 ACT A 614 O 115.5
REMARK 620 3 HOH A 878 O 90.6 114.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 618 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 126 OD1
REMARK 620 2 HOH A 728 O 53.7
REMARK 620 3 HOH A 887 O 96.7 114.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 168 NE2
REMARK 620 2 ACT A 612 O 91.2
REMARK 620 3 ACT A 612 OXT 127.2 58.6
REMARK 620 4 GLU A 342 OE1 35.1 65.8 120.9
REMARK 620 5 HOH A 720 O 111.6 89.6 110.4 86.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 610 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 193 OE2
REMARK 620 2 ASP A 437 OD1 106.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 605 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 420 NE2
REMARK 620 2 HIS A 435 NE2 124.9
REMARK 620 3 ASP A 457 OD1 91.4 109.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 606 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 487 NE2
REMARK 620 2 GLU A 489 OE1 102.9
REMARK 620 3 ACT A 611 O 136.5 110.7
REMARK 620 4 ACT A 611 OXT 82.8 113.4 59.2
REMARK 620 5 ASP A 79 OD2 65.4 86.7 89.4 35.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 608 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACT A 617 O
REMARK 620 2 HOH A 705 O 95.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 618
DBREF 6H19 A 2 533 UNP P19835 CEL_HUMAN 22 553
SEQADV 6H19 HIS A -13 UNP P19835 EXPRESSION TAG
SEQADV 6H19 HIS A -12 UNP P19835 EXPRESSION TAG
SEQADV 6H19 HIS A -11 UNP P19835 EXPRESSION TAG
SEQADV 6H19 HIS A -10 UNP P19835 EXPRESSION TAG
SEQADV 6H19 HIS A -9 UNP P19835 EXPRESSION TAG
SEQADV 6H19 HIS A -8 UNP P19835 EXPRESSION TAG
SEQADV 6H19 HIS A -7 UNP P19835 EXPRESSION TAG
SEQADV 6H19 HIS A -6 UNP P19835 EXPRESSION TAG
SEQADV 6H19 GLU A -5 UNP P19835 EXPRESSION TAG
SEQADV 6H19 ASN A -4 UNP P19835 EXPRESSION TAG
SEQADV 6H19 LEU A -3 UNP P19835 EXPRESSION TAG
SEQADV 6H19 TYR A -2 UNP P19835 EXPRESSION TAG
SEQADV 6H19 PHE A -1 UNP P19835 EXPRESSION TAG
SEQADV 6H19 GLN A 0 UNP P19835 EXPRESSION TAG
SEQADV 6H19 SER A 1 UNP P19835 EXPRESSION TAG
SEQADV 6H19 ASP A 186 UNP P19835 ASN 206 ENGINEERED MUTATION
SEQADV 6H19 ASP A 298 UNP P19835 ALA 318 ENGINEERED MUTATION
SEQRES 1 A 547 HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 A 547 GLN SER LYS LEU GLY ALA VAL TYR THR GLU GLY GLY PHE
SEQRES 3 A 547 VAL GLU GLY VAL ASN LYS LYS LEU GLY LEU LEU GLY ASP
SEQRES 4 A 547 SER VAL ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA PRO
SEQRES 5 A 547 THR LYS ALA LEU GLU ASN PRO GLN PRO HIS PRO GLY TRP
SEQRES 6 A 547 GLN GLY THR LEU LYS ALA LYS ASN PHE LYS LYS ARG CYS
SEQRES 7 A 547 LEU GLN ALA THR ILE THR GLN ASP SER THR TYR GLY ASP
SEQRES 8 A 547 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY
SEQRES 9 A 547 ARG LYS GLN VAL SER ARG ASP LEU PRO VAL MET ILE TRP
SEQRES 10 A 547 ILE TYR GLY GLY ALA PHE LEU MET GLY SER GLY HIS GLY
SEQRES 11 A 547 ALA ASN PHE LEU ASN ASN TYR LEU TYR ASP GLY GLU GLU
SEQRES 12 A 547 ILE ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN
SEQRES 13 A 547 TYR ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP
SEQRES 14 A 547 ALA ASN LEU PRO GLY ASN TYR GLY LEU ARG ASP GLN HIS
SEQRES 15 A 547 MET ALA ILE ALA TRP VAL LYS ARG ASN ILE ALA ALA PHE
SEQRES 16 A 547 GLY GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SDP
SEQRES 17 A 547 ALA GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO
SEQRES 18 A 547 TYR ASN LYS GLY LEU ILE ARG ARG ALA ILE SER GLN SER
SEQRES 19 A 547 GLY VAL ALA LEU SER PRO TRP VAL ILE GLN LYS ASN PRO
SEQRES 20 A 547 LEU PHE TRP ALA LYS LYS VAL ALA GLU LYS VAL GLY CYS
SEQRES 21 A 547 PRO VAL GLY ASP ALA ALA ARG MET ALA GLN CYS LEU LYS
SEQRES 22 A 547 VAL THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS VAL
SEQRES 23 A 547 PRO LEU ALA GLY LEU GLU TYR PRO MET LEU HIS TYR VAL
SEQRES 24 A 547 GLY PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP
SEQRES 25 A 547 ASP PRO ILE ASN LEU TYR ALA ASN ALA ALA ASP ILE ASP
SEQRES 26 A 547 TYR ILE ALA GLY THR ASN ASN MET ASP GLY HIS ILE PHE
SEQRES 27 A 547 ALA SER ILE ASP MET PRO ALA ILE ASN LYS GLY ASN LYS
SEQRES 28 A 547 LYS VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLU
SEQRES 29 A 547 PHE THR ILE THR LYS GLY LEU ARG GLY ALA LYS THR THR
SEQRES 30 A 547 PHE ASP VAL TYR THR GLU SER TRP ALA GLN ASP PRO SER
SEQRES 31 A 547 GLN GLU ASN LYS LYS LYS THR VAL VAL ASP PHE GLU THR
SEQRES 32 A 547 ASP VAL LEU PHE LEU VAL PRO THR GLU ILE ALA LEU ALA
SEQRES 33 A 547 GLN HIS ARG ALA ASN ALA LYS SER ALA LYS THR TYR ALA
SEQRES 34 A 547 TYR LEU PHE SER HIS PRO SER ARG MET PRO VAL TYR PRO
SEQRES 35 A 547 LYS TRP VAL GLY ALA ASP HIS ALA ASP ASP ILE GLN TYR
SEQRES 36 A 547 VAL PHE GLY LYS PRO PHE ALA THR PRO THR GLY TYR ARG
SEQRES 37 A 547 PRO GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR
SEQRES 38 A 547 TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN MET GLY
SEQRES 39 A 547 ASP SER ALA VAL PRO THR HIS TRP GLU PRO TYR THR THR
SEQRES 40 A 547 GLU ASN SER GLY TYR LEU GLU ILE THR LYS LYS MET GLY
SEQRES 41 A 547 SER SER SER MET LYS ARG SER LEU ARG THR ASN PHE LEU
SEQRES 42 A 547 ARG TYR TRP THR LEU THR TYR LEU ALA LEU PRO THR VAL
SEQRES 43 A 547 THR
MODRES 6H19 SDP A 194 SER MODIFIED RESIDUE
HET SDP A 194 12
HET ZN A 601 1
HET ZN A 602 1
HET ZN A 603 1
HET ZN A 604 1
HET ZN A 605 1
HET ZN A 606 1
HET ZN A 607 1
HET ZN A 608 1
HET ZN A 609 1
HET ZN A 610 1
HET ACT A 611 4
HET ACT A 612 4
HET ACT A 613 4
HET ACT A 614 4
HET ACT A 615 4
HET ACT A 616 4
HET ACT A 617 4
HET NA A 618 1
HETNAM SDP 2-AMINO-3-(DIETHOXY-PHOSPHORYLOXY)-PROPIONIC ACID
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
FORMUL 1 SDP C7 H16 N O6 P
FORMUL 2 ZN 10(ZN 2+)
FORMUL 12 ACT 7(C2 H3 O2 1-)
FORMUL 19 NA NA 1+
FORMUL 20 HOH *202(H2 O)
HELIX 1 AA1 GLY A 127 ASN A 135 1 9
HELIX 2 AA2 VAL A 145 LEU A 151 1 7
HELIX 3 AA3 ASN A 161 ILE A 178 1 18
HELIX 4 AA4 ALA A 179 PHE A 181 5 3
HELIX 5 AA5 SDP A 194 SER A 206 1 13
HELIX 6 AA6 PRO A 207 LYS A 210 5 4
HELIX 7 AA7 ASN A 232 GLY A 245 1 14
HELIX 8 AA8 ASP A 250 VAL A 260 1 11
HELIX 9 AA9 ASP A 262 ALA A 269 1 8
HELIX 10 AB1 PRO A 280 VAL A 285 5 6
HELIX 11 AB2 ASP A 299 ALA A 308 5 10
HELIX 12 AB3 GLY A 321 MET A 329 1 9
HELIX 13 AB4 PRO A 330 ASN A 333 5 4
HELIX 14 AB5 THR A 340 THR A 352 1 13
HELIX 15 AB6 LYS A 355 GLU A 369 1 15
HELIX 16 AB7 SER A 370 ALA A 372 5 3
HELIX 17 AB8 SER A 376 PHE A 393 1 18
HELIX 18 AB9 PHE A 393 ASN A 407 1 15
HELIX 19 AC1 ASP A 438 PHE A 443 1 6
HELIX 20 AC2 GLY A 444 THR A 449 1 6
HELIX 21 AC3 PRO A 450 TYR A 453 5 4
HELIX 22 AC4 ARG A 454 GLY A 475 1 22
HELIX 23 AC5 GLY A 506 SER A 508 5 3
HELIX 24 AC6 ARG A 515 LEU A 524 1 10
SHEET 1 AA1 3 VAL A 6 THR A 8 0
SHEET 2 AA1 3 GLY A 11 GLU A 14 -1 O VAL A 13 N VAL A 6
SHEET 3 AA1 3 THR A 54 LYS A 56 1 O LEU A 55 N PHE A 12
SHEET 1 AA211 VAL A 16 LYS A 19 0
SHEET 2 AA211 SER A 26 PRO A 34 -1 O ILE A 29 N VAL A 16
SHEET 3 AA211 TYR A 82 GLN A 89 -1 O LEU A 83 N ILE A 33
SHEET 4 AA211 ILE A 137 PHE A 141 -1 O THR A 140 N ASN A 84
SHEET 5 AA211 LEU A 98 ILE A 104 1 N MET A 101 O ILE A 137
SHEET 6 AA211 GLY A 183 GLU A 193 1 O THR A 189 N VAL A 100
SHEET 7 AA211 ARG A 215 GLN A 219 1 O GLN A 219 N GLY A 192
SHEET 8 AA211 ASP A 311 ASN A 317 1 O ILE A 313 N SER A 218
SHEET 9 AA211 THR A 413 PHE A 418 1 O PHE A 418 N THR A 316
SHEET 10 AA211 GLY A 497 ILE A 501 1 O ILE A 501 N LEU A 417
SHEET 11 AA211 MET A 510 ARG A 512 -1 O LYS A 511 N TYR A 498
SHEET 1 AA3 2 GLN A 66 ALA A 67 0
SHEET 2 AA3 2 THR A 74 TYR A 75 -1 O TYR A 75 N GLN A 66
SSBOND 1 CYS A 64 CYS A 80 1555 1555 2.04
SSBOND 2 CYS A 246 CYS A 257 1555 1555 2.06
LINK NE2 HIS A 48 ZN ZN A 601 1555 1555 2.14
LINK OD1 ASP A 77 ZN ZN A 603 1555 1555 2.00
LINK OE2 GLU A 78 ZN ZN A 603 1555 1555 1.98
LINK OD1 ASP A 97 ZN ZN A 607 1555 1555 2.57
LINK OD2 ASP A 97 ZN ZN A 607 1555 1555 2.28
LINK NE2 HIS A 115 ZN ZN A 604 1555 1555 2.17
LINK OD1 ASP A 126 NA NA A 618 1555 1555 2.75
LINK NE2 HIS A 168 ZN ZN A 602 1555 1555 2.07
LINK C GLU A 193 N SDP A 194 1555 1555 1.33
LINK OE2 GLU A 193 ZN ZN A 610 1555 1555 1.94
LINK C SDP A 194 N ALA A 195 1555 1555 1.34
LINK OE1 GLU A 350 ZN ZN A 609 1555 1555 2.10
LINK NE2 HIS A 420 ZN ZN A 605 1555 1555 2.49
LINK NE2 HIS A 435 ZN ZN A 605 1555 1555 2.21
LINK OD1 ASP A 437 ZN ZN A 610 1555 1555 2.26
LINK OD1 ASP A 457 ZN ZN A 605 1555 1555 1.96
LINK NE2 HIS A 487 ZN ZN A 606 1555 1555 2.11
LINK OE1 GLU A 489 ZN ZN A 606 1555 1555 2.02
LINK ZN ZN A 601 O ACT A 613 1555 1555 2.09
LINK ZN ZN A 601 O HOH A 722 1555 1555 2.17
LINK ZN ZN A 601 OXT ACT A 613 1555 1555 2.24
LINK ZN ZN A 601 O HOH A 749 1555 1555 2.24
LINK ZN ZN A 601 O HOH A 865 1555 1555 1.99
LINK ZN ZN A 602 O ACT A 612 1555 1555 2.56
LINK ZN ZN A 602 OXT ACT A 612 1555 1555 2.00
LINK ZN ZN A 604 O ACT A 614 1555 1555 2.49
LINK ZN ZN A 604 O HOH A 878 1555 1555 2.30
LINK ZN ZN A 606 O ACT A 611 1555 1555 1.96
LINK ZN ZN A 606 OXT ACT A 611 1555 1555 2.52
LINK ZN ZN A 608 O ACT A 617 1555 1555 2.67
LINK ZN ZN A 608 O HOH A 705 1555 1555 2.39
LINK NA NA A 618 O HOH A 728 1555 1555 2.95
LINK NA NA A 618 O HOH A 887 1555 1555 2.87
LINK OD2 ASP A 79 ZN ZN A 606 1555 3555 2.03
LINK OE1 GLU A 342 ZN ZN A 602 1555 2554 1.94
LINK OD2 ASP A 476 ZN ZN A 603 1555 3545 1.96
LINK ZN ZN A 602 O HOH A 720 1555 2555 1.91
LINK ZN ZN A 603 O HOH A 708 1555 3555 2.00
CISPEP 1 HIS A 420 PRO A 421 0 -7.29
SITE 1 AC1 5 HIS A 48 ACT A 613 HOH A 722 HOH A 749
SITE 2 AC1 5 HOH A 865
SITE 1 AC2 4 HIS A 168 GLU A 342 ACT A 612 HOH A 720
SITE 1 AC3 4 ASP A 77 GLU A 78 ASP A 476 HOH A 708
SITE 1 AC4 4 HIS A 115 ACT A 614 ACT A 615 HOH A 878
SITE 1 AC5 4 HIS A 420 HIS A 435 TYR A 441 ASP A 457
SITE 1 AC6 4 ASP A 79 HIS A 487 GLU A 489 ACT A 611
SITE 1 AC7 1 ASP A 97
SITE 1 AC8 3 HIS A 283 ACT A 617 HOH A 705
SITE 1 AC9 2 TYR A 279 GLU A 350
SITE 1 AD1 3 GLU A 193 ASP A 437 ACT A 616
SITE 1 AD2 7 ASP A 77 ASP A 79 HIS A 487 GLU A 489
SITE 2 AD2 7 PRO A 490 ZN A 606 HOH A 708
SITE 1 AD3 7 HIS A 168 TYR A 208 GLU A 341 GLU A 342
SITE 2 AD3 7 ZN A 602 HOH A 771 HOH A 773
SITE 1 AD4 4 HIS A 48 TYR A 82 ZN A 601 HOH A 749
SITE 1 AD5 3 PHE A 60 ZN A 604 ACT A 615
SITE 1 AD6 4 ARG A 63 TYR A 75 ZN A 604 ACT A 614
SITE 1 AD7 6 SER A 220 ASP A 320 PHE A 324 PHE A 393
SITE 2 AD7 6 ASP A 437 ZN A 610
SITE 1 AD8 3 HIS A 283 ZN A 608 HOH A 705
SITE 1 AD9 5 LYS A 18 ASP A 126 GLU A 128 HOH A 728
SITE 2 AD9 5 HOH A 887
CRYST1 56.120 97.810 110.150 90.00 90.00 90.00 P 21 21 21 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 0.017819 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010224 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009079 0.00000
TER 4110 THR A 533
MASTER 429 0 19 24 16 0 23 6 4311 1 81 43
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