6h0t-pdb | HEADER HYDROLASE 10-JUL-18 6H0T
TITLE CRYSTAL STRUCTURE OF NATIVE RECOMBINANT HUMAN BILE SALT ACTIVATED
TITLE 2 LIPASE
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: CRYSTALS WITH UNCLEAVED TAGGED ENZYME
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., HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TOUVREY,X.BRAZZOLOTTO,F.NACHON
REVDAT 1 27-MAR-19 6H0T 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. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 49846
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 2389
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 44.6200 - 4.8800 0.99 2969 152 0.1786 0.1988
REMARK 3 2 4.8800 - 3.8800 0.99 2849 152 0.1602 0.1910
REMARK 3 3 3.8800 - 3.3900 0.99 2816 154 0.1872 0.2389
REMARK 3 4 3.3900 - 3.0800 0.99 2801 132 0.2178 0.2467
REMARK 3 5 3.0800 - 2.8600 1.00 2812 156 0.2353 0.2608
REMARK 3 6 2.8600 - 2.6900 1.00 2809 124 0.2301 0.2755
REMARK 3 7 2.6900 - 2.5500 1.00 2773 143 0.2260 0.2685
REMARK 3 8 2.5500 - 2.4400 1.00 2784 133 0.2226 0.2725
REMARK 3 9 2.4400 - 2.3500 1.00 2799 128 0.2284 0.2991
REMARK 3 10 2.3500 - 2.2700 1.00 2767 126 0.2305 0.2908
REMARK 3 11 2.2700 - 2.2000 1.00 2781 138 0.2391 0.2521
REMARK 3 12 2.2000 - 2.1300 1.00 2746 145 0.2457 0.2994
REMARK 3 13 2.1300 - 2.0800 1.00 2752 150 0.2609 0.2905
REMARK 3 14 2.0800 - 2.0300 0.99 2759 134 0.2907 0.3353
REMARK 3 15 2.0300 - 1.9800 0.99 2749 155 0.3310 0.4056
REMARK 3 16 1.9800 - 1.9400 0.99 2743 137 0.3437 0.3983
REMARK 3 17 1.9400 - 1.9000 0.99 2748 130 0.3901 0.4283
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) : 0.254
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.562
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.12
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 4146
REMARK 3 ANGLE : 0.848 5635
REMARK 3 CHIRALITY : 0.055 610
REMARK 3 PLANARITY : 0.006 725
REMARK 3 DIHEDRAL : 6.000 2434
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 6H0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200010857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-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 : ID23-1
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49920
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 39.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08457
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0700
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) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 1.23100
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: 1F6W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
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 29.13700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.82000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.83800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.82000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.13700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.83800
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: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -243.0 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 GLN A 0
REMARK 465 MET A 111
REMARK 465 GLY A 112
REMARK 465 SER A 113
REMARK 465 GLY A 114
REMARK 465 HIS A 115
REMARK 465 GLY A 116
REMARK 465 ALA A 117
REMARK 465 ASN A 118
REMARK 465 PHE A 119
REMARK 465 LEU A 120
REMARK 465 ASN A 121
REMARK 465 ASN A 122
REMARK 465 VAL A 272
REMARK 465 PRO A 273
REMARK 465 LEU A 274
REMARK 465 ALA A 275
REMARK 465 GLY A 276
REMARK 465 LEU A 277
REMARK 465 GLU A 278
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 SER A 1 OG
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 O VAL A 285 O HOH A 701 2.16
REMARK 500 OE2 GLU A 193 O HOH A 702 2.19
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 176 NE - CZ - NH2 ANGL. DEV. = -4.3 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 THR A 68 -170.98 -63.88
REMARK 500 GLN A 71 18.95 57.58
REMARK 500 LYS A 92 -86.40 -86.13
REMARK 500 LEU A 158 81.26 -152.07
REMARK 500 SER A 194 -120.43 60.66
REMARK 500 ASP A 294 -81.82 -138.15
REMARK 500 MET A 329 79.50 -155.65
REMARK 500 ASN A 333 34.66 -97.48
REMARK 500 LYS A 334 104.68 -170.58
REMARK 500 PHE A 393 -56.32 -132.70
REMARK 500 LYS A 409 -83.48 -107.34
REMARK 500 PRO A 428 8.39 -66.32
REMARK 500 TRP A 430 41.58 -80.11
REMARK 500 LEU A 524 -64.05 -106.37
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 605 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 48 NE2
REMARK 620 2 HOH A 798 O 92.5
REMARK 620 3 ACT A 611 OXT 84.6 97.9
REMARK 620 4 HOH A 730 O 168.6 77.1 92.1
REMARK 620 5 HOH A 716 O 98.2 105.9 155.8 89.3
REMARK 620 6 ACT A 611 O 97.1 157.8 63.3 91.2 92.6
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 OD2
REMARK 620 2 GLU A 78 OE1 75.8
REMARK 620 3 GLU A 78 OE2 115.5 54.2
REMARK 620 4 ASP A 476 OD2 43.9 64.7 76.7
REMARK 620 N 1 2 3
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 ASP A 97 OD1
REMARK 620 2 ASP A 97 OD2 51.5
REMARK 620 N 1
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 168 NE2
REMARK 620 2 ACT A 610 OXT 120.5
REMARK 620 3 GLU A 342 OE2 37.3 113.1
REMARK 620 N 1 2
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 HIS A 322 ND1
REMARK 620 2 ASP A 434 OD2 84.1
REMARK 620 3 ACT A 612 O 125.0 129.4
REMARK 620 4 ACT A 612 OXT 94.3 87.0 54.2
REMARK 620 5 HOH A 805 O 90.5 104.2 114.5 168.3
REMARK 620 N 1 2 3 4
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 487 NE2
REMARK 620 2 GLU A 489 OE1 102.4
REMARK 620 3 ACT A 609 O 142.3 103.0
REMARK 620 4 ACT A 609 OXT 86.4 115.5 57.6
REMARK 620 5 ASP A 79 OD2 64.8 89.0 88.3 37.9
REMARK 620 N 1 2 3 4
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 ACT A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT 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 GOL A 613
DBREF 6H0T A 2 533 UNP P19835 CEL_HUMAN 22 553
SEQADV 6H0T HIS A -13 UNP P19835 EXPRESSION TAG
SEQADV 6H0T HIS A -12 UNP P19835 EXPRESSION TAG
SEQADV 6H0T HIS A -11 UNP P19835 EXPRESSION TAG
SEQADV 6H0T HIS A -10 UNP P19835 EXPRESSION TAG
SEQADV 6H0T HIS A -9 UNP P19835 EXPRESSION TAG
SEQADV 6H0T HIS A -8 UNP P19835 EXPRESSION TAG
SEQADV 6H0T HIS A -7 UNP P19835 EXPRESSION TAG
SEQADV 6H0T HIS A -6 UNP P19835 EXPRESSION TAG
SEQADV 6H0T GLU A -5 UNP P19835 EXPRESSION TAG
SEQADV 6H0T ASN A -4 UNP P19835 EXPRESSION TAG
SEQADV 6H0T LEU A -3 UNP P19835 EXPRESSION TAG
SEQADV 6H0T TYR A -2 UNP P19835 EXPRESSION TAG
SEQADV 6H0T PHE A -1 UNP P19835 EXPRESSION TAG
SEQADV 6H0T GLN A 0 UNP P19835 EXPRESSION TAG
SEQADV 6H0T SER A 1 UNP P19835 EXPRESSION TAG
SEQADV 6H0T ASP A 186 UNP P19835 ASN 206 ENGINEERED MUTATION
SEQADV 6H0T 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 SER
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
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 ACT A 609 4
HET ACT A 610 4
HET ACT A 611 4
HET ACT A 612 4
HET GOL A 613 6
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN 8(ZN 2+)
FORMUL 10 ACT 4(C2 H3 O2 1-)
FORMUL 14 GOL C3 H8 O3
FORMUL 15 HOH *112(H2 O)
HELIX 1 AA1 GLY A 127 ASN A 135 1 9
HELIX 2 AA2 GLY A 146 LEU A 151 1 6
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 SER 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 LYS A 334 5 5
HELIX 14 AB5 THR A 340 THR A 352 1 13
HELIX 15 AB6 LYS A 355 THR A 368 1 14
HELIX 16 AB7 GLU A 369 ALA A 372 5 4
HELIX 17 AB8 SER A 376 PHE A 393 1 18
HELIX 18 AB9 PHE A 393 ALA A 408 1 16
HELIX 19 AC1 ASP A 437 PHE A 443 1 7
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
HELIX 25 AC7 LEU A 524 LEU A 529 1 6
SHEET 1 AA1 3 ALA A 5 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 VAL A 87 N ASP A 28
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 2.05
SSBOND 2 CYS A 246 CYS A 257 1555 1555 2.05
LINK NE2 HIS A 48 ZN ZN A 605 1555 1555 2.15
LINK OD2 ASP A 77 ZN ZN A 603 1555 1555 2.03
LINK OE1 GLU A 78 ZN ZN A 603 1555 1555 2.67
LINK OE2 GLU A 78 ZN ZN A 603 1555 1555 1.84
LINK OD1 ASP A 97 ZN ZN A 606 1555 1555 2.66
LINK OD2 ASP A 97 ZN ZN A 606 1555 1555 2.41
LINK NE2 HIS A 168 ZN ZN A 601 1555 1555 2.02
LINK ND1 HIS A 322 ZN ZN A 607 1555 1555 2.35
LINK OD2 ASP A 328 ZN ZN A 604 1555 1555 1.82
LINK OD2 ASP A 434 ZN ZN A 607 1555 1555 2.23
LINK NE2 HIS A 487 ZN ZN A 602 1555 1555 2.04
LINK OE1 GLU A 489 ZN ZN A 602 1555 1555 1.94
LINK ZN ZN A 601 OXT ACT A 610 1555 1555 2.09
LINK ZN ZN A 602 O ACT A 609 1555 1555 2.24
LINK ZN ZN A 602 OXT ACT A 609 1555 1555 2.40
LINK ZN ZN A 605 O HOH A 798 1555 1555 2.02
LINK ZN ZN A 605 OXT ACT A 611 1555 1555 2.37
LINK ZN ZN A 605 O HOH A 730 1555 1555 2.12
LINK ZN ZN A 605 O HOH A 716 1555 1555 2.13
LINK ZN ZN A 605 O ACT A 611 1555 1555 1.85
LINK ZN ZN A 607 O ACT A 612 1555 1555 2.54
LINK ZN ZN A 607 OXT ACT A 612 1555 1555 2.45
LINK ZN ZN A 607 O HOH A 805 1555 1555 2.31
LINK OD2 ASP A 79 ZN ZN A 602 1555 3645 2.04
LINK OE2 GLU A 342 ZN ZN A 601 1555 2554 2.02
LINK OD2 ASP A 476 ZN ZN A 603 1555 3655 1.97
SITE 1 AC1 3 HIS A 168 GLU A 342 ACT A 610
SITE 1 AC2 4 ASP A 79 HIS A 487 GLU A 489 ACT A 609
SITE 1 AC3 3 ASP A 77 GLU A 78 ASP A 476
SITE 1 AC4 4 MET A 281 ASP A 328 PHE A 351 GLU A 388
SITE 1 AC5 5 HIS A 48 ACT A 611 HOH A 716 HOH A 730
SITE 2 AC5 5 HOH A 798
SITE 1 AC6 1 ASP A 97
SITE 1 AC7 4 HIS A 322 ASP A 434 ACT A 612 HOH A 805
SITE 1 AC8 6 GLY A 107 ALA A 108 PHE A 109 LEU A 110
SITE 2 AC8 6 SER A 194 ALA A 195
SITE 1 AC9 6 ASP A 77 ASP A 79 HIS A 487 GLU A 489
SITE 2 AC9 6 PRO A 490 ZN A 602
SITE 1 AD1 6 HIS A 168 TYR A 208 GLU A 341 GLU A 342
SITE 2 AD1 6 ZN A 601 HOH A 703
SITE 1 AD2 5 HIS A 48 TYR A 82 ZN A 605 HOH A 716
SITE 2 AD2 5 HOH A 730
SITE 1 AD3 4 HIS A 322 ILE A 323 ASP A 434 ZN A 607
SITE 1 AD4 9 GLY A 315 THR A 316 LEU A 394 THR A 397
SITE 2 AD4 9 GLU A 398 LEU A 401 TYR A 416 TYR A 498
SITE 3 AD4 9 LEU A 514
CRYST1 58.274 97.676 109.640 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 0.017160 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009121 0.00000
TER 4020 THR A 533
MASTER 428 0 13 25 16 0 20 6 4161 1 51 43
END
|