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HEADER HYDROLASE 10-JUN-20 6ZCC
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HOB (HALOTAG7-BASED
TITLE 2 OLIGONUCLEOTIDE BINDER) LABELED WITH A CHLOROALKANE-
TITLE 3 TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 (SYNTHETIC) FLUOROPHORE, TETRAMETHYLRHODAMINE, OLIGONUCLEOTIDE
KEYWDS 3 BINDER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
REVDAT 1 21-APR-21 6ZCC 0
JRNL AUTH M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HOB
JRNL TITL 2 (HALOTAG7-BASED OLIGONUCLEOTIDE BINDER) LABELED WITH A
JRNL TITL 3 CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 38697
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1934
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 43.5300 - 3.6600 0.95 2908 152 0.1526 0.1587
REMARK 3 2 3.6600 - 2.9000 1.00 2904 153 0.1668 0.1987
REMARK 3 3 2.9000 - 2.5400 1.00 2875 152 0.1959 0.2546
REMARK 3 4 2.5400 - 2.3000 1.00 2853 150 0.2021 0.2469
REMARK 3 5 2.3000 - 2.1400 1.00 2846 150 0.2027 0.2395
REMARK 3 6 2.1400 - 2.0100 1.00 2827 148 0.2078 0.2851
REMARK 3 7 2.0100 - 1.9100 1.00 2841 150 0.2229 0.2595
REMARK 3 8 1.9100 - 1.8300 0.99 2809 148 0.2382 0.2925
REMARK 3 9 1.8300 - 1.7600 0.99 2806 148 0.2363 0.2959
REMARK 3 10 1.7600 - 1.7000 0.98 2770 145 0.2464 0.3183
REMARK 3 11 1.7000 - 1.6500 0.92 2589 137 0.2568 0.2799
REMARK 3 12 1.6500 - 1.6000 0.86 2423 127 0.2732 0.3457
REMARK 3 13 1.6000 - 1.5600 0.76 2152 113 0.3124 0.3906
REMARK 3 14 1.5600 - 1.5200 0.42 1160 61 0.3822 0.4412
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.195
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.428
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 2479
REMARK 3 ANGLE : 1.014 3385
REMARK 3 CHIRALITY : 0.058 351
REMARK 3 PLANARITY : 0.008 473
REMARK 3 DIHEDRAL : 6.111 2046
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 6ZCC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1292106998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-19
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99984
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38699
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : 5.910
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.38
REMARK 200 R MERGE FOR SHELL (I) : 0.24100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.390
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: 6Y7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 20% (M/V) PEG
REMARK 280 3350, 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 26.10500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.42500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.38500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.42500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.10500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.38500
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: 450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 GLU A 294
REMARK 465 ILE A 295
REMARK 465 SER A 296
REMARK 465 GLY A 297
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 PRO A 9 58.66 -90.74
REMARK 500 ASP A 31 102.46 -58.31
REMARK 500 PRO A 42 42.94 -107.80
REMARK 500 GLU A 98 -101.87 -121.67
REMARK 500 ASP A 106 -130.13 57.24
REMARK 500 LYS A 156 -48.68 70.85
REMARK 500 VAL A 245 -67.53 -135.10
REMARK 500 LEU A 271 -96.61 -116.88
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 712 DISTANCE = 6.20 ANGSTROMS
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 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 19 O
REMARK 620 2 HOH A 401 O 84.7
REMARK 620 3 HOH A 413 O 86.1 122.1
REMARK 620 4 HOH A 440 O 83.0 155.0 78.7
REMARK 620 5 HOH A 501 O 130.4 101.3 126.8 71.1
REMARK 620 6 HOH A 502 O 82.9 70.9 162.2 86.1 54.5
REMARK 620 7 HOH A 638 O 157.5 86.5 81.1 112.2 71.7 113.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 153 O
REMARK 620 2 HOH A 419 O 86.4
REMARK 620 3 HOH A 488 O 71.1 83.4
REMARK 620 4 HOH A 578 O 70.8 150.4 105.6
REMARK 620 5 HOH A 649 O 101.1 85.7 167.0 80.8
REMARK 620 6 HOH A 699 O 164.8 78.5 104.6 124.2 80.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 306 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 181 O
REMARK 620 2 GLU A 224 OE1 57.5
REMARK 620 3 ASP A 227 OD2 59.4 4.3
REMARK 620 4 HOH A 458 O 96.3 87.5 91.1
REMARK 620 5 HOH A 467 O 83.1 131.8 135.7 68.9
REMARK 620 6 HOH A 611 O 82.9 118.4 116.0 146.8 78.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 227 OD1
REMARK 620 2 HOH A 515 O 71.7
REMARK 620 3 HOH A 547 O 79.2 104.2
REMARK 620 4 HOH A 566 O 71.1 132.3 97.0
REMARK 620 5 HOH A 654 O 118.9 56.9 83.4 169.8
REMARK 620 6 HOH A 655 O 137.0 148.8 76.3 77.6 92.7
REMARK 620 7 HOH A 680 O 125.1 95.5 153.1 82.6 92.4 77.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OEH A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6Y7A RELATED DB: PDB
REMARK 900 RELATED ID: 6Y7B RELATED DB: PDB
DBREF 6ZCC A 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 6ZCC GLY A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZCC VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6ZCC THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6ZCC GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6ZCC PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6ZCC MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6ZCC PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6ZCC LYS A 143 UNP P0A3G3 GLU 143 ENGINEERED MUTATION
SEQADV 6ZCC LYS A 147 UNP P0A3G3 GLU 147 ENGINEERED MUTATION
SEQADV 6ZCC LYS A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6ZCC LYS A 156 UNP P0A3G3 ASP 156 ENGINEERED MUTATION
SEQADV 6ZCC LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6ZCC VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6ZCC THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6ZCC MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6ZCC GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6ZCC ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6ZCC GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6ZCC ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6ZCC LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6ZCC ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6ZCC ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6ZCC LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6ZCC SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6ZCC THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6ZCC GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZCC ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZCC SER A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZCC GLY A 297 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 295 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 A 295 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 A 295 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 A 295 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 A 295 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 A 295 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 A 295 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 A 295 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 A 295 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 A 295 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 A 295 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO LYS PHE ALA
SEQRES 12 A 295 ARG LYS THR PHE GLN ALA PHE ARG THR LYS LYS VAL GLY
SEQRES 13 A 295 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 A 295 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 A 295 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 A 295 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 A 295 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 A 295 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 A 295 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 A 295 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 A 295 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 A 295 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 A 295 TRP LEU SER THR LEU GLU ILE SER GLY
HET OEH A 301 44
HET ACT A 302 4
HET CA A 303 1
HET CA A 304 1
HET CA A 305 1
HET CA A 306 1
HETNAM OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)
HETNAM 2 OEH ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)
HETNAM 3 OEH XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM
HETNAM ACT ACETATE ION
HETNAM CA CALCIUM ION
FORMUL 2 OEH C35 H43 CL N3 O6 1+
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 CA 4(CA 2+)
FORMUL 8 HOH *312(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 PHE A 144 5 3
HELIX 7 AA7 ALA A 145 ARG A 153 1 9
HELIX 8 AA8 LYS A 156 ILE A 163 1 8
HELIX 9 AA9 ASN A 166 GLY A 171 1 6
HELIX 10 AB1 LEU A 173 VAL A 177 5 5
HELIX 11 AB2 THR A 182 GLU A 191 1 10
HELIX 12 AB3 PRO A 192 LEU A 194 5 3
HELIX 13 AB4 ASN A 195 ASP A 198 5 4
HELIX 14 AB5 ARG A 199 LEU A 209 1 11
HELIX 15 AB6 PRO A 215 SER A 232 1 18
HELIX 16 AB7 PRO A 248 LEU A 259 1 12
HELIX 17 AB8 LEU A 273 ASN A 278 1 6
HELIX 18 AB9 ASN A 278 THR A 292 1 15
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O VAL A 265 N LEU A 238
LINK OD2 ASP A 106 C20 OEH A 301 1555 1555 1.38
LINK O GLY A 19 CA CA A 303 1555 1555 2.22
LINK O ARG A 153 CA CA A 304 1555 1555 2.41
LINK O LEU A 181 CA CA A 306 1555 1555 2.50
LINK OE1 GLU A 224 CA CA A 306 1555 2555 2.53
LINK OD1 ASP A 227 CA CA A 305 1555 1555 2.48
LINK OD2 ASP A 227 CA CA A 306 1555 2555 2.49
LINK CA CA A 303 O HOH A 401 1555 4445 2.26
LINK CA CA A 303 O HOH A 413 1555 1555 2.45
LINK CA CA A 303 O HOH A 440 1555 4545 2.42
LINK CA CA A 303 O HOH A 501 1555 4545 2.16
LINK CA CA A 303 O HOH A 502 1555 4445 2.96
LINK CA CA A 303 O HOH A 638 1555 4445 2.45
LINK CA CA A 304 O HOH A 419 1555 1555 2.38
LINK CA CA A 304 O HOH A 488 1555 1555 2.30
LINK CA CA A 304 O HOH A 578 1555 1555 2.69
LINK CA CA A 304 O HOH A 649 1555 1555 2.43
LINK CA CA A 304 O HOH A 699 1555 1555 2.46
LINK CA CA A 305 O HOH A 515 1555 2555 2.34
LINK CA CA A 305 O HOH A 547 1555 1555 2.27
LINK CA CA A 305 O HOH A 566 1555 1555 2.58
LINK CA CA A 305 O HOH A 654 1555 2555 2.28
LINK CA CA A 305 O HOH A 655 1555 1555 2.44
LINK CA CA A 305 O HOH A 680 1555 1555 2.44
LINK CA CA A 306 O HOH A 458 1555 1555 2.81
LINK CA CA A 306 O HOH A 467 1555 1555 2.99
LINK CA CA A 306 O HOH A 611 1555 2554 2.44
CISPEP 1 ASN A 41 PRO A 42 0 3.40
CISPEP 2 GLU A 214 PRO A 215 0 -4.90
CISPEP 3 THR A 242 PRO A 243 0 5.83
SITE 1 AC1 20 ASP A 106 PRO A 120 ALA A 145 THR A 148
SITE 2 AC1 20 PHE A 149 VAL A 167 GLU A 170 GLY A 171
SITE 3 AC1 20 THR A 172 MET A 175 GLU A 224 TRP A 228
SITE 4 AC1 20 GLN A 231 SER A 232 PRO A 233 ASN A 272
SITE 5 AC1 20 ACT A 302 HOH A 431 HOH A 479 HOH A 603
SITE 1 AC2 8 ASN A 41 TRP A 107 PHE A 149 PHE A 168
SITE 2 AC2 8 PHE A 205 PRO A 206 LEU A 209 OEH A 301
SITE 1 AC3 8 GLY A 19 ASP A 31 HOH A 401 HOH A 413
SITE 2 AC3 8 HOH A 440 HOH A 501 HOH A 502 HOH A 638
SITE 1 AC4 6 ARG A 153 HOH A 419 HOH A 488 HOH A 578
SITE 2 AC4 6 HOH A 649 HOH A 699
SITE 1 AC5 7 ASP A 227 HOH A 515 HOH A 547 HOH A 566
SITE 2 AC5 7 HOH A 654 HOH A 655 HOH A 680
SITE 1 AC6 6 LEU A 181 GLU A 224 ASP A 227 HOH A 458
SITE 2 AC6 6 HOH A 467 HOH A 611
CRYST1 52.210 64.770 78.850 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 0.019153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015439 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012682 0.00000
TER 2349 LEU A 293
MASTER 333 0 6 18 8 0 15 6 2699 1 71 23
END |