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HEADER HYDROLASE 17-JAN-19 6QI0
TITLE TIME RESOLVED STRUCTURAL ANALYSIS OF THE FULL TURNOVER OF AN ENZYME -
TITLE 2 9024 MS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 1076;
SOURCE 4 GENE: RPA1163;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TIME-RESOLVED, CATALYSIS, INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.C.SCHULZ,P.MEHRABI,E.F.PAI,D.MILLER
REVDAT 1 25-SEP-19 6QI0 0
JRNL AUTH P.MEHRABI,E.C.SCHULZ,R.DSOUZA,H.M.MULLER-WERKMEISTER,
JRNL AUTH 2 F.TELLKAMP,R.J.D.MILLER,E.F.PAI
JRNL TITL TIME-RESOLVED CRYSTALLOGRAPHY REVEALS ALLOSTERIC
JRNL TITL 2 COMMUNICATION ALIGNED WITH MOLECULAR BREATHING.
JRNL REF SCIENCE V. 365 1167 2019
JRNL REFN ESSN 1095-9203
JRNL PMID 31515393
JRNL DOI 10.1126/SCIENCE.AAW9904
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 53325
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 2634
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 19.9894 - 4.6068 1.00 2744 164 0.1819 0.1674
REMARK 3 2 4.6068 - 3.6639 1.00 2760 128 0.1510 0.1677
REMARK 3 3 3.6639 - 3.2029 1.00 2698 157 0.1535 0.1755
REMARK 3 4 3.2029 - 2.9110 1.00 2706 153 0.1605 0.1892
REMARK 3 5 2.9110 - 2.7029 1.00 2715 135 0.1646 0.1974
REMARK 3 6 2.7029 - 2.5439 1.00 2673 160 0.1669 0.2158
REMARK 3 7 2.5439 - 2.4167 1.00 2700 141 0.1591 0.1996
REMARK 3 8 2.4167 - 2.3117 1.00 2696 145 0.1548 0.2052
REMARK 3 9 2.3117 - 2.2228 1.00 2739 122 0.1610 0.2166
REMARK 3 10 2.2228 - 2.1462 1.00 2693 146 0.1604 0.1874
REMARK 3 11 2.1462 - 2.0792 1.00 2669 158 0.1686 0.2123
REMARK 3 12 2.0792 - 2.0198 1.00 2712 131 0.1718 0.2236
REMARK 3 13 2.0198 - 1.9667 1.00 2649 150 0.1732 0.2202
REMARK 3 14 1.9667 - 1.9187 1.00 2759 123 0.1780 0.2326
REMARK 3 15 1.9187 - 1.8751 1.00 2707 107 0.1826 0.2466
REMARK 3 16 1.8751 - 1.8352 1.00 2698 141 0.1911 0.2513
REMARK 3 17 1.8352 - 1.7986 1.00 2689 130 0.2163 0.2882
REMARK 3 18 1.7986 - 1.7646 1.00 2736 139 0.2493 0.3234
REMARK 3 19 1.7646 - 1.7331 0.74 1948 104 0.3124 0.3305
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.220
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 : 0.009 4857
REMARK 3 ANGLE : 1.085 6616
REMARK 3 CHIRALITY : 0.054 677
REMARK 3 PLANARITY : 0.007 869
REMARK 3 DIHEDRAL : 15.060 3938
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 6QI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1200013242.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0089
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53325
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 81.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 54.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
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 (%): 36.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20 % (W/V)) PEG3350, 200 MM CACL2,
REMARK 280 AND 100 MM TRIS-HCL PH 8.5, BATCH MODE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.28500
REMARK 290 SMTRY3 2 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: 2600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 300
REMARK 465 ALA A 301
REMARK 465 PRO A 302
REMARK 465 GLY A 303
REMARK 465 SER A 304
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 252
REMARK 465 ILE B 253
REMARK 465 ALA B 254
REMARK 465 GLN B 255
REMARK 465 SER B 256
REMARK 465 ALA B 257
REMARK 465 ALA B 258
REMARK 465 ALA B 300
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
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 41 65.22 -107.51
REMARK 500 ASP A 110 -130.17 60.05
REMARK 500 ILE A 153 51.52 -115.85
REMARK 500 ASP A 173 73.43 -153.66
REMARK 500 TYR A 224 -91.49 -119.81
REMARK 500 ALA A 258 -174.35 -173.84
REMARK 500 GLU A 277 98.17 -65.22
REMARK 500 GLU A 277 97.18 -63.98
REMARK 500 PRO B 41 65.60 -103.27
REMARK 500 GLN B 42 -168.49 -121.44
REMARK 500 ASP B 110 -127.21 57.12
REMARK 500 ASP B 173 69.45 -168.65
REMARK 500 TYR B 224 -97.27 -119.03
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 B 695 DISTANCE = 6.31 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 B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 173 OD2
REMARK 620 2 HOH A 620 O 108.6
REMARK 620 3 HOH A 584 O 88.7 80.1
REMARK 620 4 ALA A 236 O 70.4 49.1 50.2
REMARK 620 5 HOH A 635 O 101.9 110.5 161.1 148.3
REMARK 620 6 HOH A 554 O 79.9 162.6 85.1 125.0 81.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402
DBREF 6QI0 A 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
DBREF 6QI0 B 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
SEQADV 6QI0 GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6QI0 HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6QI0 GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6QI0 SER A 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6QI0 GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6QI0 HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6QI0 GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 6QI0 SER B 304 UNP Q6NAM1 EXPRESSION TAG
SEQRES 1 A 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 A 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 A 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 A 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 A 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 A 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 A 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 A 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 A 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 A 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 A 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 A 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 A 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 A 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 A 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 A 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 A 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 A 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 A 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 A 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 A 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 A 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 A 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 A 306 PHE SER ALA ALA PRO GLY SER
SEQRES 1 B 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 B 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 B 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 B 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 B 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 B 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 B 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 B 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 B 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 B 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 B 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 B 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 B 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 B 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 B 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 B 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 B 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 B 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 B 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 B 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 B 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 B 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 B 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 B 306 PHE SER ALA ALA PRO GLY SER
HET FAH A 401 5
HET GOA B 401 5
HET CA B 402 1
HETNAM FAH FLUOROACETIC ACID
HETNAM GOA GLYCOLIC ACID
HETNAM CA CALCIUM ION
HETSYN GOA HYDROXYACETIC ACID; HYDROXYETHANOIC ACID
FORMUL 3 FAH C2 H3 F O2
FORMUL 4 GOA C2 H4 O3
FORMUL 5 CA CA 2+
FORMUL 6 HOH *395(H2 O)
HELIX 1 AA1 THR A 43 HIS A 48 5 6
HELIX 2 AA2 VAL A 50 GLU A 56 1 7
HELIX 3 AA3 HIS A 80 TYR A 83 5 4
HELIX 4 AA4 THR A 84 LEU A 99 1 16
HELIX 5 AA5 ASP A 110 SER A 123 1 14
HELIX 6 AA6 PRO A 137 ARG A 144 1 8
HELIX 7 AA7 ASN A 146 ILE A 153 1 8
HELIX 8 AA8 ILE A 153 LEU A 159 1 7
HELIX 9 AA9 PRO A 164 GLY A 172 1 9
HELIX 10 AB1 ASP A 173 TRP A 185 1 13
HELIX 11 AB2 ASP A 195 ASP A 208 1 14
HELIX 12 AB3 ASP A 208 TYR A 224 1 17
HELIX 13 AB4 TYR A 224 ALA A 236 1 13
HELIX 14 AB5 ILE A 253 ALA A 258 1 6
HELIX 15 AB6 THR A 259 ALA A 268 1 10
HELIX 16 AB7 PHE A 281 ALA A 286 1 6
HELIX 17 AB8 ALA A 286 SER A 299 1 14
HELIX 18 AB9 THR B 43 HIS B 48 5 6
HELIX 19 AC1 VAL B 50 ALA B 55 1 6
HELIX 20 AC2 HIS B 80 TYR B 83 5 4
HELIX 21 AC3 THR B 84 LEU B 99 1 16
HELIX 22 AC4 ASP B 110 SER B 123 1 14
HELIX 23 AC5 PRO B 137 ARG B 144 1 8
HELIX 24 AC6 ASN B 146 ILE B 153 1 8
HELIX 25 AC7 ILE B 153 LEU B 159 1 7
HELIX 26 AC8 PRO B 164 GLY B 171 1 8
HELIX 27 AC9 ASP B 173 TRP B 185 1 13
HELIX 28 AD1 ASP B 195 ALA B 207 1 13
HELIX 29 AD2 ASP B 208 TYR B 224 1 17
HELIX 30 AD3 TYR B 224 GLY B 237 1 14
HELIX 31 AD4 PRO B 260 ALA B 268 1 9
HELIX 32 AD5 PHE B 281 ALA B 286 1 6
HELIX 33 AD6 ALA B 286 SER B 299 1 14
SHEET 1 AA1 8 GLY A 12 ILE A 16 0
SHEET 2 AA1 8 ILE A 23 GLY A 29 -1 O ALA A 25 N GLU A 14
SHEET 3 AA1 8 LYS A 59 ALA A 63 -1 O VAL A 62 N ARG A 26
SHEET 4 AA1 8 PRO A 33 LEU A 37 1 N LEU A 34 O ILE A 61
SHEET 5 AA1 8 PHE A 104 HIS A 109 1 O ALA A 105 N LEU A 35
SHEET 6 AA1 8 LEU A 127 LEU A 133 1 O ALA A 131 N LEU A 106
SHEET 7 AA1 8 MET A 244 GLY A 249 1 O LEU A 245 N VAL A 132
SHEET 8 AA1 8 VAL A 271 ILE A 276 1 O GLN A 272 N ALA A 246
SHEET 1 AA2 8 GLY B 12 ILE B 16 0
SHEET 2 AA2 8 ILE B 23 GLY B 28 -1 O ALA B 25 N GLU B 14
SHEET 3 AA2 8 LYS B 59 ALA B 63 -1 O VAL B 62 N ARG B 26
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N LEU B 36 O ILE B 61
SHEET 5 AA2 8 PHE B 104 HIS B 109 1 O ALA B 105 N LEU B 35
SHEET 6 AA2 8 LEU B 127 LEU B 133 1 O LEU B 133 N GLY B 108
SHEET 7 AA2 8 MET B 244 GLY B 249 1 O LEU B 245 N VAL B 132
SHEET 8 AA2 8 VAL B 271 ILE B 276 1 O ILE B 276 N TRP B 248
LINK OD2 ASP B 173 CA CA B 402 1555 1555 2.33
LINK CA CA B 402 O HOH A 620 1555 1555 2.37
LINK CA CA B 402 O HOH A 584 1555 1555 2.50
LINK O ALA A 236 CA CA B 402 1555 2557 2.39
LINK CA CA B 402 O HOH A 635 1555 2547 2.52
LINK CA CA B 402 O HOH A 554 1555 2547 2.56
CISPEP 1 PHE A 40 PRO A 41 0 2.25
CISPEP 2 ALA A 163 PRO A 164 0 2.50
CISPEP 3 PHE B 40 PRO B 41 0 -2.47
CISPEP 4 ALA B 163 PRO B 164 0 2.57
SITE 1 AC1 8 ASP A 110 ARG A 111 ARG A 114 ILE A 135
SITE 2 AC1 8 HIS A 155 TRP A 156 TYR A 219 HOH A 508
SITE 1 AC2 6 ASP B 110 ARG B 111 ARG B 114 HIS B 155
SITE 2 AC2 6 TRP B 156 TYR B 219
SITE 1 AC3 3 HOH A 584 HOH A 620 ASP B 173
CRYST1 41.350 78.570 83.540 90.00 102.84 90.00 P 1 21 1 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 0.024184 0.000000 0.005512 0.00000
SCALE2 0.000000 0.012728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012277 0.00000
TER 2378 SER A 299
TER 4694 SER B 299
MASTER 305 0 3 33 16 0 5 6 5066 2 14 48
END |