| content |
HEADER HYDROLASE 19-MAY-16 5K3C
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 - WT/5-
TITLE 2 FLUOROTRYPTOPHAN
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 (STRAIN ATCC BAA-98
SOURCE 3 / CGA009);
SOURCE 4 ORGANISM_TAXID: 258594;
SOURCE 5 STRAIN: ATCC BAA-98 / CGA009;
SOURCE 6 GENE: RPA1163;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HOMODIMER, HYDROLASE, DEHALOGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MEHRABI,T.H.KIM,S.R.PROSSER,E.F.PAI
REVDAT 1 01-FEB-17 5K3C 0
JRNL AUTH T.H.KIM,P.MEHRABI,Z.REN,A.SLJOKA,C.ING,A.BEZGINOV,L.YE,
JRNL AUTH 2 R.POMES,R.S.PROSSER,E.F.PAI
JRNL TITL THE ROLE OF DIMER ASYMMETRY AND PROTOMER DYNAMICS IN ENZYME
JRNL TITL 2 CATALYSIS.
JRNL REF SCIENCE V. 355 2017
JRNL REFN ESSN 1095-9203
JRNL PMID 28104837
JRNL DOI 10.1126/SCIENCE.AAG2355
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 77192
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3883
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 19.1394 - 4.6582 0.96 2667 138 0.1513 0.1724
REMARK 3 2 4.6582 - 3.7062 0.99 2740 141 0.1241 0.1527
REMARK 3 3 3.7062 - 3.2403 0.99 2713 136 0.1612 0.1914
REMARK 3 4 3.2403 - 2.9452 0.99 2725 139 0.1699 0.1800
REMARK 3 5 2.9452 - 2.7347 0.99 2690 171 0.1800 0.2299
REMARK 3 6 2.7347 - 2.5739 0.99 2683 143 0.1712 0.1881
REMARK 3 7 2.5739 - 2.4452 0.99 2689 141 0.1686 0.2250
REMARK 3 8 2.4452 - 2.3390 0.99 2682 152 0.1759 0.2222
REMARK 3 9 2.3390 - 2.2491 0.98 2678 150 0.1825 0.2191
REMARK 3 10 2.2491 - 2.1716 0.98 2663 136 0.1769 0.2550
REMARK 3 11 2.1716 - 2.1038 0.99 2635 156 0.1760 0.2334
REMARK 3 12 2.1038 - 2.0437 0.99 2695 160 0.1839 0.1888
REMARK 3 13 2.0437 - 1.9900 0.98 2608 151 0.1836 0.2226
REMARK 3 14 1.9900 - 1.9415 0.98 2690 139 0.1908 0.2445
REMARK 3 15 1.9415 - 1.8974 0.97 2645 127 0.1924 0.2345
REMARK 3 16 1.8974 - 1.8570 0.97 2645 133 0.1861 0.2300
REMARK 3 17 1.8570 - 1.8199 0.98 2640 130 0.1882 0.2326
REMARK 3 18 1.8199 - 1.7856 0.97 2706 115 0.1832 0.2223
REMARK 3 19 1.7856 - 1.7537 0.97 2593 140 0.1836 0.2199
REMARK 3 20 1.7537 - 1.7240 0.97 2645 125 0.1893 0.2242
REMARK 3 21 1.7240 - 1.6962 0.97 2626 134 0.1855 0.2408
REMARK 3 22 1.6962 - 1.6701 0.96 2611 126 0.1919 0.2791
REMARK 3 23 1.6701 - 1.6456 0.96 2616 161 0.1919 0.2467
REMARK 3 24 1.6456 - 1.6224 0.96 2604 131 0.1991 0.2419
REMARK 3 25 1.6224 - 1.6005 0.96 2602 132 0.1997 0.2517
REMARK 3 26 1.6005 - 1.5797 0.96 2586 140 0.2030 0.2478
REMARK 3 27 1.5797 - 1.5600 0.90 2419 137 0.2680 0.3018
REMARK 3 28 1.5600 - 1.5412 0.67 1813 99 0.3239 0.2847
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.39
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 : 0.013 4821
REMARK 3 ANGLE : 1.588 6581
REMARK 3 CHIRALITY : 0.062 668
REMARK 3 PLANARITY : 0.008 857
REMARK 3 DIHEDRAL : 13.416 1747
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 5K3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221624.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-D
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77192
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.541
REMARK 200 RESOLUTION RANGE LOW (A) : 19.138
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.02100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21400
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: 3R3U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350 19-22%, 200MM CALCIUM
REMARK 280 CHLORIDE, 100MM TRIS HCL PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 39.73000
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: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 ASP A 3
REMARK 465 GLN A 255
REMARK 465 SER A 256
REMARK 465 ALA A 257
REMARK 465 ALA A 258
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 ASP B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
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 300
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
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 GLU B 75 CG CD OE1 OE2
REMARK 470 SER B 251 OG
REMARK 470 THR B 259 OG1 CG2
REMARK 470 GLU B 292 CG CD OE1 OE2
REMARK 470 ARG B 296 CG CD NE CZ NH1 NH2
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 HOH A 503 O HOH A 559 2.15
REMARK 500 O HOH A 506 O HOH A 765 2.16
REMARK 500 O HOH A 519 O HOH A 776 2.18
REMARK 500 O HOH B 501 O HOH B 655 2.19
REMARK 500 O SER A 299 O HOH A 501 2.19
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 GLN A 42 -169.10 -121.36
REMARK 500 ASP A 110 -129.56 61.73
REMARK 500 TYR A 224 -96.98 -122.74
REMARK 500 PRO B 41 70.93 -102.70
REMARK 500 ASP B 110 -130.27 57.98
REMARK 500 ASN B 146 -168.05 -101.45
REMARK 500 ILE B 153 59.17 -116.74
REMARK 500 TYR B 224 -95.95 -119.30
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 850 DISTANCE = 5.81 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5K3B RELATED DB: PDB
REMARK 900 RELATED ID: 5K3A RELATED DB: PDB
REMARK 900 RELATED ID: 5K3D RELATED DB: PDB
REMARK 900 RELATED ID: 5K3F RELATED DB: PDB
REMARK 900 RELATED ID: 5K3E RELATED DB: PDB
DBREF 5K3C A 3 300 UNP Q6NAM1 DEHA_RHOPA 3 300
DBREF 5K3C B 3 300 UNP Q6NAM1 DEHA_RHOPA 3 300
SEQADV 5K3C GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C MET A 1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C PRO A 2 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C ALA A 301 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C PRO A 302 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C SER A 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C MET B 1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C PRO B 2 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C ALA B 301 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C PRO B 302 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3C 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 FTR 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 FTR 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 FTR 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 FTR GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 A 306 HIS FTR 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 FTR 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 FTR GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 A 306 THR PRO LEU ASP VAL FTR ARG LYS FTR 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 FTR 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 FTR 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 FTR 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 FTR GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 B 306 HIS FTR 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 FTR 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 FTR GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 B 306 THR PRO LEU ASP VAL FTR ARG LYS FTR 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
MODRES 5K3C FTR A 15 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 47 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 70 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 142 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 156 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 185 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 248 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 264 TRP MODIFIED RESIDUE
MODRES 5K3C FTR A 267 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 15 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 47 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 70 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 142 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 156 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 185 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 248 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 264 TRP MODIFIED RESIDUE
MODRES 5K3C FTR B 267 TRP MODIFIED RESIDUE
HET FTR A 15 15
HET FTR A 47 15
HET FTR A 70 15
HET FTR A 142 15
HET FTR A 156 15
HET FTR A 185 15
HET FTR A 248 15
HET FTR A 264 15
HET FTR A 267 15
HET FTR B 15 15
HET FTR B 47 15
HET FTR B 70 15
HET FTR B 142 15
HET FTR B 156 15
HET FTR B 185 15
HET FTR B 248 15
HET FTR B 264 15
HET FTR B 267 15
HET CL A 401 1
HET CL A 402 1
HET CL B 401 1
HETNAM FTR FLUOROTRYPTOPHANE
HETNAM CL CHLORIDE ION
FORMUL 1 FTR 18(C11 H11 F N2 O2)
FORMUL 3 CL 3(CL 1-)
FORMUL 6 HOH *573(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 MET A 145 1 9
HELIX 7 AA7 ASN A 146 ILE A 153 1 8
HELIX 8 AA8 TYR A 154 LEU A 159 1 6
HELIX 9 AA9 PRO A 164 GLY A 172 1 9
HELIX 10 AB1 ASP A 173 FTR A 185 1 13
HELIX 11 AB2 ASP A 195 ALA A 207 1 13
HELIX 12 AB3 ASP A 208 TYR A 224 1 17
HELIX 13 AB4 TYR A 224 GLY A 237 1 14
HELIX 14 AB5 PRO A 260 LYS A 266 1 7
HELIX 15 AB6 PHE A 281 ALA A 286 1 6
HELIX 16 AB7 ALA A 286 SER A 299 1 14
HELIX 17 AB8 THR B 43 HIS B 48 5 6
HELIX 18 AB9 VAL B 50 GLU B 56 1 7
HELIX 19 AC1 HIS B 80 TYR B 83 5 4
HELIX 20 AC2 THR B 84 LEU B 99 1 16
HELIX 21 AC3 ASP B 110 SER B 123 1 14
HELIX 22 AC4 PRO B 137 ARG B 144 1 8
HELIX 23 AC5 ASN B 146 ILE B 153 1 8
HELIX 24 AC6 TYR B 154 LEU B 159 1 6
HELIX 25 AC7 PRO B 164 GLY B 171 1 8
HELIX 26 AC8 ASP B 173 FTR B 185 1 13
HELIX 27 AC9 ASP B 195 ALA B 207 1 13
HELIX 28 AD1 ASP B 208 TYR B 224 1 17
HELIX 29 AD2 TYR B 224 GLY B 237 1 14
HELIX 30 AD3 THR B 259 ARG B 265 1 7
HELIX 31 AD4 PHE B 281 ALA B 286 1 6
HELIX 32 AD5 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 VAL A 27 N GLY A 12
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 107 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 PHE B 11 ILE B 16 0
SHEET 2 AA2 8 ILE B 23 GLY B 29 -1 O VAL B 27 N GLY B 12
SHEET 3 AA2 8 LYS B 59 ALA B 63 -1 O VAL B 60 N GLY B 28
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N LEU B 34 O LYS B 59
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 ALA B 131 N LEU B 106
SHEET 7 AA2 8 MET B 244 GLY B 249 1 O LEU B 245 N LEU B 130
SHEET 8 AA2 8 VAL B 271 ILE B 276 1 O ILE B 276 N FTR B 248
LINK C GLU A 14 N FTR A 15 1555 1555 1.33
LINK C FTR A 15 N ILE A 16 1555 1555 1.32
LINK C MET A 46 N FTR A 47 1555 1555 1.34
LINK C FTR A 47 N HIS A 48 1555 1555 1.33
LINK C GLY A 69 N FTR A 70 1555 1555 1.33
LINK C FTR A 70 N SER A 71 1555 1555 1.33
LINK C TYR A 141 N FTR A 142 1555 1555 1.32
LINK C FTR A 142 N GLN A 143 1555 1555 1.33
LINK C HIS A 155 N FTR A 156 1555 1555 1.34
LINK C FTR A 156 N SER A 157 1555 1555 1.34
LINK C SER A 184 N FTR A 185 1555 1555 1.32
LINK C FTR A 185 N THR A 186 1555 1555 1.34
LINK C LEU A 247 N FTR A 248 1555 1555 1.32
LINK C FTR A 248 N GLY A 249 1555 1555 1.32
LINK C VAL A 263 N FTR A 264 1555 1555 1.34
LINK C FTR A 264 N ARG A 265 1555 1555 1.34
LINK C LYS A 266 N FTR A 267 1555 1555 1.34
LINK C FTR A 267 N ALA A 268 1555 1555 1.33
LINK C GLU B 14 N FTR B 15 1555 1555 1.33
LINK C FTR B 15 N ILE B 16 1555 1555 1.33
LINK C MET B 46 N FTR B 47 1555 1555 1.34
LINK C FTR B 47 N HIS B 48 1555 1555 1.34
LINK C GLY B 69 N FTR B 70 1555 1555 1.33
LINK C FTR B 70 N SER B 71 1555 1555 1.32
LINK C ATYR B 141 N FTR B 142 1555 1555 1.33
LINK C BTYR B 141 N FTR B 142 1555 1555 1.34
LINK C FTR B 142 N GLN B 143 1555 1555 1.33
LINK C HIS B 155 N FTR B 156 1555 1555 1.34
LINK C FTR B 156 N SER B 157 1555 1555 1.32
LINK C SER B 184 N FTR B 185 1555 1555 1.33
LINK C FTR B 185 N THR B 186 1555 1555 1.34
LINK C LEU B 247 N FTR B 248 1555 1555 1.33
LINK C FTR B 248 N GLY B 249 1555 1555 1.33
LINK C VAL B 263 N FTR B 264 1555 1555 1.33
LINK C FTR B 264 N ARG B 265 1555 1555 1.33
LINK C LYS B 266 N FTR B 267 1555 1555 1.34
LINK C FTR B 267 N ALA B 268 1555 1555 1.32
CISPEP 1 PHE A 40 PRO A 41 0 -3.92
CISPEP 2 ALA A 163 PRO A 164 0 4.05
CISPEP 3 PHE B 40 PRO B 41 0 -3.33
CISPEP 4 ALA B 163 PRO B 164 0 5.44
SITE 1 AC1 3 ARG A 114 LEU A 136 HOH A 585
SITE 1 AC2 3 ASP A 110 ARG A 111 ARG A 114
SITE 1 AC3 3 ASP B 110 ARG B 111 ARG B 114
CRYST1 41.890 79.460 85.240 90.00 103.02 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 0.023872 0.000000 0.005518 0.00000
SCALE2 0.000000 0.012585 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012041 0.00000
TER 2355 SER A 299
TER 4666 SER B 299
MASTER 333 0 21 32 16 0 3 6 5193 2 307 48
END |