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HEADER HYDROLASE 19-MAY-16 5K3D
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 - WT/APO -
TITLE 2 NO HALIDE
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 5K3D 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. 1.45 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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 96439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 4758
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 33.8711 - 4.5021 1.00 3112 175 0.1424 0.1357
REMARK 3 2 4.5021 - 3.5747 1.00 3107 151 0.1370 0.1715
REMARK 3 3 3.5747 - 3.1232 1.00 3075 170 0.1742 0.1908
REMARK 3 4 3.1232 - 2.8378 1.00 3094 146 0.1847 0.2337
REMARK 3 5 2.8378 - 2.6345 1.00 3079 138 0.1849 0.1986
REMARK 3 6 2.6345 - 2.4792 1.00 3075 146 0.1809 0.2176
REMARK 3 7 2.4792 - 2.3551 1.00 3067 152 0.1815 0.2260
REMARK 3 8 2.3551 - 2.2526 1.00 3056 170 0.1831 0.2073
REMARK 3 9 2.2526 - 2.1659 1.00 3037 183 0.1811 0.2231
REMARK 3 10 2.1659 - 2.0912 1.00 3033 154 0.1867 0.2187
REMARK 3 11 2.0912 - 2.0258 1.00 3057 172 0.1932 0.2275
REMARK 3 12 2.0258 - 1.9679 1.00 3075 146 0.1929 0.2291
REMARK 3 13 1.9679 - 1.9161 1.00 3042 163 0.1926 0.2355
REMARK 3 14 1.9161 - 1.8693 1.00 3061 163 0.1909 0.2482
REMARK 3 15 1.8693 - 1.8268 1.00 3045 152 0.1944 0.2256
REMARK 3 16 1.8268 - 1.7880 1.00 3110 120 0.1945 0.2692
REMARK 3 17 1.7880 - 1.7522 1.00 3053 152 0.1960 0.2557
REMARK 3 18 1.7522 - 1.7191 1.00 3065 167 0.2002 0.2266
REMARK 3 19 1.7191 - 1.6884 1.00 3028 159 0.1987 0.2550
REMARK 3 20 1.6884 - 1.6598 1.00 3037 158 0.1977 0.2224
REMARK 3 21 1.6598 - 1.6330 1.00 3042 159 0.2042 0.2706
REMARK 3 22 1.6330 - 1.6079 1.00 2994 181 0.2085 0.2304
REMARK 3 23 1.6079 - 1.5843 1.00 3080 175 0.2174 0.2346
REMARK 3 24 1.5843 - 1.5620 1.00 3049 147 0.2109 0.2699
REMARK 3 25 1.5620 - 1.5408 1.00 3062 145 0.2133 0.2355
REMARK 3 26 1.5408 - 1.5208 1.00 3031 181 0.2237 0.2514
REMARK 3 27 1.5208 - 1.5018 1.00 3032 151 0.2266 0.2557
REMARK 3 28 1.5018 - 1.4837 1.00 3031 167 0.2337 0.2693
REMARK 3 29 1.4837 - 1.4665 1.00 3070 150 0.2532 0.3096
REMARK 3 30 1.4665 - 1.4500 0.99 2982 165 0.2668 0.3032
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.21
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 : 0.010 4907
REMARK 3 ANGLE : 1.375 6701
REMARK 3 CHIRALITY : 0.057 678
REMARK 3 PLANARITY : 0.008 884
REMARK 3 DIHEDRAL : 13.550 1780
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 5K3D 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_1000221625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-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 : BRUKER AXS MICROSTAR
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS
REMARK 200 DATA SCALING SOFTWARE : PROTEUM PLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96439
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 33.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 49.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: 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 (%): 41.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350 19-22%, 200MM CALCIUM
REMARK 280 ACETATE, 100MM TRIS SO4 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 39.83850
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: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 ASP A 2
REMARK 465 SER A 251
REMARK 465 GLY A 252
REMARK 465 ILE A 253
REMARK 465 ALA A 254
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 ASP B 2
REMARK 465 ALA B 3
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 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 ARG A 296 CG CD NE CZ NH1 NH2
REMARK 470 THR B 259 OG1 CG2
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 405 O HOH A 669 2.13
REMARK 500 O HOH B 411 O HOH B 642 2.13
REMARK 500 O HOH A 518 O HOH A 560 2.14
REMARK 500 OE1 GLU B 235 O HOH B 401 2.17
REMARK 500 O HOH A 601 O HOH A 650 2.18
REMARK 500 NE ARG B 49 O HOH B 402 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 503 O HOH B 579 2647 2.16
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 PRO A 41 65.23 -101.94
REMARK 500 ASP A 110 -125.94 54.40
REMARK 500 SER A 123 59.84 -141.08
REMARK 500 ILE A 153 66.44 -119.64
REMARK 500 ASP A 173 64.34 -152.56
REMARK 500 TYR A 224 -97.53 -121.06
REMARK 500 PRO B 41 69.30 -100.59
REMARK 500 ASP B 110 -126.89 52.88
REMARK 500 ILE B 153 55.72 -117.52
REMARK 500 ASP B 173 73.64 -151.64
REMARK 500 TYR B 224 -93.99 -123.03
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 680 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 681 DISTANCE = 6.64 ANGSTROMS
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: 5K3C RELATED DB: PDB
REMARK 900 RELATED ID: 5K3F RELATED DB: PDB
REMARK 900 RELATED ID: 5K3E RELATED DB: PDB
DBREF 5K3D A 4 300 UNP Q6NAM1 DEHA_RHOPA 4 300
DBREF 5K3D B 4 300 UNP Q6NAM1 DEHA_RHOPA 4 300
SEQADV 5K3D ASP A 2 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3D ALA A 3 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3D ASP B 2 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3D ALA B 3 UNP Q6NAM1 EXPRESSION TAG
SEQRES 1 A 299 ASP ALA LEU ALA ASP LEU PHE PRO GLY PHE GLY SER GLU
SEQRES 2 A 299 TRP ILE ASN THR SER SER GLY ARG ILE PHE ALA ARG VAL
SEQRES 3 A 299 GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU HIS GLY PHE
SEQRES 4 A 299 PRO GLN THR HIS VAL MET TRP HIS ARG VAL ALA PRO LYS
SEQRES 5 A 299 LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA ASP LEU PRO
SEQRES 6 A 299 GLY TYR GLY TRP SER ASP MET PRO GLU SER ASP GLU GLN
SEQRES 7 A 299 HIS THR PRO TYR THR LYS ARG ALA MET ALA LYS GLN LEU
SEQRES 8 A 299 ILE GLU ALA MET GLU GLN LEU GLY HIS VAL HIS PHE ALA
SEQRES 9 A 299 LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL SER TYR ARG
SEQRES 10 A 299 LEU ALA LEU ASP SER PRO GLY ARG LEU SER LYS LEU ALA
SEQRES 11 A 299 VAL LEU ASP ILE LEU PRO THR TYR GLU TYR TRP GLN ARG
SEQRES 12 A 299 MET ASN ARG ALA TYR ALA LEU LYS ILE TYR HIS TRP SER
SEQRES 13 A 299 PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU ASN LEU LEU
SEQRES 14 A 299 GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA LYS LEU ALA
SEQRES 15 A 299 SER TRP THR ARG ALA GLY ASP LEU SER ALA PHE ASP PRO
SEQRES 16 A 299 ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE ALA ASP PRO
SEQRES 17 A 299 MET ARG ARG HIS VAL MET CYS GLU ASP TYR ARG ALA GLY
SEQRES 18 A 299 ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE ASP VAL GLU
SEQRES 19 A 299 ALA GLY ASN LYS ILE PRO VAL PRO MET LEU ALA LEU TRP
SEQRES 20 A 299 GLY ALA SER GLY ILE ALA GLN SER ALA ALA THR PRO LEU
SEQRES 21 A 299 ASP VAL TRP ARG LYS TRP ALA SER ASP VAL GLN GLY ALA
SEQRES 22 A 299 PRO ILE GLU SER GLY HIS PHE LEU PRO GLU GLU ALA PRO
SEQRES 23 A 299 ASP GLN THR ALA GLU ALA LEU VAL ARG PHE PHE SER ALA
SEQRES 1 B 299 ASP ALA LEU ALA ASP LEU PHE PRO GLY PHE GLY SER GLU
SEQRES 2 B 299 TRP ILE ASN THR SER SER GLY ARG ILE PHE ALA ARG VAL
SEQRES 3 B 299 GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU HIS GLY PHE
SEQRES 4 B 299 PRO GLN THR HIS VAL MET TRP HIS ARG VAL ALA PRO LYS
SEQRES 5 B 299 LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA ASP LEU PRO
SEQRES 6 B 299 GLY TYR GLY TRP SER ASP MET PRO GLU SER ASP GLU GLN
SEQRES 7 B 299 HIS THR PRO TYR THR LYS ARG ALA MET ALA LYS GLN LEU
SEQRES 8 B 299 ILE GLU ALA MET GLU GLN LEU GLY HIS VAL HIS PHE ALA
SEQRES 9 B 299 LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL SER TYR ARG
SEQRES 10 B 299 LEU ALA LEU ASP SER PRO GLY ARG LEU SER LYS LEU ALA
SEQRES 11 B 299 VAL LEU ASP ILE LEU PRO THR TYR GLU TYR TRP GLN ARG
SEQRES 12 B 299 MET ASN ARG ALA TYR ALA LEU LYS ILE TYR HIS TRP SER
SEQRES 13 B 299 PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU ASN LEU LEU
SEQRES 14 B 299 GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA LYS LEU ALA
SEQRES 15 B 299 SER TRP THR ARG ALA GLY ASP LEU SER ALA PHE ASP PRO
SEQRES 16 B 299 ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE ALA ASP PRO
SEQRES 17 B 299 MET ARG ARG HIS VAL MET CYS GLU ASP TYR ARG ALA GLY
SEQRES 18 B 299 ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE ASP VAL GLU
SEQRES 19 B 299 ALA GLY ASN LYS ILE PRO VAL PRO MET LEU ALA LEU TRP
SEQRES 20 B 299 GLY ALA SER GLY ILE ALA GLN SER ALA ALA THR PRO LEU
SEQRES 21 B 299 ASP VAL TRP ARG LYS TRP ALA SER ASP VAL GLN GLY ALA
SEQRES 22 B 299 PRO ILE GLU SER GLY HIS PHE LEU PRO GLU GLU ALA PRO
SEQRES 23 B 299 ASP GLN THR ALA GLU ALA LEU VAL ARG PHE PHE SER ALA
FORMUL 3 HOH *604(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 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 TRP 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 TRP 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 PRO B 260 LYS B 266 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 ILE A 23 N ILE A 16
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 TRP A 248 1 O LEU A 247 N VAL A 132
SHEET 8 AA1 8 VAL A 271 PRO A 275 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 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 VAL B 132
SHEET 8 AA2 8 VAL B 271 ILE B 276 1 O ILE B 276 N TRP B 248
LINK CE1BTYR A 141 CD1 ILE A 153 1555 1555 1.57
CISPEP 1 PHE A 40 PRO A 41 0 -1.35
CISPEP 2 ALA A 163 PRO A 164 0 3.35
CISPEP 3 PHE B 40 PRO B 41 0 -3.07
CISPEP 4 ALA B 163 PRO B 164 0 4.92
CRYST1 41.772 79.677 85.291 90.00 102.45 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 0.023939 0.000000 0.005285 0.00000
SCALE2 0.000000 0.012551 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012007 0.00000
TER 2370 SER A 299
TER 4738 SER B 299
MASTER 333 0 0 32 16 0 0 6 5191 2 2 46
END |