| content |
HEADER HYDROLASE 30-AUG-16 5T4T
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 -
TITLE 2 ASP110ASN - APO NO HALIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: B, A;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 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 5T4T 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. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 76737
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170
REMARK 3 FREE R VALUE TEST SET COUNT : 3966
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 82.8278 - 4.5889 0.98 2848 170 0.1433 0.1444
REMARK 3 2 4.5889 - 3.6424 0.98 2853 132 0.1235 0.1540
REMARK 3 3 3.6424 - 3.1819 0.97 2773 149 0.1429 0.1714
REMARK 3 4 3.1819 - 2.8910 0.96 2771 125 0.1539 0.1870
REMARK 3 5 2.8910 - 2.6838 0.96 2727 155 0.1636 0.1888
REMARK 3 6 2.6838 - 2.5255 0.95 2723 151 0.1639 0.2023
REMARK 3 7 2.5255 - 2.3990 0.95 2714 132 0.1590 0.2166
REMARK 3 8 2.3990 - 2.2946 0.95 2673 176 0.1615 0.1909
REMARK 3 9 2.2946 - 2.2062 0.95 2674 165 0.1638 0.1919
REMARK 3 10 2.2062 - 2.1301 0.93 2659 145 0.1622 0.1918
REMARK 3 11 2.1301 - 2.0635 0.94 2688 146 0.1716 0.2094
REMARK 3 12 2.0635 - 2.0045 0.94 2632 157 0.1713 0.2329
REMARK 3 13 2.0045 - 1.9517 0.93 2636 157 0.1776 0.2309
REMARK 3 14 1.9517 - 1.9041 0.93 2625 136 0.1748 0.2067
REMARK 3 15 1.9041 - 1.8608 0.92 2630 130 0.1816 0.2330
REMARK 3 16 1.8608 - 1.8212 0.93 2608 166 0.1820 0.2137
REMARK 3 17 1.8212 - 1.7848 0.90 2597 125 0.1853 0.2312
REMARK 3 18 1.7848 - 1.7511 0.93 2626 149 0.1936 0.2524
REMARK 3 19 1.7511 - 1.7198 0.91 2569 148 0.1980 0.2286
REMARK 3 20 1.7198 - 1.6907 0.91 2570 165 0.2030 0.2552
REMARK 3 21 1.6907 - 1.6634 0.91 2607 123 0.2048 0.2457
REMARK 3 22 1.6634 - 1.6378 0.90 2547 133 0.2046 0.2708
REMARK 3 23 1.6378 - 1.6137 0.91 2580 135 0.2138 0.3112
REMARK 3 24 1.6137 - 1.5910 0.89 2558 128 0.2238 0.2492
REMARK 3 25 1.5910 - 1.5695 0.90 2521 140 0.2252 0.2699
REMARK 3 26 1.5695 - 1.5491 0.89 2501 136 0.2340 0.2682
REMARK 3 27 1.5491 - 1.5297 0.80 2302 120 0.2504 0.3246
REMARK 3 28 1.5297 - 1.5113 0.55 1559 72 0.2394 0.2895
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.810
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 : 0.011 4894
REMARK 3 ANGLE : 1.148 6669
REMARK 3 CHIRALITY : 0.064 682
REMARK 3 PLANARITY : 0.009 878
REMARK 3 DIHEDRAL : 22.847 2858
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 5T4T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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-E DW
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 : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76737
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 82.704
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.500
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 (%): 38.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-H2SO4 PH 8.5, 200 MM
REMARK 280 CALCIUM ACETATE AND 19-22% PEG3350, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 295K
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 39.42500
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: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 300
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
REMARK 465 GLY A -1
REMARK 465 ALA A 301
REMARK 465 PRO A 302
REMARK 465 GLY A 303
REMARK 465 SER A 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 ARG B 57 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 296 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 3 CG OD1 OD2
REMARK 470 LYS A 53 CG CD CE NZ
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 728 O HOH A 752 2.17
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 501 O HOH A 545 1455 2.16
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 B 220 NE - CZ - NH2 ANGL. DEV. = 3.1 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 PRO B 41 65.31 -100.38
REMARK 500 ASN B 110 -132.56 59.15
REMARK 500 ILE B 153 57.30 -112.61
REMARK 500 ASP B 173 71.21 -150.56
REMARK 500 TYR B 224 -91.07 -123.94
REMARK 500 ALA B 286 59.80 -140.03
REMARK 500 PRO A 41 63.46 -100.88
REMARK 500 ASN A 110 -131.36 57.02
REMARK 500 ASP A 173 70.91 -151.97
REMARK 500 TYR A 224 -97.58 -124.78
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 798 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B 799 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 800 DISTANCE = 7.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
DBREF 5T4T B 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
DBREF 5T4T A 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
SEQADV 5T4T GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5T4T HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5T4T ASN B 110 UNP Q6NAM1 ASP 110 ENGINEERED MUTATION
SEQADV 5T4T GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5T4T SER B 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5T4T GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5T4T HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5T4T ASN A 110 UNP Q6NAM1 ASP 110 ENGINEERED MUTATION
SEQADV 5T4T GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5T4T SER A 304 UNP Q6NAM1 EXPRESSION TAG
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 ASN 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
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 ASN 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
HET ACT B 401 4
HET ACT B 402 4
HET ACT A 401 4
HET ACT A 402 4
HETNAM ACT ACETATE ION
FORMUL 3 ACT 4(C2 H3 O2 1-)
FORMUL 7 HOH *659(H2 O)
HELIX 1 AA1 THR B 43 HIS B 48 5 6
HELIX 2 AA2 VAL B 50 GLU B 56 1 7
HELIX 3 AA3 HIS B 80 TYR B 83 5 4
HELIX 4 AA4 THR B 84 LEU B 99 1 16
HELIX 5 AA5 ASN B 110 SER B 123 1 14
HELIX 6 AA6 PRO B 137 ARG B 144 1 8
HELIX 7 AA7 ASN B 146 ILE B 153 1 8
HELIX 8 AA8 TYR B 154 LEU B 159 1 6
HELIX 9 AA9 PRO B 164 GLY B 171 1 8
HELIX 10 AB1 ASP B 173 TRP B 185 1 13
HELIX 11 AB2 ASP B 195 ASP B 208 1 14
HELIX 12 AB3 ASP B 208 TYR B 224 1 17
HELIX 13 AB4 TYR B 224 ALA B 236 1 13
HELIX 14 AB5 THR B 259 ALA B 268 1 10
HELIX 15 AB6 PHE B 281 ALA B 286 1 6
HELIX 16 AB7 ALA B 286 SER B 299 1 14
HELIX 17 AB8 THR A 43 HIS A 48 5 6
HELIX 18 AB9 VAL A 50 GLU A 56 1 7
HELIX 19 AC1 HIS A 80 TYR A 83 5 4
HELIX 20 AC2 THR A 84 LEU A 99 1 16
HELIX 21 AC3 ASN A 110 SER A 123 1 14
HELIX 22 AC4 PRO A 137 ARG A 144 1 8
HELIX 23 AC5 ASN A 146 ILE A 153 1 8
HELIX 24 AC6 TYR A 154 ALA A 160 1 7
HELIX 25 AC7 PRO A 164 GLY A 171 1 8
HELIX 26 AC8 ASP A 173 TRP A 185 1 13
HELIX 27 AC9 ASP A 195 ALA A 207 1 13
HELIX 28 AD1 ASP A 208 TYR A 224 1 17
HELIX 29 AD2 TYR A 224 ALA A 236 1 13
HELIX 30 AD3 THR A 259 ALA A 268 1 10
HELIX 31 AD4 PHE A 281 ALA A 286 1 6
HELIX 32 AD5 ALA A 286 ALA A 300 1 15
SHEET 1 AA1 8 GLY B 12 ILE B 16 0
SHEET 2 AA1 8 ILE B 23 GLY B 29 -1 O VAL B 27 N GLY B 12
SHEET 3 AA1 8 LYS B 59 ALA B 63 -1 O VAL B 60 N GLY B 28
SHEET 4 AA1 8 PRO B 33 LEU B 37 1 N LEU B 34 O LYS B 59
SHEET 5 AA1 8 PHE B 104 HIS B 109 1 O ALA B 105 N LEU B 35
SHEET 6 AA1 8 LEU B 127 LEU B 133 1 O ALA B 131 N LEU B 106
SHEET 7 AA1 8 MET B 244 GLY B 249 1 O LEU B 245 N VAL B 132
SHEET 8 AA1 8 VAL B 271 ILE B 276 1 O GLN B 272 N ALA B 246
SHEET 1 AA2 8 GLY A 12 ILE A 16 0
SHEET 2 AA2 8 ILE A 23 GLY A 29 -1 O ILE A 23 N ILE A 16
SHEET 3 AA2 8 LYS A 59 ALA A 63 -1 O VAL A 62 N ARG A 26
SHEET 4 AA2 8 PRO A 33 LEU A 37 1 N LEU A 34 O ILE A 61
SHEET 5 AA2 8 PHE A 104 HIS A 109 1 O ALA A 107 N LEU A 35
SHEET 6 AA2 8 LEU A 127 LEU A 133 1 O ALA A 131 N LEU A 106
SHEET 7 AA2 8 MET A 244 GLY A 249 1 O LEU A 245 N VAL A 132
SHEET 8 AA2 8 VAL A 271 ILE A 276 1 O GLN A 272 N ALA A 246
CISPEP 1 PHE B 40 PRO B 41 0 -1.33
CISPEP 2 ALA B 163 PRO B 164 0 7.86
CISPEP 3 PHE A 40 PRO A 41 0 -1.67
CISPEP 4 ALA A 163 PRO A 164 0 2.13
SITE 1 AC1 8 ASN B 110 ARG B 111 ARG B 114 TRP B 156
SITE 2 AC1 8 TYR B 219 HOH B 519 HOH B 531 HOH B 687
SITE 1 AC2 7 GLU B 285 ALA B 286 PRO B 287 ASP B 288
SITE 2 AC2 7 GLN B 289 HOH B 703 HOH B 783
SITE 1 AC3 7 ASN A 110 ARG A 111 ARG A 114 TYR A 219
SITE 2 AC3 7 HOH A 535 HOH A 546 HOH A 649
SITE 1 AC4 6 ALA A 286 PRO A 287 ASP A 288 GLN A 289
SITE 2 AC4 6 HOH A 674 HOH A 764
CRYST1 41.880 78.850 85.130 90.00 103.71 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 0.023878 0.000000 0.005826 0.00000
SCALE2 0.000000 0.012682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012091 0.00000
TER 2324 SER B 299
TER 4725 ALA A 300
MASTER 352 0 4 32 16 0 8 6 5372 2 16 48
END |