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HEADER HYDROLASE 22-DEC-20 7DQ9
TITLE CRYSTAL STRUCTURE OF A TYPE-A FERULOYL ESTERASE FROM GUT ALISTIPES
TITLE 2 SHAHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PREDICTED HYDROLASES OR ACYLTRANSFERASES (ALPHA/BETA
COMPND 3 HYDROLASE SUPERFAMILY);
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: FERULOYL ESTERASE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALISTIPES SHAHII WAL 8301;
SOURCE 3 ORGANISM_TAXID: 717959;
SOURCE 4 GENE: AL1_21970;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS GUT MICROORGANISMS, ALISTIPES SHAHII, ESTERASE, ESTER BOND, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.WEI,T.Y.GU,F.J.XIN,Y.L.WANG
REVDAT 1 22-DEC-21 7DQ9 0
JRNL AUTH X.WEI,T.Y.GU,F.J.XIN,Y.L.WANG
JRNL TITL CRYSTAL STRUCTURE OF A TYPE-A FERULOYL ESTERASE FROM GUT
JRNL TITL 2 ALISTIPES SHAHII
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 116427
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 5785
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 45.4300 - 5.2851 0.98 3856 210 0.1649 0.2012
REMARK 3 2 5.2851 - 4.1959 1.00 3812 185 0.1397 0.1789
REMARK 3 3 4.1959 - 3.6657 0.91 3499 176 0.1467 0.1665
REMARK 3 4 3.6657 - 3.3307 0.89 3415 165 0.1533 0.1760
REMARK 3 5 3.3307 - 3.0920 1.00 3753 223 0.1658 0.1896
REMARK 3 6 3.0920 - 2.9098 1.00 3814 165 0.1648 0.2117
REMARK 3 7 2.9098 - 2.7641 1.00 3799 189 0.1654 0.2034
REMARK 3 8 2.7641 - 2.6437 1.00 3773 196 0.1704 0.2077
REMARK 3 9 2.6437 - 2.5420 1.00 3761 220 0.1712 0.2020
REMARK 3 10 2.5420 - 2.4543 1.00 3812 184 0.1718 0.2218
REMARK 3 11 2.4543 - 2.3775 1.00 3722 222 0.1713 0.1932
REMARK 3 12 2.3775 - 2.3096 1.00 3813 185 0.1681 0.1998
REMARK 3 13 2.3096 - 2.2488 0.79 2973 167 0.1741 0.1993
REMARK 3 14 2.2488 - 2.1939 0.80 3006 152 0.1719 0.1884
REMARK 3 15 2.1939 - 2.1440 1.00 3811 175 0.1649 0.2061
REMARK 3 16 2.1440 - 2.0984 1.00 3747 194 0.1684 0.2013
REMARK 3 17 2.0984 - 2.0564 1.00 3777 205 0.1733 0.2187
REMARK 3 18 2.0564 - 2.0176 1.00 3795 191 0.1761 0.2189
REMARK 3 19 2.0176 - 1.9816 1.00 3770 172 0.1756 0.2335
REMARK 3 20 1.9816 - 1.9480 1.00 3785 178 0.1757 0.2161
REMARK 3 21 1.9480 - 1.9166 1.00 3769 198 0.1794 0.2292
REMARK 3 22 1.9166 - 1.8871 0.99 3737 204 0.1788 0.2381
REMARK 3 23 1.8871 - 1.8593 1.00 3757 216 0.1770 0.2290
REMARK 3 24 1.8593 - 1.8331 1.00 3748 183 0.1806 0.2157
REMARK 3 25 1.8331 - 1.8084 1.00 3748 221 0.1776 0.2497
REMARK 3 26 1.8084 - 1.7849 1.00 3778 227 0.1845 0.2154
REMARK 3 27 1.7849 - 1.7626 1.00 3715 162 0.1836 0.2374
REMARK 3 28 1.7626 - 1.7413 1.00 3758 221 0.1879 0.2231
REMARK 3 29 1.7413 - 1.7211 1.00 3784 216 0.2001 0.2431
REMARK 3 30 1.7211 - 1.7020 0.89 3355 183 0.2051 0.2553
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) : 18.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.29
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7DQ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1300019839.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.42
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 3.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116510
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.27400
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: 4UHH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BISTRIS PROPANE (PH 7.42), 22%
REMARK 280 PEG3350, 0.2M POTASSIUM THIOCYANATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293.15K
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 37.77250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 LYS A 266
REMARK 465 LYS B 266
REMARK 465 ARG C 151
REMARK 465 VAL C 152
REMARK 465 ALA C 153
REMARK 465 PRO C 154
REMARK 465 LYS C 266
REMARK 465 LYS D 266
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 501 O HOH A 582 2.05
REMARK 500 O HOH B 400 O HOH B 576 2.10
REMARK 500 O HOH C 412 O HOH C 657 2.11
REMARK 500 O HOH A 475 O HOH A 578 2.12
REMARK 500 OE1 GLU D 181 O HOH D 301 2.12
REMARK 500 NZ LYS A 230 O HOH A 301 2.12
REMARK 500 O HOH C 488 O HOH C 597 2.13
REMARK 500 O HOH A 501 O HOH A 544 2.14
REMARK 500 O HOH A 544 O HOH A 606 2.14
REMARK 500 OD1 ASP D 182 O HOH D 302 2.14
REMARK 500 OE1 GLU C 160 NH1 ARG C 163 2.15
REMARK 500 O HOH A 582 O HOH A 607 2.15
REMARK 500 O HOH D 458 O HOH D 523 2.16
REMARK 500 O HOH D 549 O HOH D 596 2.17
REMARK 500 OE1 GLU D 107 O HOH D 303 2.17
REMARK 500 O HOH B 382 O HOH B 563 2.17
REMARK 500 O HOH A 396 O HOH A 469 2.18
REMARK 500 O HOH C 310 O HOH C 495 2.18
REMARK 500 O HOH A 333 O HOH A 618 2.18
REMARK 500 OE1 GLU B 231 O HOH B 301 2.19
REMARK 500 O HOH D 386 O HOH D 414 2.19
REMARK 500 O HOH A 540 O HOH A 640 2.19
REMARK 500 O HOH B 420 O HOH B 494 2.19
REMARK 500 O HOH D 342 O HOH D 542 2.19
REMARK 500 O HOH A 392 O HOH A 672 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 C 647 O HOH C 677 2445 2.14
REMARK 500 O HOH A 719 O HOH B 628 1445 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 19 -43.90 70.99
REMARK 500 SER A 96 -109.41 54.05
REMARK 500 GLN B 19 -45.01 74.04
REMARK 500 SER B 96 -112.78 53.47
REMARK 500 ASN B 242 18.52 90.22
REMARK 500 GLN C 19 -44.08 71.37
REMARK 500 SER C 96 -110.89 55.71
REMARK 500 GLN D 19 -42.34 71.14
REMARK 500 SER D 96 -108.20 53.07
REMARK 500 LYS D 145 37.99 -99.23
REMARK 500 ALA D 153 70.84 -157.77
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 724 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 725 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 726 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH C 681 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH C 682 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH C 683 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH C 684 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH C 685 DISTANCE = 7.77 ANGSTROMS
REMARK 525 HOH D 601 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH D 602 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH D 603 DISTANCE = 6.53 ANGSTROMS
DBREF 7DQ9 A 1 266 UNP D4INH0 D4INH0_9BACT 1 266
DBREF 7DQ9 B 1 266 UNP D4INH0 D4INH0_9BACT 1 266
DBREF 7DQ9 C 1 266 UNP D4INH0 D4INH0_9BACT 1 266
DBREF 7DQ9 D 1 266 UNP D4INH0 D4INH0_9BACT 1 266
SEQRES 1 A 266 MET ILE GLU LYS PHE ILE MET ALA GLY PRO THR ALA LEU
SEQRES 2 A 266 HIS VAL CYS ASP SER GLN LYS GLY ASP LYS CYS VAL VAL
SEQRES 3 A 266 LEU LEU HIS GLY TYR LEU GLU SER MET LEU VAL TRP GLU
SEQRES 4 A 266 ASP PHE VAL PRO PHE LEU TYR LYS GLU LEU ARG VAL VAL
SEQRES 5 A 266 THR LEU ASP LEU PRO GLY HIS GLY ILE SER VAL VAL THR
SEQRES 6 A 266 GLY GLU GLU HIS SER MET GLU PHE LEU ALA ASP THR VAL
SEQRES 7 A 266 ALA ASP ALA LEU ARG ALA LEU GLY ILE PRO ARG CYS THR
SEQRES 8 A 266 LEU VAL GLY HIS SER MET GLY GLY TYR VAL ALA LEU ALA
SEQRES 9 A 266 PHE CYS GLU ARG HIS PRO ASP MET LEU ASN GLY VAL VAL
SEQRES 10 A 266 LEU LEU SER SER THR PRO ASN ALA ASP THR PRO GLU LYS
SEQRES 11 A 266 SER GLU ASN ARG ARG ARG GLU ILE ALA LEU VAL LYS ALA
SEQRES 12 A 266 GLY LYS LYS ASP ALA LEU ALA ARG VAL ALA PRO GLU ALA
SEQRES 13 A 266 GLY PHE ALA GLU ASP ASN ARG THR ARG MET LYS ASP TYR
SEQRES 14 A 266 ILE GLU ASP LEU THR GLU GLN VAL ALA VAL THR GLU ASP
SEQRES 15 A 266 GLU GLY ILE VAL ALA LEU LEU ASN GLY MET ILE ALA ARG
SEQRES 16 A 266 LYS ASP GLN ASN GLU MET LEU ARG ALA SER LYS VAL PRO
SEQRES 17 A 266 GLN LEU PHE ILE LEU GLY ARG LYS ASP ASN TYR ILE PRO
SEQRES 18 A 266 VAL GLU ALA ALA GLU LYS MET VAL LYS GLU HIS LEU GLN
SEQRES 19 A 266 ALA ARG VAL VAL TRP LEU GLU ASN SER GLY HIS MET GLY
SEQRES 20 A 266 PHE LEU GLU GLU PRO GLU THR THR ALA ARG ALA ILE LEU
SEQRES 21 A 266 ASP PHE VAL ASN GLY LYS
SEQRES 1 B 266 MET ILE GLU LYS PHE ILE MET ALA GLY PRO THR ALA LEU
SEQRES 2 B 266 HIS VAL CYS ASP SER GLN LYS GLY ASP LYS CYS VAL VAL
SEQRES 3 B 266 LEU LEU HIS GLY TYR LEU GLU SER MET LEU VAL TRP GLU
SEQRES 4 B 266 ASP PHE VAL PRO PHE LEU TYR LYS GLU LEU ARG VAL VAL
SEQRES 5 B 266 THR LEU ASP LEU PRO GLY HIS GLY ILE SER VAL VAL THR
SEQRES 6 B 266 GLY GLU GLU HIS SER MET GLU PHE LEU ALA ASP THR VAL
SEQRES 7 B 266 ALA ASP ALA LEU ARG ALA LEU GLY ILE PRO ARG CYS THR
SEQRES 8 B 266 LEU VAL GLY HIS SER MET GLY GLY TYR VAL ALA LEU ALA
SEQRES 9 B 266 PHE CYS GLU ARG HIS PRO ASP MET LEU ASN GLY VAL VAL
SEQRES 10 B 266 LEU LEU SER SER THR PRO ASN ALA ASP THR PRO GLU LYS
SEQRES 11 B 266 SER GLU ASN ARG ARG ARG GLU ILE ALA LEU VAL LYS ALA
SEQRES 12 B 266 GLY LYS LYS ASP ALA LEU ALA ARG VAL ALA PRO GLU ALA
SEQRES 13 B 266 GLY PHE ALA GLU ASP ASN ARG THR ARG MET LYS ASP TYR
SEQRES 14 B 266 ILE GLU ASP LEU THR GLU GLN VAL ALA VAL THR GLU ASP
SEQRES 15 B 266 GLU GLY ILE VAL ALA LEU LEU ASN GLY MET ILE ALA ARG
SEQRES 16 B 266 LYS ASP GLN ASN GLU MET LEU ARG ALA SER LYS VAL PRO
SEQRES 17 B 266 GLN LEU PHE ILE LEU GLY ARG LYS ASP ASN TYR ILE PRO
SEQRES 18 B 266 VAL GLU ALA ALA GLU LYS MET VAL LYS GLU HIS LEU GLN
SEQRES 19 B 266 ALA ARG VAL VAL TRP LEU GLU ASN SER GLY HIS MET GLY
SEQRES 20 B 266 PHE LEU GLU GLU PRO GLU THR THR ALA ARG ALA ILE LEU
SEQRES 21 B 266 ASP PHE VAL ASN GLY LYS
SEQRES 1 C 266 MET ILE GLU LYS PHE ILE MET ALA GLY PRO THR ALA LEU
SEQRES 2 C 266 HIS VAL CYS ASP SER GLN LYS GLY ASP LYS CYS VAL VAL
SEQRES 3 C 266 LEU LEU HIS GLY TYR LEU GLU SER MET LEU VAL TRP GLU
SEQRES 4 C 266 ASP PHE VAL PRO PHE LEU TYR LYS GLU LEU ARG VAL VAL
SEQRES 5 C 266 THR LEU ASP LEU PRO GLY HIS GLY ILE SER VAL VAL THR
SEQRES 6 C 266 GLY GLU GLU HIS SER MET GLU PHE LEU ALA ASP THR VAL
SEQRES 7 C 266 ALA ASP ALA LEU ARG ALA LEU GLY ILE PRO ARG CYS THR
SEQRES 8 C 266 LEU VAL GLY HIS SER MET GLY GLY TYR VAL ALA LEU ALA
SEQRES 9 C 266 PHE CYS GLU ARG HIS PRO ASP MET LEU ASN GLY VAL VAL
SEQRES 10 C 266 LEU LEU SER SER THR PRO ASN ALA ASP THR PRO GLU LYS
SEQRES 11 C 266 SER GLU ASN ARG ARG ARG GLU ILE ALA LEU VAL LYS ALA
SEQRES 12 C 266 GLY LYS LYS ASP ALA LEU ALA ARG VAL ALA PRO GLU ALA
SEQRES 13 C 266 GLY PHE ALA GLU ASP ASN ARG THR ARG MET LYS ASP TYR
SEQRES 14 C 266 ILE GLU ASP LEU THR GLU GLN VAL ALA VAL THR GLU ASP
SEQRES 15 C 266 GLU GLY ILE VAL ALA LEU LEU ASN GLY MET ILE ALA ARG
SEQRES 16 C 266 LYS ASP GLN ASN GLU MET LEU ARG ALA SER LYS VAL PRO
SEQRES 17 C 266 GLN LEU PHE ILE LEU GLY ARG LYS ASP ASN TYR ILE PRO
SEQRES 18 C 266 VAL GLU ALA ALA GLU LYS MET VAL LYS GLU HIS LEU GLN
SEQRES 19 C 266 ALA ARG VAL VAL TRP LEU GLU ASN SER GLY HIS MET GLY
SEQRES 20 C 266 PHE LEU GLU GLU PRO GLU THR THR ALA ARG ALA ILE LEU
SEQRES 21 C 266 ASP PHE VAL ASN GLY LYS
SEQRES 1 D 266 MET ILE GLU LYS PHE ILE MET ALA GLY PRO THR ALA LEU
SEQRES 2 D 266 HIS VAL CYS ASP SER GLN LYS GLY ASP LYS CYS VAL VAL
SEQRES 3 D 266 LEU LEU HIS GLY TYR LEU GLU SER MET LEU VAL TRP GLU
SEQRES 4 D 266 ASP PHE VAL PRO PHE LEU TYR LYS GLU LEU ARG VAL VAL
SEQRES 5 D 266 THR LEU ASP LEU PRO GLY HIS GLY ILE SER VAL VAL THR
SEQRES 6 D 266 GLY GLU GLU HIS SER MET GLU PHE LEU ALA ASP THR VAL
SEQRES 7 D 266 ALA ASP ALA LEU ARG ALA LEU GLY ILE PRO ARG CYS THR
SEQRES 8 D 266 LEU VAL GLY HIS SER MET GLY GLY TYR VAL ALA LEU ALA
SEQRES 9 D 266 PHE CYS GLU ARG HIS PRO ASP MET LEU ASN GLY VAL VAL
SEQRES 10 D 266 LEU LEU SER SER THR PRO ASN ALA ASP THR PRO GLU LYS
SEQRES 11 D 266 SER GLU ASN ARG ARG ARG GLU ILE ALA LEU VAL LYS ALA
SEQRES 12 D 266 GLY LYS LYS ASP ALA LEU ALA ARG VAL ALA PRO GLU ALA
SEQRES 13 D 266 GLY PHE ALA GLU ASP ASN ARG THR ARG MET LYS ASP TYR
SEQRES 14 D 266 ILE GLU ASP LEU THR GLU GLN VAL ALA VAL THR GLU ASP
SEQRES 15 D 266 GLU GLY ILE VAL ALA LEU LEU ASN GLY MET ILE ALA ARG
SEQRES 16 D 266 LYS ASP GLN ASN GLU MET LEU ARG ALA SER LYS VAL PRO
SEQRES 17 D 266 GLN LEU PHE ILE LEU GLY ARG LYS ASP ASN TYR ILE PRO
SEQRES 18 D 266 VAL GLU ALA ALA GLU LYS MET VAL LYS GLU HIS LEU GLN
SEQRES 19 D 266 ALA ARG VAL VAL TRP LEU GLU ASN SER GLY HIS MET GLY
SEQRES 20 D 266 PHE LEU GLU GLU PRO GLU THR THR ALA ARG ALA ILE LEU
SEQRES 21 D 266 ASP PHE VAL ASN GLY LYS
FORMUL 5 HOH *1473(H2 O)
HELIX 1 AA1 SER A 34 GLU A 39 5 6
HELIX 2 AA2 PHE A 41 LEU A 45 5 5
HELIX 3 AA3 SER A 70 GLY A 86 1 17
HELIX 4 AA4 SER A 96 HIS A 109 1 14
HELIX 5 AA5 THR A 127 ALA A 143 1 17
HELIX 6 AA6 LYS A 145 ASP A 147 5 3
HELIX 7 AA7 ALA A 148 GLY A 157 1 10
HELIX 8 AA8 ALA A 159 ARG A 163 5 5
HELIX 9 AA9 MET A 166 VAL A 179 1 14
HELIX 10 AB1 GLU A 181 ARG A 195 1 15
HELIX 11 AB2 GLN A 198 SER A 205 1 8
HELIX 12 AB3 PRO A 221 GLU A 231 1 11
HELIX 13 AB4 MET A 246 GLU A 251 1 6
HELIX 14 AB5 GLU A 251 ASN A 264 1 14
HELIX 15 AB6 SER B 34 GLU B 39 5 6
HELIX 16 AB7 PHE B 41 LEU B 45 5 5
HELIX 17 AB8 SER B 70 GLY B 86 1 17
HELIX 18 AB9 SER B 96 HIS B 109 1 14
HELIX 19 AC1 THR B 127 ALA B 143 1 17
HELIX 20 AC2 LYS B 145 GLY B 157 1 13
HELIX 21 AC3 ALA B 159 ARG B 163 5 5
HELIX 22 AC4 MET B 166 VAL B 179 1 14
HELIX 23 AC5 GLU B 181 ARG B 195 1 15
HELIX 24 AC6 GLN B 198 SER B 205 1 8
HELIX 25 AC7 PRO B 221 GLU B 231 1 11
HELIX 26 AC8 MET B 246 GLU B 251 1 6
HELIX 27 AC9 GLU B 251 ASN B 264 1 14
HELIX 28 AD1 SER C 34 GLU C 39 5 6
HELIX 29 AD2 PHE C 41 LEU C 45 5 5
HELIX 30 AD3 SER C 70 GLY C 86 1 17
HELIX 31 AD4 SER C 96 HIS C 109 1 14
HELIX 32 AD5 THR C 127 ALA C 143 1 17
HELIX 33 AD6 LYS C 145 LEU C 149 5 5
HELIX 34 AD7 ALA C 159 ARG C 163 5 5
HELIX 35 AD8 MET C 166 VAL C 179 1 14
HELIX 36 AD9 GLU C 181 ARG C 195 1 15
HELIX 37 AE1 GLN C 198 SER C 205 1 8
HELIX 38 AE2 PRO C 221 GLU C 231 1 11
HELIX 39 AE3 MET C 246 GLU C 251 1 6
HELIX 40 AE4 GLU C 251 ASN C 264 1 14
HELIX 41 AE5 SER D 34 GLU D 39 5 6
HELIX 42 AE6 PHE D 41 LEU D 45 5 5
HELIX 43 AE7 SER D 70 GLY D 86 1 17
HELIX 44 AE8 SER D 96 HIS D 109 1 14
HELIX 45 AE9 THR D 127 ALA D 143 1 17
HELIX 46 AF1 LYS D 145 ASP D 147 5 3
HELIX 47 AF2 ALA D 148 ALA D 153 1 6
HELIX 48 AF3 ALA D 159 ARG D 163 5 5
HELIX 49 AF4 MET D 166 VAL D 179 1 14
HELIX 50 AF5 GLU D 181 ARG D 195 1 15
HELIX 51 AF6 GLN D 198 SER D 205 1 8
HELIX 52 AF7 PRO D 221 GLU D 231 1 11
HELIX 53 AF8 MET D 246 GLU D 251 1 6
HELIX 54 AF9 GLU D 251 ASN D 264 1 14
SHEET 1 AA1 8 ILE A 2 ALA A 8 0
SHEET 2 AA1 8 THR A 11 ASP A 17 -1 O VAL A 15 N LYS A 4
SHEET 3 AA1 8 ARG A 50 LEU A 54 -1 O THR A 53 N CYS A 16
SHEET 4 AA1 8 CYS A 24 LEU A 28 1 N VAL A 25 O ARG A 50
SHEET 5 AA1 8 CYS A 90 HIS A 95 1 O VAL A 93 N VAL A 26
SHEET 6 AA1 8 LEU A 113 LEU A 119 1 O ASN A 114 N CYS A 90
SHEET 7 AA1 8 GLN A 209 GLY A 214 1 O LEU A 210 N LEU A 118
SHEET 8 AA1 8 ARG A 236 LEU A 240 1 O VAL A 238 N PHE A 211
SHEET 1 AA2 8 ILE B 2 ALA B 8 0
SHEET 2 AA2 8 THR B 11 ASP B 17 -1 O VAL B 15 N LYS B 4
SHEET 3 AA2 8 ARG B 50 LEU B 54 -1 O THR B 53 N CYS B 16
SHEET 4 AA2 8 CYS B 24 LEU B 28 1 N LEU B 27 O VAL B 52
SHEET 5 AA2 8 CYS B 90 HIS B 95 1 O VAL B 93 N VAL B 26
SHEET 6 AA2 8 LEU B 113 LEU B 119 1 O ASN B 114 N CYS B 90
SHEET 7 AA2 8 GLN B 209 GLY B 214 1 O LEU B 210 N LEU B 118
SHEET 8 AA2 8 ARG B 236 LEU B 240 1 O ARG B 236 N PHE B 211
SHEET 1 AA3 8 ILE C 2 ALA C 8 0
SHEET 2 AA3 8 THR C 11 ASP C 17 -1 O VAL C 15 N LYS C 4
SHEET 3 AA3 8 ARG C 50 LEU C 54 -1 O THR C 53 N CYS C 16
SHEET 4 AA3 8 CYS C 24 LEU C 28 1 N LEU C 27 O VAL C 52
SHEET 5 AA3 8 CYS C 90 HIS C 95 1 O VAL C 93 N VAL C 26
SHEET 6 AA3 8 LEU C 113 LEU C 119 1 O ASN C 114 N CYS C 90
SHEET 7 AA3 8 GLN C 209 GLY C 214 1 O ILE C 212 N LEU C 118
SHEET 8 AA3 8 ARG C 236 LEU C 240 1 O LEU C 240 N LEU C 213
SHEET 1 AA4 8 ILE D 2 ALA D 8 0
SHEET 2 AA4 8 THR D 11 ASP D 17 -1 O VAL D 15 N LYS D 4
SHEET 3 AA4 8 ARG D 50 LEU D 54 -1 O THR D 53 N CYS D 16
SHEET 4 AA4 8 CYS D 24 LEU D 28 1 N VAL D 25 O ARG D 50
SHEET 5 AA4 8 CYS D 90 HIS D 95 1 O VAL D 93 N VAL D 26
SHEET 6 AA4 8 LEU D 113 LEU D 119 1 O ASN D 114 N CYS D 90
SHEET 7 AA4 8 GLN D 209 GLY D 214 1 O ILE D 212 N LEU D 118
SHEET 8 AA4 8 ARG D 236 LEU D 240 1 O VAL D 238 N PHE D 211
CRYST1 45.469 75.545 161.021 90.00 92.34 90.00 P 1 21 1 8
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 0.021993 0.000000 0.000898 0.00000
SCALE2 0.000000 0.013237 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006216 0.00000
TER 2058 GLY A 265
TER 4116 GLY B 265
TER 6144 GLY C 265
TER 8202 GLY D 265
MASTER 350 0 0 54 32 0 0 6 9671 4 0 84
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