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HEADER HYDROLASE 22-APR-23 8SLJ
TITLE K164A MUTANT OF A CHLOROGENIC ACID ESTERASE FROM LACTOBACILLUS
TITLE 2 HELVETICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS HELVETICUS;
SOURCE 3 ORGANISM_TAXID: 1587;
SOURCE 4 GENE: BCM45_08315;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS CHLOROGENIC ACID, ESTERASE, FERULIC ACID ESTERASE, INSERTION DOMAIN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.P.OWENS,K.K.OMORI
REVDAT 1 27-MAR-24 8SLJ 0
JRNL AUTH K.K.OMORI,C.T.DRUCKER,T.L.S.OKUMURA,N.B.CARL,B.T.DINN,D.LY,
JRNL AUTH 2 K.N.SACAPANO,A.TAJII,C.P.OWENS
JRNL TITL THE STRUCTURE OF A LACTOBACILLUS HELVETICUS CHLOROGENIC ACID
JRNL TITL 2 ESTERASE AND THE DYNAMICS OF ITS INSERTION DOMAIN PROVIDE
JRNL TITL 3 INSIGHTS INTO SUBSTRATE BINDING.
JRNL REF FEBS LETT. V. 597 2946 2023
JRNL REFN ISSN 0014-5793
JRNL PMID 37698360
JRNL DOI 10.1002/1873-3468.14731
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 80084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4016
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 67.4800 - 6.4500 0.98 2665 156 0.1619 0.1702
REMARK 3 2 6.4500 - 5.1200 1.00 2690 144 0.0000 0.1670
REMARK 3 3 5.1200 - 4.4800 0.97 2603 137 0.1362 0.1756
REMARK 3 4 4.4800 - 4.0700 0.99 2664 145 0.1385 0.1820
REMARK 3 5 4.0700 - 3.7800 0.99 2617 147 0.0000 0.1383
REMARK 3 6 3.7800 - 3.5500 1.00 2670 142 0.1550 0.1942
REMARK 3 7 3.5500 - 3.3700 1.00 2668 122 0.1706 0.2020
REMARK 3 8 3.3700 - 3.2300 0.97 2615 119 0.1716 0.2159
REMARK 3 9 3.2300 - 3.1000 0.98 2602 137 0.1763 0.1776
REMARK 3 10 3.1000 - 3.0000 0.98 2622 140 0.1785 0.2199
REMARK 3 11 3.0000 - 2.9000 0.99 2637 142 0.1792 0.2178
REMARK 3 12 2.9000 - 2.8200 0.99 2605 147 0.1803 0.2173
REMARK 3 13 2.8200 - 2.7500 1.00 2643 131 0.1810 0.2132
REMARK 3 14 2.7500 - 2.6800 0.99 2631 170 0.1871 0.1921
REMARK 3 15 2.6800 - 2.6200 0.99 2634 129 0.1776 0.2181
REMARK 3 16 2.6200 - 2.5600 0.99 2655 136 0.1840 0.2056
REMARK 3 17 2.5600 - 2.5100 0.97 2545 139 0.1809 0.2182
REMARK 3 18 2.5100 - 2.4600 0.97 2583 130 0.1878 0.2382
REMARK 3 19 2.4600 - 2.4200 0.98 2645 109 0.1934 0.2330
REMARK 3 20 2.4200 - 2.3800 0.98 2587 144 0.2065 0.2420
REMARK 3 21 2.3800 - 2.3400 0.99 2630 140 0.2129 0.2556
REMARK 3 22 2.3400 - 2.3000 0.99 2633 116 0.2222 0.2510
REMARK 3 23 2.3000 - 2.2700 0.99 2604 160 0.2248 0.2360
REMARK 3 24 2.2700 - 2.2400 0.99 2576 135 0.2251 0.2837
REMARK 3 25 2.2400 - 2.2100 0.99 2659 141 0.2324 0.2530
REMARK 3 26 2.2100 - 2.1800 0.99 2641 120 0.2479 0.3002
REMARK 3 27 2.1800 - 2.1500 0.99 2609 144 0.2574 0.2875
REMARK 3 28 2.1500 - 2.1300 0.99 2642 162 0.2716 0.3170
REMARK 3 29 2.1300 - 2.1010 0.95 2493 132 0.2962 0.3565
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.67
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 : 0.007 NULL
REMARK 3 ANGLE : 0.846 NULL
REMARK 3 CHIRALITY : 0.054 900
REMARK 3 PLANARITY : 0.008 1085
REMARK 3 DIHEDRAL : 5.364 824
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 8SLJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1000273963.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-23
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : DIALS
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80226
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.101
REMARK 200 RESOLUTION RANGE LOW (A) : 67.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.08979
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.46660
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.020
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRIC ACID, PEG 6000, ZINC CHLORIDE,
REMARK 280 LITHIUM CHLORIDE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 89.80300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.91450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 89.80300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 55.91450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 458 LIES ON A SPECIAL POSITION.
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 B 348 O HOH B 493 1.85
REMARK 500 O HOH B 458 O HOH B 502 1.89
REMARK 500 O HOH A 406 O HOH A 541 1.91
REMARK 500 OD1 ASP A 99 O HOH A 301 1.92
REMARK 500 NE2 GLN B 187 O HOH B 301 1.93
REMARK 500 O HOH B 371 O HOH B 483 1.94
REMARK 500 OE2 GLU A 214 O HOH A 302 1.95
REMARK 500 O HOH A 483 O HOH A 521 2.01
REMARK 500 O HOH B 425 O HOH B 460 2.02
REMARK 500 OE2 GLU C 214 O HOH C 301 2.03
REMARK 500 O HOH A 530 O HOH A 546 2.03
REMARK 500 O HOH C 348 O HOH C 446 2.05
REMARK 500 O HOH C 324 O HOH C 484 2.05
REMARK 500 OD2 ASP A 99 O HOH A 303 2.05
REMARK 500 O HOH B 436 O HOH B 522 2.06
REMARK 500 OE2 GLU C 7 O HOH C 302 2.06
REMARK 500 O HOH A 415 O HOH A 520 2.08
REMARK 500 O ASP C 213 O HOH C 303 2.09
REMARK 500 O LEU C 160 O HOH C 304 2.11
REMARK 500 O HOH C 475 O HOH C 486 2.12
REMARK 500 O HOH B 443 O HOH B 484 2.12
REMARK 500 O HOH A 327 O HOH A 505 2.13
REMARK 500 O HOH C 515 O HOH C 523 2.15
REMARK 500 N GLY B 10 O HOH B 302 2.16
REMARK 500 OD1 ASP B 138 O HOH B 303 2.16
REMARK 500 O HOH C 512 O HOH C 532 2.16
REMARK 500 O PRO A 249 O HOH A 304 2.16
REMARK 500 O HOH C 376 O HOH C 406 2.17
REMARK 500 O PRO A 225 O HOH A 305 2.18
REMARK 500 OD1 ASP C 237 O HOH C 305 2.18
REMARK 500 O HOH C 437 O HOH C 482 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 575 O HOH A 575 2555 1.74
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 THR A 35 -2.63 66.88
REMARK 500 ARG A 98 -89.59 -95.11
REMARK 500 SER A 106 -126.40 62.83
REMARK 500 ALA A 132 55.89 -95.03
REMARK 500 HIS A 153 58.85 -143.29
REMARK 500 PRO A 206 -9.51 -58.63
REMARK 500 ASN A 226 -7.04 76.93
REMARK 500 ALA A 250 37.03 75.40
REMARK 500 THR B 35 -2.45 65.91
REMARK 500 ARG B 98 -89.10 -92.45
REMARK 500 SER B 106 -119.98 54.48
REMARK 500 ALA B 132 55.11 -93.01
REMARK 500 ASN B 226 -2.29 72.55
REMARK 500 ALA B 250 44.01 79.54
REMARK 500 ARG C 98 -97.92 -98.66
REMARK 500 SER C 106 -125.31 60.48
REMARK 500 VAL C 122 -59.94 -123.46
REMARK 500 ALA C 250 46.79 -84.45
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 585 DISTANCE = 6.18 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8SKM RELATED DB: PDB
REMARK 900 WILD TYPE STRUCTURE
DBREF1 8SLJ A 1 251 UNP A0A0D5MKR6_LACHE
DBREF2 8SLJ A A0A0D5MKR6 1 251
DBREF1 8SLJ B 1 251 UNP A0A0D5MKR6_LACHE
DBREF2 8SLJ B A0A0D5MKR6 1 251
DBREF1 8SLJ C 1 251 UNP A0A0D5MKR6_LACHE
DBREF2 8SLJ C A0A0D5MKR6 1 251
SEQADV 8SLJ SER A 0 UNP A0A0D5MKR EXPRESSION TAG
SEQADV 8SLJ ALA A 164 UNP A0A0D5MKR LYS 164 ENGINEERED MUTATION
SEQADV 8SLJ SER B 0 UNP A0A0D5MKR EXPRESSION TAG
SEQADV 8SLJ ALA B 164 UNP A0A0D5MKR LYS 164 ENGINEERED MUTATION
SEQADV 8SLJ SER C 0 UNP A0A0D5MKR EXPRESSION TAG
SEQADV 8SLJ ALA C 164 UNP A0A0D5MKR LYS 164 ENGINEERED MUTATION
SEQRES 1 A 252 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 A 252 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 A 252 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 A 252 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 A 252 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 A 252 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 A 252 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 A 252 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 A 252 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 A 252 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 A 252 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 A 252 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 A 252 ASP VAL VAL PRO LEU VAL GLY ASN ALA LEU GLY MET LYS
SEQRES 14 A 252 VAL GLY GLY PHE TYR LEU ARG THR ALA GLN VAL LEU PRO
SEQRES 15 A 252 ILE TYR GLU VAL SER GLN ARG PHE THR ARG PRO VAL SER
SEQRES 16 A 252 VAL ILE ALA GLY THR ASN ASP GLN VAL VAL ASP PRO LYS
SEQRES 17 A 252 TYR ALA LYS LYS TYR ASP GLU VAL TYR GLU ASN SER GLU
SEQRES 18 A 252 LEU HIS MET ILE PRO ASN ALA ASP HIS ARG PHE SER GLY
SEQRES 19 A 252 GLY TYR LYS ASP MET ALA ALA ASP LEU THR ALA GLN PHE
SEQRES 20 A 252 LEU LYS PRO ALA PHE
SEQRES 1 B 252 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 B 252 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 B 252 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 B 252 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 B 252 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 B 252 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 B 252 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 B 252 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 B 252 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 B 252 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 B 252 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 B 252 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 B 252 ASP VAL VAL PRO LEU VAL GLY ASN ALA LEU GLY MET LYS
SEQRES 14 B 252 VAL GLY GLY PHE TYR LEU ARG THR ALA GLN VAL LEU PRO
SEQRES 15 B 252 ILE TYR GLU VAL SER GLN ARG PHE THR ARG PRO VAL SER
SEQRES 16 B 252 VAL ILE ALA GLY THR ASN ASP GLN VAL VAL ASP PRO LYS
SEQRES 17 B 252 TYR ALA LYS LYS TYR ASP GLU VAL TYR GLU ASN SER GLU
SEQRES 18 B 252 LEU HIS MET ILE PRO ASN ALA ASP HIS ARG PHE SER GLY
SEQRES 19 B 252 GLY TYR LYS ASP MET ALA ALA ASP LEU THR ALA GLN PHE
SEQRES 20 B 252 LEU LYS PRO ALA PHE
SEQRES 1 C 252 SER MET SER ARG ILE THR ILE GLU ARG ASP GLY LEU THR
SEQRES 2 C 252 LEU VAL GLY ASP ARG GLU GLU PRO PHE GLY GLU ILE TYR
SEQRES 3 C 252 ASP MET ALA ILE ILE MET HIS GLY PHE THR ALA ASN ARG
SEQRES 4 C 252 ASN THR ASP LEU LEU ARG GLN ILE ALA ASP ASP LEU ARG
SEQRES 5 C 252 ASP GLU ASN VAL ALA SER VAL ARG PHE ASP PHE ASN GLY
SEQRES 6 C 252 HIS GLY GLU SER ASP GLY LYS PHE GLU ASP MET THR VAL
SEQRES 7 C 252 CYS ASN GLU ILE ALA ASP GLY LYS ALA ILE LEU ASP TYR
SEQRES 8 C 252 VAL HIS THR ASP PRO HIS VAL ARG ASP ILE PHE LEU VAL
SEQRES 9 C 252 GLY HIS SER GLN GLY GLY VAL VAL ALA SER MET LEU ALA
SEQRES 10 C 252 GLY LEU TYR PRO ASP VAL VAL LYS LYS VAL VAL LEU LEU
SEQRES 11 C 252 ALA PRO ALA ALA GLN LEU LYS ASP ASP ALA LEU ARG GLY
SEQRES 12 C 252 ASN THR GLN GLY ALA THR TYR ASP PRO ASN HIS ILE PRO
SEQRES 13 C 252 ASP VAL VAL PRO LEU VAL GLY ASN ALA LEU GLY MET LYS
SEQRES 14 C 252 VAL GLY GLY PHE TYR LEU ARG THR ALA GLN VAL LEU PRO
SEQRES 15 C 252 ILE TYR GLU VAL SER GLN ARG PHE THR ARG PRO VAL SER
SEQRES 16 C 252 VAL ILE ALA GLY THR ASN ASP GLN VAL VAL ASP PRO LYS
SEQRES 17 C 252 TYR ALA LYS LYS TYR ASP GLU VAL TYR GLU ASN SER GLU
SEQRES 18 C 252 LEU HIS MET ILE PRO ASN ALA ASP HIS ARG PHE SER GLY
SEQRES 19 C 252 GLY TYR LYS ASP MET ALA ALA ASP LEU THR ALA GLN PHE
SEQRES 20 C 252 LEU LYS PRO ALA PHE
FORMUL 4 HOH *743(H2 O)
HELIX 1 AA1 THR A 40 ASP A 52 1 13
HELIX 2 AA2 LYS A 71 MET A 75 5 5
HELIX 3 AA3 THR A 76 THR A 93 1 18
HELIX 4 AA4 GLN A 107 TYR A 119 1 13
HELIX 5 AA5 ALA A 133 GLY A 142 1 10
HELIX 6 AA6 VAL A 161 LEU A 165 5 5
HELIX 7 AA7 GLY A 171 VAL A 179 1 9
HELIX 8 AA8 PRO A 181 GLN A 187 1 7
HELIX 9 AA9 PRO A 206 TYR A 216 1 11
HELIX 10 AB1 GLY A 233 LYS A 248 1 16
HELIX 11 AB2 THR B 40 GLU B 53 1 14
HELIX 12 AB3 LYS B 71 MET B 75 5 5
HELIX 13 AB4 THR B 76 THR B 93 1 18
HELIX 14 AB5 GLN B 107 TYR B 119 1 13
HELIX 15 AB6 ALA B 133 GLY B 142 1 10
HELIX 16 AB7 VAL B 161 LEU B 165 5 5
HELIX 17 AB8 GLY B 171 VAL B 179 1 9
HELIX 18 AB9 PRO B 181 GLN B 187 1 7
HELIX 19 AC1 ASP B 205 TYR B 216 1 12
HELIX 20 AC2 GLY B 234 LYS B 248 1 15
HELIX 21 AC3 THR C 40 ASP C 52 1 13
HELIX 22 AC4 LYS C 71 MET C 75 5 5
HELIX 23 AC5 THR C 76 THR C 93 1 18
HELIX 24 AC6 GLN C 107 TYR C 119 1 13
HELIX 25 AC7 GLN C 134 GLY C 142 1 9
HELIX 26 AC8 VAL C 161 LEU C 165 5 5
HELIX 27 AC9 GLY C 171 VAL C 179 1 9
HELIX 28 AD1 PRO C 181 GLN C 187 1 7
HELIX 29 AD2 ASP C 205 TYR C 216 1 12
HELIX 30 AD3 GLY C 234 LYS C 248 1 15
SHEET 1 AA1 8 ARG A 3 ARG A 8 0
SHEET 2 AA1 8 LEU A 11 GLU A 18 -1 O LEU A 13 N ILE A 6
SHEET 3 AA1 8 VAL A 55 PHE A 60 -1 O SER A 57 N GLU A 18
SHEET 4 AA1 8 TYR A 25 MET A 31 1 N ILE A 30 O VAL A 58
SHEET 5 AA1 8 VAL A 97 HIS A 105 1 O VAL A 103 N MET A 31
SHEET 6 AA1 8 LYS A 125 LEU A 129 1 O LEU A 129 N GLY A 104
SHEET 7 AA1 8 VAL A 193 GLY A 198 1 O ILE A 196 N LEU A 128
SHEET 8 AA1 8 SER A 219 ILE A 224 1 O ILE A 224 N ALA A 197
SHEET 1 AA2 2 ASN A 143 THR A 144 0
SHEET 2 AA2 2 ALA A 147 THR A 148 -1 O ALA A 147 N THR A 144
SHEET 1 AA3 2 VAL A 157 PRO A 159 0
SHEET 2 AA3 2 LYS A 168 GLY A 170 -1 O VAL A 169 N VAL A 158
SHEET 1 AA4 8 MET B 1 ARG B 8 0
SHEET 2 AA4 8 LEU B 11 GLU B 18 -1 O ARG B 17 N SER B 2
SHEET 3 AA4 8 VAL B 55 PHE B 60 -1 O SER B 57 N GLU B 18
SHEET 4 AA4 8 TYR B 25 MET B 31 1 N ILE B 30 O VAL B 58
SHEET 5 AA4 8 VAL B 97 HIS B 105 1 O PHE B 101 N ILE B 29
SHEET 6 AA4 8 LYS B 125 LEU B 129 1 O LEU B 129 N GLY B 104
SHEET 7 AA4 8 VAL B 193 GLY B 198 1 O ILE B 196 N LEU B 128
SHEET 8 AA4 8 SER B 219 ILE B 224 1 O HIS B 222 N VAL B 195
SHEET 1 AA5 2 ASN B 143 THR B 144 0
SHEET 2 AA5 2 ALA B 147 THR B 148 -1 O ALA B 147 N THR B 144
SHEET 1 AA6 2 VAL B 157 PRO B 159 0
SHEET 2 AA6 2 LYS B 168 GLY B 170 -1 O VAL B 169 N VAL B 158
SHEET 1 AA7 8 ARG C 3 ARG C 8 0
SHEET 2 AA7 8 LEU C 11 GLU C 18 -1 O LEU C 13 N ILE C 6
SHEET 3 AA7 8 VAL C 55 PHE C 60 -1 O SER C 57 N GLU C 18
SHEET 4 AA7 8 TYR C 25 MET C 31 1 N ILE C 30 O VAL C 58
SHEET 5 AA7 8 VAL C 97 HIS C 105 1 O VAL C 103 N MET C 31
SHEET 6 AA7 8 LYS C 125 LEU C 129 1 O LEU C 129 N GLY C 104
SHEET 7 AA7 8 VAL C 193 GLY C 198 1 O ILE C 196 N LEU C 128
SHEET 8 AA7 8 SER C 219 ILE C 224 1 O HIS C 222 N VAL C 195
SHEET 1 AA8 2 ASN C 143 THR C 144 0
SHEET 2 AA8 2 ALA C 147 THR C 148 -1 O ALA C 147 N THR C 144
SHEET 1 AA9 2 VAL C 157 PRO C 159 0
SHEET 2 AA9 2 LYS C 168 GLY C 170 -1 O VAL C 169 N VAL C 158
CRYST1 179.606 111.829 75.930 90.00 111.41 90.00 C 1 2 1 12
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 0.005568 0.000000 0.002183 0.00000
SCALE2 0.000000 0.008942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014146 0.00000
TER 1957 PHE A 251
TER 3914 PHE B 251
TER 5870 PHE C 251
MASTER 345 0 0 30 36 0 0 6 6610 3 0 60
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