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HEADER HYDROLASE 20-APR-23 8SKM
TITLE WILD TYPE CHLOROGENIC ACID ESTERASE FROM LACTOBACILLUS HELVETICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROGENIC ACID ESTERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: 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,T.L.S.OKUMURA
REVDAT 1 27-MAR-24 8SKM 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.19.2_4158: ???)
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 69602
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) : 0.177
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2015
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 35.9100 - 5.3000 0.99 4939 151 0.1670 0.1883
REMARK 3 2 5.3000 - 4.2100 0.99 4867 144 0.1353 0.1648
REMARK 3 3 4.2100 - 3.6800 1.00 4906 143 0.1282 0.1459
REMARK 3 4 3.6800 - 3.3400 1.00 4871 147 0.1516 0.1774
REMARK 3 5 3.3400 - 3.1000 1.00 4855 143 0.1706 0.2199
REMARK 3 6 3.1000 - 2.9200 1.00 4844 137 0.1774 0.2156
REMARK 3 7 2.9200 - 2.7700 1.00 4859 157 0.1860 0.2110
REMARK 3 8 2.7700 - 2.6500 1.00 4839 142 0.1980 0.2437
REMARK 3 9 2.6500 - 2.5500 0.99 4833 140 0.2037 0.2614
REMARK 3 10 2.5500 - 2.4600 0.99 4813 151 0.2250 0.2635
REMARK 3 11 2.4600 - 2.3800 1.00 4833 134 0.2304 0.2719
REMARK 3 12 2.3800 - 2.3200 0.99 4806 146 0.2440 0.2843
REMARK 3 13 2.3200 - 2.2600 0.98 4768 139 0.2569 0.2883
REMARK 3 14 2.2600 - 2.2000 0.94 4554 141 0.2707 0.3040
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.68
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 : 0.008 6006
REMARK 3 ANGLE : 0.956 8153
REMARK 3 CHIRALITY : 0.058 905
REMARK 3 PLANARITY : 0.009 1089
REMARK 3 DIHEDRAL : 6.148 833
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 8SKM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1000273961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-22
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 : SSRL
REMARK 200 BEAMLINE : BL12-2
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 : 649288
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 37.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.57130
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 1.64500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.700
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 (%): 70.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRIC ACID, PEG 6000, LITHIUM
REMARK 280 CHLORIDE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, 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 90.27450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.14600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 90.27450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 55.14600
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, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 BIOMT1 2 -1.000000 0.000000 0.000000 152.71494
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 70.69706
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 C 393 LIES ON A SPECIAL POSITION.
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 LEU A 165 CG CD1 CD2
REMARK 470 PHE B 251 CG CD1 CD2 CE1 CE2 CZ
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 OG SER B 0 O HOH B 301 1.98
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 -2.06 68.02
REMARK 500 ARG A 98 -87.12 -96.37
REMARK 500 SER A 106 -120.72 59.72
REMARK 500 ALA A 132 57.96 -91.35
REMARK 500 LYS A 164 31.28 -93.34
REMARK 500 PHE A 231 87.87 -56.37
REMARK 500 ALA A 250 45.17 78.38
REMARK 500 THR B 35 -6.91 81.54
REMARK 500 ARG B 98 -89.57 -97.99
REMARK 500 SER B 106 -124.33 58.40
REMARK 500 ALA B 132 58.57 -92.97
REMARK 500 ALA B 250 42.67 -88.18
REMARK 500 ARG C 98 -91.23 -97.36
REMARK 500 SER C 106 -124.74 62.62
REMARK 500 ASN C 226 -3.51 74.34
REMARK 500 ALA C 250 46.63 71.75
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 451 DISTANCE = 6.62 ANGSTROMS
DBREF1 8SKM A 1 251 UNP A0A0D5MKR6_LACHE
DBREF2 8SKM A A0A0D5MKR6 1 251
DBREF1 8SKM B 1 251 UNP A0A0D5MKR6_LACHE
DBREF2 8SKM B A0A0D5MKR6 1 251
DBREF1 8SKM C 1 251 UNP A0A0D5MKR6_LACHE
DBREF2 8SKM C A0A0D5MKR6 1 251
SEQADV 8SKM SER A 0 UNP A0A0D5MKR EXPRESSION TAG
SEQADV 8SKM SER B 0 UNP A0A0D5MKR EXPRESSION TAG
SEQADV 8SKM SER C 0 UNP A0A0D5MKR EXPRESSION TAG
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 LYS 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 LYS 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 LYS 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 *452(H2 O)
HELIX 1 AA1 THR A 40 GLU A 53 1 14
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 SER A 106 TYR A 119 1 14
HELIX 5 AA5 GLN A 134 GLY A 142 1 9
HELIX 6 AA6 VAL A 161 LEU A 165 5 5
HELIX 7 AA7 GLY A 171 LEU A 180 1 10
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 ASP B 94 1 19
HELIX 14 AB5 SER B 106 TYR B 119 1 14
HELIX 15 AB6 GLN B 134 GLY B 142 1 9
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 PRO B 206 TYR B 216 1 11
HELIX 20 AC2 GLY B 233 LYS B 248 1 16
HELIX 21 AC3 THR C 40 GLU C 53 1 14
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 SER C 106 TYR C 119 1 14
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 PRO C 206 TYR C 216 1 11
HELIX 30 AD3 GLY C 233 LYS C 248 1 16
SHEET 1 AA1 8 MET A 1 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 ASP A 99 N MET A 27
SHEET 6 AA1 8 VAL A 123 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 GLU A 220 N VAL A 195
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 ARG B 3 ARG B 8 0
SHEET 2 AA4 8 LEU B 11 GLU B 18 -1 O LEU B 13 N ILE B 6
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 ASP B 99 N MET B 27
SHEET 6 AA4 8 VAL B 123 LEU B 129 1 O LYS B 124 N ILE B 100
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 GLU B 220 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 GLU C 7 0
SHEET 2 AA7 8 THR C 12 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 PHE C 101 N ILE C 29
SHEET 6 AA7 8 VAL C 123 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 GLU C 220 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 180.549 110.292 75.979 90.00 111.49 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 0.005539 0.000000 0.002181 0.00000
SCALE2 0.000000 0.009067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014145 0.00000
TER 1958 PHE A 251
TER 3913 PHE B 251
TER 5874 PHE C 251
MASTER 282 0 0 30 36 0 0 6 6323 3 0 60
END |