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HEADER HYDROLASE 04-AUG-08 3E1G
TITLE SNAPSHOTS OF ESTERASE D FROM LACTOBACILLUS RHAMNOSUS:
TITLE 2 INSIGHTS INTO A ROTATION DRIVEN CATALYTIC MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE D;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS RHAMNOSUS;
SOURCE 3 ORGANISM_TAXID: 486408;
SOURCE 4 STRAIN: HN001;
SOURCE 5 GENE: ESTD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEXHTC
KEYWDS ALPHA BETA HYDROLASE, MECHANISM, CATALYTIC TRIAD, ROTATION,
KEYWDS 2 ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.BENNETT,M.-L.DELABRE,R.HOLLAND,G.E.NORRIS
REVDAT 1 04-AUG-09 3E1G 0
JRNL AUTH M.D.BENNETT,M.-L.DELABRE,R.HOLLAND,G.E.NORRIS
JRNL TITL SNAPSHOTS OF ESTERASE D FROM LACTOBACILLUS
JRNL TITL 2 RHAMNOSUS: INSIGHTS INTO A ROTATION DRIVEN
JRNL TITL 3 CATALYTIC MECHANISM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 11667
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 578
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 839
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 40
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1793
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.51000
REMARK 3 B22 (A**2) : 1.51000
REMARK 3 B33 (A**2) : -2.26000
REMARK 3 B12 (A**2) : 0.75000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.248
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.224
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.020
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1849 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1163 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2522 ; 0.802 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2848 ; 0.682 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 238 ; 8.167 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 78 ;35.882 ;24.615
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 259 ;15.014 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;13.851 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 283 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2105 ; 0.021 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 377 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 419 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1217 ; 0.212 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 902 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 905 ; 0.104 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 85 ; 0.159 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.071 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 6 ; 0.259 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 39 ; 0.318 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.149 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3E1G COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048754.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.0
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 : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC BLUE
REMARK 200 OPTICS : OSMIC BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTAL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34921
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 33.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.1000
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: MOLREP
REMARK 200 STARTING MODEL: 1R1D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NA ACETATE, PH 6.0,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.49400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.24700
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.24700
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 116.49400
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A -6
REMARK 465 ALA A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ILE A -2
REMARK 465 ARG A -1
REMARK 465 ASN A 0
REMARK 465 SER A 1
REMARK 465 ILE A 2
REMARK 465 ASN A 242
REMARK 465 GLU A 243
REMARK 465 GLY A 244
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 LYS A 5 CD CE NZ
REMARK 470 LYS A 87 NZ
REMARK 470 LYS A 124 CD CE NZ
REMARK 470 LYS A 133 CD CE NZ
REMARK 470 TYR A 137 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 LYS A 177 CD CE NZ
REMARK 470 ARG A 194 NE CZ NH1 NH2
REMARK 470 ARG A 208 CD NE CZ NH1 NH2
REMARK 470 ASP A 216 OD1 OD2
REMARK 470 LYS A 218 CD CE NZ
REMARK 470 GLN A 239 CG CD OE1 NE2
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 A 94 P DEP A 245 1.62
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 14 -71.64 -128.79
REMARK 500 SER A 94 -109.80 48.24
REMARK 500 SER A 117 63.10 37.29
REMARK 500 SER A 118 86.23 -152.00
REMARK 500 ILE A 120 -67.81 78.55
REMARK 500 ASP A 146 151.16 -26.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 214 ASP A 215 -149.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 56 -10.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP A 245
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DKR RELATED DB: PDB
REMARK 900 RELATED ID: 3DLT RELATED DB: PDB
DBREF 3E1G A 2 244 UNP B2CZF3 B2CZF3_LACRH 2 244
SEQADV 3E1G GLY A -6 UNP B2CZF3 EXPRESSION TAG
SEQADV 3E1G ALA A -5 UNP B2CZF3 EXPRESSION TAG
SEQADV 3E1G MET A -4 UNP B2CZF3 EXPRESSION TAG
SEQADV 3E1G GLY A -3 UNP B2CZF3 EXPRESSION TAG
SEQADV 3E1G ILE A -2 UNP B2CZF3 EXPRESSION TAG
SEQADV 3E1G ARG A -1 UNP B2CZF3 EXPRESSION TAG
SEQADV 3E1G ASN A 0 UNP B2CZF3 EXPRESSION TAG
SEQADV 3E1G SER A 1 UNP B2CZF3 EXPRESSION TAG
SEQRES 1 A 251 GLY ALA MET GLY ILE ARG ASN SER ILE PHE ARG LYS PRO
SEQRES 2 A 251 GLN PRO PHE GLU TYR GLU GLY THR ASP THR GLY VAL VAL
SEQRES 3 A 251 LEU LEU HIS ALA TYR THR GLY SER PRO ASN ASP MET ASN
SEQRES 4 A 251 PHE MET ALA ARG ALA LEU GLN ARG SER GLY TYR GLY VAL
SEQRES 5 A 251 TYR VAL PRO LEU PHE SER GLY HIS GLY THR VAL GLU PRO
SEQRES 6 A 251 LEU ASP ILE LEU THR LYS GLY ASN PRO ASP ILE TRP TRP
SEQRES 7 A 251 ALA GLU SER SER ALA ALA VAL ALA HIS MET THR ALA LYS
SEQRES 8 A 251 TYR ALA LYS VAL PHE VAL PHE GLY LEU SER LEU GLY GLY
SEQRES 9 A 251 ILE PHE ALA MET LYS ALA LEU GLU THR LEU PRO GLY ILE
SEQRES 10 A 251 THR ALA GLY GLY VAL PHE SER SER PRO ILE LEU PRO GLY
SEQRES 11 A 251 LYS HIS HIS LEU VAL PRO GLY PHE LEU LYS TYR ALA GLU
SEQRES 12 A 251 TYR MET ASN ARG LEU ALA GLY LYS SER ASP GLU SER THR
SEQRES 13 A 251 GLN ILE LEU ALA TYR LEU PRO GLY GLN LEU ALA ALA ILE
SEQRES 14 A 251 ASP GLN PHE ALA THR THR VAL ALA ALA ASP LEU ASN LEU
SEQRES 15 A 251 VAL LYS GLN PRO THR PHE ILE GLY GLN ALA GLY GLN ASP
SEQRES 16 A 251 GLU LEU VAL ASP GLY ARG LEU ALA TYR GLN LEU ARG ASP
SEQRES 17 A 251 ALA LEU ILE ASN ALA ALA ARG VAL ASP PHE HIS TRP TYR
SEQRES 18 A 251 ASP ASP ALA LYS HIS VAL ILE THR VAL ASN SER ALA HIS
SEQRES 19 A 251 HIS ALA LEU GLU GLU ASP VAL ILE ALA PHE MET GLN GLN
SEQRES 20 A 251 GLU ASN GLU GLY
HET DEP A 245 8
HETNAM DEP DIETHYL PHOSPHONATE
FORMUL 2 DEP C4 H11 O3 P
FORMUL 3 HOH *87(H2 O)
HELIX 1 1 SER A 27 ASP A 30 5 4
HELIX 2 2 MET A 31 SER A 41 1 11
HELIX 3 3 PRO A 58 GLY A 65 1 8
HELIX 4 4 ASN A 66 ALA A 83 1 18
HELIX 5 5 SER A 94 LEU A 107 1 14
HELIX 6 6 HIS A 126 GLY A 143 1 18
HELIX 7 7 GLU A 147 ASP A 172 1 26
HELIX 8 8 LEU A 173 VAL A 176 5 4
HELIX 9 9 ASP A 192 ARG A 194 5 3
HELIX 10 10 LEU A 195 LEU A 203 1 9
HELIX 11 11 ALA A 226 GLU A 241 1 16
SHEET 1 A 7 PHE A 9 TYR A 11 0
SHEET 2 A 7 GLY A 44 VAL A 47 -1 O VAL A 47 N PHE A 9
SHEET 3 A 7 THR A 16 LEU A 21 1 N LEU A 20 O TYR A 46
SHEET 4 A 7 LYS A 87 LEU A 93 1 O LYS A 87 N GLY A 17
SHEET 5 A 7 ALA A 112 PHE A 116 1 O PHE A 116 N GLY A 92
SHEET 6 A 7 THR A 180 ALA A 185 1 O PHE A 181 N VAL A 115
SHEET 7 A 7 VAL A 209 TYR A 214 1 O HIS A 212 N ILE A 182
SITE 1 AC1 7 ALA A 23 TYR A 24 SER A 94 LEU A 95
SITE 2 AC1 7 LEU A 127 ILE A 162 HIS A 219
CRYST1 47.322 47.322 174.741 90.00 90.00 120.00 P 32 2 1 6
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 0.021132 0.012200 0.000000 0.00000
SCALE2 0.000000 0.024401 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005723 0.00000
TER 1794 GLU A 241
MASTER 346 0 1 11 7 0 2 6 1888 1 8 20
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