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HEADER HYDROLASE 04-FEB-10 3LP5
TITLE THE CRYSTAL STRUCTURE OF THE PUTATIVE CELL SURFACE HYDROLASE
TITLE 2 FROM LACTOBACILLUS PLANTARUM WCFS1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE CELL SURFACE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 40-288;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 1590;
SOURCE 4 STRAIN: WCFS1;
SOURCE 5 GENE: GI:28270776, LP_1165;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS SURFACE HYDROLASE, LACTOBACILLUS PLANTARUM, STRUCTURAL
KEYWDS 2 GENOMICS, PSI2, MCSG, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,H.LI,G.COBB,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 16-MAR-10 3LP5 0
JRNL AUTH R.ZHANG,H.LI,G.COBB,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF THE PUTATIVE CELL SURFACE
JRNL TITL 2 HYDROLASE FROM LACTOBACILLUS PLANTARUM WCFS1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 16267
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 866
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1139
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1980
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.38000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : 1.33000
REMARK 3 B12 (A**2) : 0.00000
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): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.473
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2023 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2743 ; 1.728 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 249 ; 6.238 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;34.229 ;24.286
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 350 ;15.692 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;15.983 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 310 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1518 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1245 ; 1.081 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2022 ; 1.970 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 778 ; 3.328 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 721 ; 5.649 ; 4.500
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 50
REMARK 3 RESIDUE RANGE : A 51 A 100
REMARK 3 RESIDUE RANGE : A 101 A 150
REMARK 3 RESIDUE RANGE : A 151 A 200
REMARK 3 RESIDUE RANGE : A 201 A 249
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2067 18.8965 28.2748
REMARK 3 T TENSOR
REMARK 3 T11: 0.0319 T22: 0.0394
REMARK 3 T33: 0.0121 T12: 0.0026
REMARK 3 T13: -0.0106 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.3885 L22: 0.8423
REMARK 3 L33: 0.4476 L12: 0.0767
REMARK 3 L13: 0.0019 L23: -0.2740
REMARK 3 S TENSOR
REMARK 3 S11: 0.0222 S12: -0.0365 S13: -0.0764
REMARK 3 S21: 0.0107 S22: -0.0221 S23: -0.0276
REMARK 3 S31: -0.0231 S32: -0.0478 S33: -0.0001
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 3LP5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057555.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL3000
REMARK 200 DATA SCALING SOFTWARE : HKL3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16267
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 61.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.18700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.66500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000_SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M TRI-SODIUM CITRATE DEHYDRATE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 25.84000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.07700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.84000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.07700
REMARK 290 SMTRY3 4 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: 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 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 NH2 ARG A 70 O HOH A 359 1.94
REMARK 500 O LEU A 161 O HOH A 332 2.03
REMARK 500 NE ARG A 70 O HOH A 359 2.05
REMARK 500 O HOH A 365 O HOH A 390 2.15
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 A 156 NE - CZ - NH1 ANGL. DEV. = 3.4 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 SER A 105 -129.61 58.89
REMARK 500 SER A 122 71.33 -116.01
REMARK 500 MET A 139 -133.73 59.53
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 399 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 400 DISTANCE = 7.81 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 251 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 32 O
REMARK 620 2 THR A 30 OG1 99.1
REMARK 620 3 HOH A 281 O 93.5 107.6
REMARK 620 4 GLY A 27 O 174.3 84.5 89.6
REMARK 620 5 THR A 30 O 87.8 76.7 175.2 88.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 251
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC60678.2 RELATED DB: TARGETDB
DBREF 3LP5 A 1 249 UNP Q88XN2 Q88XN2_LACPL 40 288
SEQADV 3LP5 ALA A 0 UNP Q88XN2 EXPRESSION TAG
SEQRES 1 A 250 ALA THR ARG MET ALA PRO VAL ILE MET VAL PRO GLY SER
SEQRES 2 A 250 SER ALA SER GLN ASN ARG PHE ASP SER LEU ILE THR GLU
SEQRES 3 A 250 LEU GLY LYS GLU THR PRO LYS LYS HIS SER VAL LEU LYS
SEQRES 4 A 250 LEU THR VAL GLN THR ASP GLY THR ILE LYS TYR SER GLY
SEQRES 5 A 250 SER ILE ALA ALA ASN ASP ASN GLU PRO PHE ILE VAL ILE
SEQRES 6 A 250 GLY PHE ALA ASN ASN ARG ASP GLY LYS ALA ASN ILE ASP
SEQRES 7 A 250 LYS GLN ALA VAL TRP LEU ASN THR ALA PHE LYS ALA LEU
SEQRES 8 A 250 VAL LYS THR TYR HIS PHE ASN HIS PHE TYR ALA LEU GLY
SEQRES 9 A 250 HIS SER ASN GLY GLY LEU ILE TRP THR LEU PHE LEU GLU
SEQRES 10 A 250 ARG TYR LEU LYS GLU SER PRO LYS VAL HIS ILE ASP ARG
SEQRES 11 A 250 LEU MET THR ILE ALA SER PRO TYR ASN MET GLU SER THR
SEQRES 12 A 250 SER THR THR ALA LYS THR SER MET PHE LYS GLU LEU TYR
SEQRES 13 A 250 ARG TYR ARG THR GLY LEU PRO GLU SER LEU THR VAL TYR
SEQRES 14 A 250 SER ILE ALA GLY THR GLU ASN TYR THR SER ASP GLY THR
SEQRES 15 A 250 VAL PRO TYR ASN SER VAL ASN TYR GLY LYS TYR ILE PHE
SEQRES 16 A 250 GLN ASP GLN VAL LYS HIS PHE THR GLU ILE THR VAL THR
SEQRES 17 A 250 GLY ALA ASN THR ALA HIS SER ASP LEU PRO GLN ASN LYS
SEQRES 18 A 250 GLN ILE VAL SER LEU ILE ARG GLN TYR LEU LEU ALA GLU
SEQRES 19 A 250 THR MET PRO ASP LYS VAL ARG GLN LYS ASN ALA GLN ARG
SEQRES 20 A 250 VAL GLN ASN
HET NA A 250 1
HET NA A 251 1
HETNAM NA SODIUM ION
FORMUL 2 NA 2(NA 1+)
FORMUL 4 HOH *154(H2 O)
HELIX 1 1 SER A 12 ALA A 14 5 3
HELIX 2 2 SER A 15 THR A 30 1 16
HELIX 3 3 GLY A 72 LYS A 92 1 21
HELIX 4 4 SER A 105 TYR A 118 1 14
HELIX 5 5 LEU A 119 SER A 122 5 4
HELIX 6 6 THR A 148 TYR A 157 1 10
HELIX 7 7 ARG A 158 LEU A 161 5 4
HELIX 8 8 PRO A 183 ASN A 188 1 6
HELIX 9 9 TYR A 189 GLN A 195 1 7
HELIX 10 10 ASP A 215 LEU A 230 1 16
HELIX 11 11 PRO A 236 GLN A 245 1 10
SHEET 1 A 8 ILE A 47 GLY A 51 0
SHEET 2 A 8 VAL A 36 VAL A 41 -1 N LYS A 38 O SER A 50
SHEET 3 A 8 PHE A 61 PHE A 66 1 O GLY A 65 N VAL A 41
SHEET 4 A 8 VAL A 6 VAL A 9 1 N MET A 8 O ILE A 62
SHEET 5 A 8 HIS A 98 HIS A 104 1 O TYR A 100 N ILE A 7
SHEET 6 A 8 HIS A 126 ILE A 133 1 O MET A 131 N GLY A 103
SHEET 7 A 8 THR A 166 ALA A 171 1 O TYR A 168 N LEU A 130
SHEET 8 A 8 HIS A 200 THR A 205 1 O HIS A 200 N VAL A 167
LINK O LYS A 32 NA NA A 251 1555 1555 2.16
LINK OG1 THR A 30 NA NA A 251 1555 1555 2.34
LINK NA NA A 251 O HOH A 281 1555 1555 2.36
LINK O GLY A 27 NA NA A 251 1555 1555 2.37
LINK O THR A 30 NA NA A 251 1555 1555 2.46
CISPEP 1 ASP A 179 GLY A 180 0 -10.81
SITE 1 AC1 4 GLY A 27 THR A 30 LYS A 32 HOH A 281
CRYST1 51.680 122.154 38.659 90.00 90.00 90.00 P 21 21 2 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 0.019350 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025867 0.00000
TER 1981 ASN A 249
MASTER 340 0 2 11 8 0 1 6 2136 1 7 20
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