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HEADER HYDROLASE 09-OCT-13 4N5I
TITLE CRYSTAL STRUCTURE OF A C8-C4 SN3 INHIBITED ESTERASE B FROM
TITLE 2 LACTOBACILLUS RHAMNOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE;
COMPND 3 CHAIN: X;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS RHAMNOSUS;
SOURCE 3 ORGANISM_TAXID: 568704;
SOURCE 4 STRAIN: LC 705;
SOURCE 5 GENE: LC705_02872, LRH_10360;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX 6P3;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX_6P3_ESTB
KEYWDS ALPHA/BETA HYDROLASE FOLD, ESTERASE/LIPASE TRANSFERASE,
KEYWDS 2 TRIACYLGLYCERASE, HYDROLYSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.COLBERT,M.D BENNETT,D.J LUN,T.S LOO,B.F ANDERSON,G.E NORRIS
REVDAT 1 16-APR-14 4N5I 0
JRNL AUTH D.A.COLBERT,M.D BENNETT,D.J LUN,T.S LOO,B.F ANDERSON,
JRNL AUTH 2 G.E NORRIS
JRNL TITL CRYSTAL STRUCTURE OF A C8-C4 SN3 INHIBITED ESTERASE B FROM
JRNL TITL 2 LACTOBACILLUS RHAMNOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 22293
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1201
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) : 1600
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2472
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : 0.39000
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): 0.169
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.157
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.665
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2598 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2403 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3525 ; 1.764 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5512 ; 0.928 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 316 ; 6.758 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 135 ;34.940 ;24.296
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 406 ;14.523 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;21.249 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 368 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3013 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 641 ; 0.001 ; 0.020
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): 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4N5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB082777.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.5
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-002
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CAPILLARY FOCUSING OPTICS AND
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : CAPILLARY FOCUSING OPTICS AND
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23508
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 27.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.170
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.14
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
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: PDB ENTRY 4N5H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM PHOSPHATE, 0.1 M
REMARK 280 TRISHCL, PH 7.2-8.5 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 54.91300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.91300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 29.67350
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.91300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.91300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.67350
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 54.91300
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 54.91300
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 29.67350
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 54.91300
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 54.91300
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 29.67350
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: X
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 MET X 1
REMARK 465 ALA X 2
REMARK 465 ASP X 3
REMARK 465 GLU X 4
REMARK 465 PHE X 316
REMARK 465 GLU X 317
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 X 146 P9 2HD X 401 1.76
REMARK 500 NE2 GLN X 160 O HOH X 691 1.91
REMARK 500 OD1 ASP X 243 ND1 HIS X 278 2.01
REMARK 500 O HOH X 694 O HOH X 704 2.11
REMARK 500 O HOH X 683 O HOH X 754 2.17
REMARK 500 O HOH X 729 O HOH X 743 2.17
REMARK 500 O HOH X 716 O HOH X 729 2.18
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 X 597 O HOH X 682 3555 1.92
REMARK 500 OD1 ASP X 28 O HOH X 569 3555 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP X 37 CE3 TRP X 37 CZ3 0.104
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 X 51 49.83 -85.75
REMARK 500 TRP X 77 -8.66 66.00
REMARK 500 SER X 146 -114.21 58.72
REMARK 500 ASN X 174 44.28 -90.40
REMARK 500 CYS X 184 53.75 37.76
REMARK 500 VAL X 186 67.43 -114.18
REMARK 500 ALA X 195 -134.71 40.04
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 X 692 DISTANCE = 6.62 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2HD X 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT X 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT X 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N5H RELATED DB: PDB
DBREF 4N5I X 1 317 UNP C7TF14 C7TF14_LACRL 1 317
SEQADV 4N5I VAL X 218 UNP C7TF14 ALA 218 ENGINEERED MUTATION
SEQRES 1 X 317 MET ALA ASP GLU GLU ALA MET LEU ALA LYS VAL GLN ALA
SEQRES 2 X 317 SER TRP ALA GLN THR ALA ALA ARG ASP LYS ALA ARG TYR
SEQRES 3 X 317 ALA ASP GLU ARG VAL PRO GLU ASP VAL HIS TRP GLU THR
SEQRES 4 X 317 GLU TYR ARG TYR GLU GLN SER ALA ASP PRO GLN GLN THR
SEQRES 5 X 317 LEU ASN LEU TYR TYR PRO ALA LYS ARG ARG ASN ALA THR
SEQRES 6 X 317 MET PRO THR VAL ILE ASP ILE HIS GLY GLY GLY TRP PHE
SEQRES 7 X 317 TYR GLY ASP ARG ASN LEU ASN ARG ASN TYR CYS ARG TYR
SEQRES 8 X 317 LEU ALA SER GLN GLY TYR ALA VAL MET GLY MET GLY TYR
SEQRES 9 X 317 ARG LEU LEU PRO ASP VAL ASP LEU ARG GLY GLN ILE GLN
SEQRES 10 X 317 ASP ILE PHE ALA SER LEU ARG TRP LEU SER HIS PHE GLY
SEQRES 11 X 317 PRO GLN ARG GLY PHE ASP LEU ASP HIS VAL LEU LEU THR
SEQRES 12 X 317 GLY ASP SER ALA GLY GLY HIS LEU ALA SER LEU VAL ALA
SEQRES 13 X 317 CYS ILE GLN GLN SER ALA GLU LEU GLN GLU LEU PHE GLY
SEQRES 14 X 317 VAL SER ARG VAL ASN PHE ASN PHE THR LEU VAL ALA LEU
SEQRES 15 X 317 VAL CYS PRO VAL ALA GLU PRO SER LYS LEU PRO GLU ALA
SEQRES 16 X 317 ALA GLY ASP MET SER ASP MET ALA ALA PHE TYR LEU ASP
SEQRES 17 X 317 LYS LEU SER GLY GLY ASP GLN ALA LEU VAL ASP HIS LEU
SEQRES 18 X 317 ASN PHE SER GLN VAL VAL LYS GLY LEU ASP LEU PRO PRO
SEQRES 19 X 317 PHE MET LEU ILE GLY GLY GLN ASN ASP SER PHE TYR LEU
SEQRES 20 X 317 GLN SER GLN ALA LEU LEU LYS VAL PHE ASP ALA ASN HIS
SEQRES 21 X 317 VAL THR TYR THR THR LYS LEU TRP PRO ALA SER ALA GLY
SEQRES 22 X 317 PRO HIS LEU LYS HIS VAL PHE ASN VAL GLN HIS TRP GLU
SEQRES 23 X 317 TRP PRO GLU SER ILE GLU THR ASN LEU GLU MET LEU ARG
SEQRES 24 X 317 THR PHE ASP ALA LEU SER LYS GLN GLN ASP GLN ALA GLU
SEQRES 25 X 317 GLU ASN GLU PHE GLU
HET 2HD X 401 24
HET ACT X 402 4
HET ACT X 403 4
HETNAM 2HD (2R)-2,3-DIBUTOXYPROPYL (R)-OCTYLPHOSPHINATE
HETNAM ACT ACETATE ION
FORMUL 2 2HD C19 H41 O4 P
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 HOH *297(H2 O)
HELIX 1 1 GLU X 5 GLU X 29 1 25
HELIX 2 2 ASN X 85 GLN X 95 1 11
HELIX 3 3 ASP X 111 GLY X 130 1 20
HELIX 4 4 PRO X 131 ARG X 133 5 3
HELIX 5 5 SER X 146 SER X 161 1 16
HELIX 6 6 SER X 161 GLY X 169 1 9
HELIX 7 7 GLU X 188 LEU X 192 5 5
HELIX 8 8 ALA X 196 ASP X 198 5 3
HELIX 9 9 MET X 199 GLY X 212 1 14
HELIX 10 10 ASP X 214 ASP X 219 1 6
HELIX 11 11 ASN X 222 VAL X 227 1 6
HELIX 12 12 PHE X 245 ASN X 259 1 15
HELIX 13 13 PRO X 269 GLY X 273 5 5
HELIX 14 14 VAL X 279 HIS X 284 1 6
HELIX 15 15 TRP X 287 GLU X 312 1 26
SHEET 1 A 8 VAL X 35 ARG X 42 0
SHEET 2 A 8 THR X 52 PRO X 58 -1 O TYR X 57 N HIS X 36
SHEET 3 A 8 ALA X 98 MET X 102 -1 O VAL X 99 N TYR X 56
SHEET 4 A 8 MET X 66 ILE X 72 1 N VAL X 69 O MET X 100
SHEET 5 A 8 PHE X 135 ASP X 145 1 O LEU X 141 N THR X 68
SHEET 6 A 8 LEU X 179 VAL X 183 1 O VAL X 183 N GLY X 144
SHEET 7 A 8 PHE X 235 GLY X 240 1 O ILE X 238 N LEU X 182
SHEET 8 A 8 TYR X 263 TRP X 268 1 O TRP X 268 N GLY X 239
CISPEP 1 LEU X 107 PRO X 108 0 0.89
SITE 1 AC1 10 TRP X 15 GLY X 74 GLY X 75 GLY X 76
SITE 2 AC1 10 SER X 146 ALA X 147 PHE X 245 HIS X 278
SITE 3 AC1 10 GLN X 283 HOH X 706
SITE 1 AC2 5 GLU X 5 ALA X 6 HOH X 734 HOH X 792
SITE 2 AC2 5 HOH X 796
SITE 1 AC3 3 LYS X 266 LEU X 267 TRP X 268
CRYST1 109.826 109.826 59.347 90.00 90.00 90.00 I 4 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 0.009105 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009105 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016850 0.00000
TER 2499 GLU X 315
MASTER 375 0 3 15 8 0 6 6 2801 1 32 25
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