HEADER ISOMERASE 18-FEB-10 3LUY
TITLE PUTATIVE CHORISMATE MUTASE FROM BIFIDOBACTERIUM ADOLESCENTIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE CHORISMATE MUTASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BIFIDOBACTERIUM ADOLESCENTIS;
SOURCE 3 ORGANISM_TAXID: 367928;
SOURCE 4 STRAIN: ATCC 15703;
SOURCE 5 GENE: BAD_1067, PHEA;
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: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS STRUCTURAL GENOMICS, APC38059, CHORISMATE, MUTASE, 3-PHENYLPYRUVATE,
KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,L.BIGELOW,J.BEARDEN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 3 08-NOV-17 3LUY 1 REMARK
REVDAT 2 13-JUL-11 3LUY 1 VERSN
REVDAT 1 09-MAR-10 3LUY 0
JRNL AUTH J.OSIPIUK,L.BIGELOW,J.BEARDEN,A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF PUTATIVE CHORISMATE MUTASE FROM
JRNL TITL 2 BIFIDOBACTERIUM ADOLESCENTIS.
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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 25902
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1317
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) : 1739
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2526
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 138
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 47.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.16000
REMARK 3 B22 (A**2) : 1.78000
REMARK 3 B33 (A**2) : 0.38000
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): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.792
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2728 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1828 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3750 ; 1.658 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4450 ; 0.966 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 358 ; 6.080 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;34.632 ;23.723
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 419 ;15.846 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;23.104 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 410 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3145 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 579 ; 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): 1679 ; 1.057 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 670 ; 0.283 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2719 ; 1.851 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1049 ; 2.748 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1014 ; 4.233 ; 4.500
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 326
REMARK 3 RESIDUE RANGE : A 501 A 501
REMARK 3 RESIDUE RANGE : A 327 A 464
REMARK 3 ORIGIN FOR THE GROUP (A): 90.0263 0.7151 4.9094
REMARK 3 T TENSOR
REMARK 3 T11: 0.0143 T22: 0.0557
REMARK 3 T33: 0.0791 T12: -0.0039
REMARK 3 T13: 0.0086 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.9469 L22: 0.6285
REMARK 3 L33: 1.6770 L12: 0.1415
REMARK 3 L13: -0.0766 L23: 0.5531
REMARK 3 S TENSOR
REMARK 3 S11: -0.0453 S12: 0.1205 S13: -0.0771
REMARK 3 S21: -0.0783 S22: 0.0479 S23: 0.0262
REMARK 3 S31: -0.0679 S32: -0.1724 S33: -0.0025
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 RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3LUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25950
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
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) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.82200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.090
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, SOLVE, RESOLVE, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM CHLORIDE, 0.05 M HEPES
REMARK 280 BUFFER, 35% PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH), PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
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 49.97700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.59900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.97700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.59900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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 199.90800
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 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
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 286 O HOH A 337 2.07
REMARK 500 NH2 ARG A 262 O HOH A 397 2.07
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 ASP A 74 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 265 CB - CG - OD1 ANGL. DEV. = 6.0 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 TRP A 61 -60.60 -121.06
REMARK 500 ASP A 81 66.68 -156.38
REMARK 500 ALA A 199 64.07 35.61
REMARK 500 GLU A 202 41.61 -91.21
REMARK 500 LEU A 212 51.91 -97.96
REMARK 500 LYS A 242 47.02 73.45
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 PPY A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC38059 RELATED DB: TARGETDB
DBREF 3LUY A 2 326 UNP A1A2B5 A1A2B5_BIFAA 2 326
SEQADV 3LUY SER A -2 UNP A1A2B5 EXPRESSION TAG
SEQADV 3LUY ASN A -1 UNP A1A2B5 EXPRESSION TAG
SEQADV 3LUY ALA A 0 UNP A1A2B5 EXPRESSION TAG
SEQADV 3LUY MSE A 1 UNP A1A2B5 EXPRESSION TAG
SEQRES 1 A 329 SER ASN ALA MSE SER ALA ARG LYS LEU PHE TYR LEU GLY
SEQRES 2 A 329 PRO GLN GLY THR PHE THR HIS GLN ALA ALA VAL ASN ALA
SEQRES 3 A 329 ALA GLN GLU LEU ALA ARG PHE GLU PRO GLN GLY PHE ASP
SEQRES 4 A 329 LEU MSE PRO MSE ASP ASP VAL PRO GLN ILE LEU ASP ALA
SEQRES 5 A 329 ALA GLN HIS GLY ASP GLY TRP GLY ILE VAL ALA TRP GLU
SEQRES 6 A 329 ASN ASN VAL GLU GLY TYR VAL VAL PRO ASN LEU ASP ALA
SEQRES 7 A 329 LEU ILE ASP ALA LYS ASP LEU VAL GLY PHE ALA ARG VAL
SEQRES 8 A 329 GLY VAL ASN VAL GLU PHE ASP ALA TYR VAL ALA GLN GLY
SEQRES 9 A 329 ALA ASP PRO ALA GLU ALA ARG ILE ALA THR ALA HIS PRO
SEQRES 10 A 329 HIS GLY LEU ALA GLN CYS LYS ARG PHE ILE ALA GLU HIS
SEQRES 11 A 329 ARG LEU SER THR GLN PRO ALA THR SER ASN ALA ALA ALA
SEQRES 12 A 329 CYS ARG ASP LEU ILE PRO GLY GLU ILE ALA PHE GLY PRO
SEQRES 13 A 329 ALA ILE CYS GLY GLU LEU TYR ASP ILE THR ARG ILE GLY
SEQRES 14 A 329 THR ALA ILE GLN ASP TYR GLN GLY ALA ALA THR ASP PHE
SEQRES 15 A 329 LEU VAL LEU SER PRO ARG ALA GLU VAL ALA ARG LEU LEU
SEQRES 16 A 329 ALA LYS PRO ARG ALA GLU ALA ASN VAL GLU TYR GLU SER
SEQRES 17 A 329 VAL LEU THR LEU ILE PRO LEU VAL THR GLY PRO GLY VAL
SEQRES 18 A 329 LEU ALA ASN LEU LEU ASP VAL PHE ARG ASP ALA GLY LEU
SEQRES 19 A 329 ASN MSE THR SER PHE ILE SER ARG PRO ILE LYS GLY ARG
SEQRES 20 A 329 THR GLY THR TYR SER PHE ILE VAL THR LEU ASP ALA ALA
SEQRES 21 A 329 PRO TRP GLU GLU ARG PHE ARG ASP ALA LEU VAL GLU ILE
SEQRES 22 A 329 ALA GLU HIS GLY ASP TRP ALA LYS THR LEU ALA VAL TYR
SEQRES 23 A 329 PRO ARG ARG GLU HIS PRO ASN PRO PRO VAL THR SER TRP
SEQRES 24 A 329 MSE LEU PRO GLN GLY GLY VAL ARG LEU ASP ASP SER HIS
SEQRES 25 A 329 LEU PRO ASP ASP TRP GLN ASN ASP GLU THR VAL ARG ARG
SEQRES 26 A 329 GLU LEU MSE TRP
MODRES 3LUY MSE A 1 MET SELENOMETHIONINE
MODRES 3LUY MSE A 38 MET SELENOMETHIONINE
MODRES 3LUY MSE A 40 MET SELENOMETHIONINE
MODRES 3LUY MSE A 233 MET SELENOMETHIONINE
MODRES 3LUY MSE A 297 MET SELENOMETHIONINE
MODRES 3LUY MSE A 325 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 38 8
HET MSE A 40 8
HET MSE A 233 8
HET MSE A 297 8
HET MSE A 325 8
HET PPY A 501 12
HETNAM MSE SELENOMETHIONINE
HETNAM PPY 3-PHENYLPYRUVIC ACID
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 PPY C9 H8 O3
FORMUL 3 HOH *138(H2 O)
HELIX 1 1 THR A 14 LEU A 27 1 14
HELIX 2 2 ALA A 28 GLU A 31 5 4
HELIX 3 3 ASP A 42 GLY A 53 1 12
HELIX 4 4 VAL A 69 ASP A 78 1 10
HELIX 5 5 ASP A 103 ALA A 107 5 5
HELIX 6 6 HIS A 113 CYS A 120 1 8
HELIX 7 7 CYS A 120 HIS A 127 1 8
HELIX 8 8 SER A 136 ASP A 143 1 8
HELIX 9 9 ILE A 155 TYR A 160 1 6
HELIX 10 10 PRO A 184 LEU A 192 1 9
HELIX 11 11 LEU A 192 GLU A 198 1 7
HELIX 12 12 GLY A 217 ALA A 229 1 13
HELIX 13 13 GLU A 260 HIS A 273 1 14
HELIX 14 14 PRO A 292 TRP A 296 5 5
HELIX 15 15 ASP A 313 ASN A 316 5 4
HELIX 16 16 ASP A 317 MSE A 325 1 9
SHEET 1 A 4 PHE A 35 MSE A 40 0
SHEET 2 A 4 ARG A 4 LEU A 9 1 N ARG A 4 O ASP A 36
SHEET 3 A 4 TRP A 56 ASN A 63 1 O TRP A 56 N PHE A 7
SHEET 4 A 4 GLY A 67 TYR A 68 -1 O GLY A 67 N ASN A 63
SHEET 1 B 5 PHE A 35 MSE A 40 0
SHEET 2 B 5 ARG A 4 LEU A 9 1 N ARG A 4 O ASP A 36
SHEET 3 B 5 TRP A 56 ASN A 63 1 O TRP A 56 N PHE A 7
SHEET 4 B 5 ALA A 176 SER A 183 -1 O ASP A 178 N GLU A 62
SHEET 5 B 5 VAL A 83 ASN A 91 -1 N PHE A 85 O VAL A 181
SHEET 1 C 5 SER A 130 PRO A 133 0
SHEET 2 C 5 ILE A 109 ALA A 112 1 N ALA A 110 O GLN A 132
SHEET 3 C 5 GLU A 148 GLY A 152 1 O ILE A 149 N ILE A 109
SHEET 4 C 5 ASP A 95 ALA A 99 -1 N ASP A 95 O GLY A 152
SHEET 5 C 5 ILE A 162 GLY A 166 -1 O THR A 163 N VAL A 98
SHEET 1 D 4 MSE A 233 ILE A 241 0
SHEET 2 D 4 ARG A 244 LEU A 254 -1 O THR A 253 N THR A 234
SHEET 3 D 4 TYR A 203 ILE A 210 -1 N LEU A 207 O VAL A 252
SHEET 4 D 4 TRP A 276 PRO A 284 -1 O TRP A 276 N ILE A 210
LINK C MSE A 1 N SER A 2 1555 1555 1.34
LINK C LEU A 37 N MSE A 38 1555 1555 1.34
LINK C MSE A 38 N PRO A 39 1555 1555 1.35
LINK C PRO A 39 N MSE A 40 1555 1555 1.33
LINK C MSE A 40 N ASP A 41 1555 1555 1.32
LINK C ASN A 232 N MSE A 233 1555 1555 1.32
LINK C MSE A 233 N THR A 234 1555 1555 1.33
LINK C TRP A 296 N MSE A 297 1555 1555 1.31
LINK C MSE A 297 N LEU A 298 1555 1555 1.32
LINK C LEU A 324 N MSE A 325 1555 1555 1.34
LINK C MSE A 325 N TRP A 326 1555 1555 1.33
CISPEP 1 GLY A 10 PRO A 11 0 5.47
SITE 1 AC1 13 GLY A 215 GLY A 217 VAL A 218 LEU A 219
SITE 2 AC1 13 ASN A 232 MSE A 233 THR A 234 SER A 235
SITE 3 AC1 13 TYR A 248 PHE A 250 HOH A 327 HOH A 403
SITE 4 AC1 13 HOH A 404
CRYST1 99.954 59.198 63.172 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 0.010005 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015830 0.00000
HETATM 1 N MSE A 1 67.554 22.000 -3.512 1.00 56.44 N
HETATM 2 CA MSE A 1 66.734 20.782 -3.797 1.00 57.42 C
HETATM 3 C MSE A 1 67.512 19.664 -4.510 1.00 55.57 C
HETATM 4 O MSE A 1 66.997 18.544 -4.655 1.00 56.11 O
HETATM 5 CB MSE A 1 65.533 21.152 -4.671 1.00 58.64 C
HETATM 6 CG MSE A 1 64.317 20.247 -4.457 1.00 64.40 C
HETATM 7 SE MSE A 1 62.677 20.656 -5.538 1.00 81.22 SE
HETATM 8 CE MSE A 1 62.644 22.664 -5.665 1.00 75.69 C
(ATOM LINES ARE NOT SHOWN.)
END
