HEADER TRANSFERASE 15-JUL-10 3NYS
TITLE X-RAY STRUCTURE OF THE K185A MUTANT OF WBPE (WLBE) FROM PSEUDOMONAS
TITLE 2 AERUGINOSA IN COMPLEX WITH PLP AT 1.45 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOTRANSFERASE WBPE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: PA3155, WBPE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RESETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET31
KEYWDS AMINOTRANSFERASE, PLP BINDING, NUCLEOTIDE-SUGAR BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.M.HOLDEN,J.B.THODEN
REVDAT 4 06-SEP-23 3NYS 1 REMARK SEQADV LINK
REVDAT 3 29-MAR-17 3NYS 1 JRNL
REVDAT 2 11-JAN-17 3NYS 1 JRNL VERSN
REVDAT 1 28-JUL-10 3NYS 0
JRNL AUTH G.T.DOW,M.GILBERT,J.B.THODEN,H.M.HOLDEN
JRNL TITL STRUCTURAL INVESTIGATION ON WLARG FROM CAMPYLOBACTER JEJUNI:
JRNL TITL 2 A SUGAR AMINOTRANSFERASE.
JRNL REF PROTEIN SCI. V. 26 586 2017
JRNL REFN ISSN 0961-8368
JRNL PMID 28028852
JRNL DOI 10.1002/PRO.3109
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 59196
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3163
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4103
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 207
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2729
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 485
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.070
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.148
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2809 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3824 ; 2.003 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 362 ; 6.320 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 117 ;32.588 ;24.615
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 467 ;12.307 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.877 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 444 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2115 ; 0.010 ; 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): 1796 ; 1.598 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2901 ; 2.405 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1013 ; 3.611 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 921 ; 5.312 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 3NYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060448.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MONDEL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62362
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : 0.32000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 3FRK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PENTAERYTHRITROL PROPOXYLATE, 100
REMARK 280 MM MES, PH 6, 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 28.39150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.78500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.39150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.78500
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: 5330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 -23.50771
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -69.51315
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 NA NA A 369 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 577 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 579 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 635 LIES ON A SPECIAL POSITION.
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 LEU A 360
REMARK 465 GLU A 361
REMARK 465 HIS A 362
REMARK 465 HIS A 363
REMARK 465 HIS A 364
REMARK 465 HIS A 365
REMARK 465 HIS A 366
REMARK 465 HIS A 367
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 ASN A 359 CG OD1 ND2
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 O ASP A 6 O HOH A 550 1.91
REMARK 500 O HOH A 706 O HOH A 722 1.99
REMARK 500 O HOH A 423 O HOH A 706 2.00
REMARK 500 O HOH A 445 O HOH A 446 2.06
REMARK 500 O HOH A 406 O HOH A 776 2.06
REMARK 500 O HOH A 467 O HOH A 682 2.07
REMARK 500 O HOH A 471 O HOH A 800 2.08
REMARK 500 O HOH A 685 O HOH A 807 2.09
REMARK 500 O HOH A 614 O HOH A 854 2.09
REMARK 500 O HOH A 709 O HOH A 804 2.14
REMARK 500 O HOH A 699 O HOH A 754 2.16
REMARK 500 O HOH A 487 O HOH A 795 2.17
REMARK 500 O HOH A 420 O HOH A 809 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 CG MET A 1 O HOH A 458 3455 2.03
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 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 61 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 MET A 341 CG - SD - CE ANGL. DEV. = -12.8 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 ALA A 157 31.14 -98.59
REMARK 500 CYS A 171 -2.84 90.11
REMARK 500 CYS A 189 -165.82 -101.23
REMARK 500 TYR A 219 -5.43 78.84
REMARK 500
REMARK 500 REMARK: NULL
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 369 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 564 O
REMARK 620 2 HOH A 592 O 91.9
REMARK 620 3 HOH A 818 O 91.0 88.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 369
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NYT RELATED DB: PDB
REMARK 900 SAME PROTEIN, K185A MUTATION, PLP:UDP-3-AMINO-2-N-ACETYLGLUCURONIC
REMARK 900 ACID ALDIMINE
REMARK 900 RELATED ID: 3NYU RELATED DB: PDB
REMARK 900 SAME PROTEIN, WITH PLP INTERNAL ALDIMINE ADDUCT
DBREF 3NYS A 1 359 UNP Q9HZ76 Q9HZ76_PSEAE 1 359
SEQADV 3NYS ALA A 185 UNP Q9HZ76 LYS 185 ENGINEERED MUTATION
SEQADV 3NYS LEU A 360 UNP Q9HZ76 EXPRESSION TAG
SEQADV 3NYS GLU A 361 UNP Q9HZ76 EXPRESSION TAG
SEQADV 3NYS HIS A 362 UNP Q9HZ76 EXPRESSION TAG
SEQADV 3NYS HIS A 363 UNP Q9HZ76 EXPRESSION TAG
SEQADV 3NYS HIS A 364 UNP Q9HZ76 EXPRESSION TAG
SEQADV 3NYS HIS A 365 UNP Q9HZ76 EXPRESSION TAG
SEQADV 3NYS HIS A 366 UNP Q9HZ76 EXPRESSION TAG
SEQADV 3NYS HIS A 367 UNP Q9HZ76 EXPRESSION TAG
SEQRES 1 A 367 MET ILE GLU PHE ILE ASP LEU LYS ASN GLN GLN ALA ARG
SEQRES 2 A 367 ILE LYS ASP LYS ILE ASP ALA GLY ILE GLN ARG VAL LEU
SEQRES 3 A 367 ARG HIS GLY GLN TYR ILE LEU GLY PRO GLU VAL THR GLU
SEQRES 4 A 367 LEU GLU ASP ARG LEU ALA ASP PHE VAL GLY ALA LYS TYR
SEQRES 5 A 367 CYS ILE SER CYS ALA ASN GLY THR ASP ALA LEU GLN ILE
SEQRES 6 A 367 VAL GLN MET ALA LEU GLY VAL GLY PRO GLY ASP GLU VAL
SEQRES 7 A 367 ILE THR PRO GLY PHE THR TYR VAL ALA THR ALA GLU THR
SEQRES 8 A 367 VAL ALA LEU LEU GLY ALA LYS PRO VAL TYR VAL ASP ILE
SEQRES 9 A 367 ASP PRO ARG THR TYR ASN LEU ASP PRO GLN LEU LEU GLU
SEQRES 10 A 367 ALA ALA ILE THR PRO ARG THR LYS ALA ILE ILE PRO VAL
SEQRES 11 A 367 SER LEU TYR GLY GLN CYS ALA ASP PHE ASP ALA ILE ASN
SEQRES 12 A 367 ALA ILE ALA SER LYS TYR GLY ILE PRO VAL ILE GLU ASP
SEQRES 13 A 367 ALA ALA GLN SER PHE GLY ALA SER TYR LYS GLY LYS ARG
SEQRES 14 A 367 SER CYS ASN LEU SER THR VAL ALA CYS THR SER PHE PHE
SEQRES 15 A 367 PRO SER ALA PRO LEU GLY CYS TYR GLY ASP GLY GLY ALA
SEQRES 16 A 367 ILE PHE THR ASN ASP ASP GLU LEU ALA THR ALA ILE ARG
SEQRES 17 A 367 GLN ILE ALA ARG HIS GLY GLN ASP ARG ARG TYR HIS HIS
SEQRES 18 A 367 ILE ARG VAL GLY VAL ASN SER ARG LEU ASP THR LEU GLN
SEQRES 19 A 367 ALA ALA ILE LEU LEU PRO LYS LEU GLU ILE PHE GLU GLU
SEQRES 20 A 367 GLU ILE ALA LEU ARG GLN LYS VAL ALA ALA GLU TYR ASP
SEQRES 21 A 367 LEU SER LEU LYS GLN VAL GLY ILE GLY THR PRO PHE ILE
SEQRES 22 A 367 GLU VAL ASN ASN ILE SER VAL TYR ALA GLN TYR THR VAL
SEQRES 23 A 367 ARG MET ASP ASN ARG GLU SER VAL GLN ALA SER LEU LYS
SEQRES 24 A 367 ALA ALA GLY VAL PRO THR ALA VAL HIS TYR PRO ILE PRO
SEQRES 25 A 367 LEU ASN LYS GLN PRO ALA VAL ALA ASP GLU LYS ALA LYS
SEQRES 26 A 367 LEU PRO VAL GLY ASP LYS ALA ALA THR GLN VAL MET SER
SEQRES 27 A 367 LEU PRO MET HIS PRO TYR LEU ASP THR ALA SER ILE LYS
SEQRES 28 A 367 ILE ILE CYS ALA ALA LEU THR ASN LEU GLU HIS HIS HIS
SEQRES 29 A 367 HIS HIS HIS
HET PLP A 368 16
HET NA A 369 1
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM NA SODIUM ION
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 PLP C8 H10 N O6 P
FORMUL 3 NA NA 1+
FORMUL 4 HOH *485(H2 O)
HELIX 1 1 LEU A 7 ILE A 14 1 8
HELIX 2 2 ILE A 14 GLY A 29 1 16
HELIX 3 3 GLY A 34 GLY A 49 1 16
HELIX 4 4 ASN A 58 LEU A 70 1 13
HELIX 5 5 VAL A 86 LEU A 95 1 10
HELIX 6 6 ASP A 112 ILE A 120 5 9
HELIX 7 7 SER A 131 GLN A 135 5 5
HELIX 8 8 ASP A 138 TYR A 149 1 12
HELIX 9 9 ASP A 200 ALA A 211 1 12
HELIX 10 10 ASP A 231 ILE A 244 1 14
HELIX 11 11 ILE A 244 VAL A 266 1 23
HELIX 12 12 ASN A 290 GLY A 302 1 13
HELIX 13 13 PRO A 312 ALA A 320 5 9
HELIX 14 14 LEU A 326 GLN A 335 1 10
HELIX 15 15 ASP A 346 ASN A 359 1 14
SHEET 1 A 4 TYR A 52 CYS A 56 0
SHEET 2 A 4 GLY A 194 THR A 198 -1 O ILE A 196 N ILE A 54
SHEET 3 A 4 VAL A 176 SER A 180 -1 N THR A 179 O ALA A 195
SHEET 4 A 4 ILE A 154 ASP A 156 1 N GLU A 155 O CYS A 178
SHEET 1 B 3 LYS A 98 VAL A 102 0
SHEET 2 B 3 GLU A 77 PRO A 81 1 N THR A 80 O VAL A 100
SHEET 3 B 3 THR A 124 ILE A 127 1 O LYS A 125 N GLU A 77
SHEET 1 C 3 LYS A 168 ARG A 169 0
SHEET 2 C 3 SER A 164 TYR A 165 -1 N TYR A 165 O LYS A 168
SHEET 3 C 3 ASN A 277 ILE A 278 -1 O ILE A 278 N SER A 164
SHEET 1 D 2 GLN A 215 ARG A 217 0
SHEET 2 D 2 HIS A 220 HIS A 221 -1 O HIS A 220 N ARG A 217
SHEET 1 E 2 TYR A 284 ARG A 287 0
SHEET 2 E 2 VAL A 336 LEU A 339 -1 O MET A 337 N VAL A 286
LINK NA NA A 369 O HOH A 564 1555 1555 2.06
LINK NA NA A 369 O HOH A 592 1555 1555 2.06
LINK NA NA A 369 O HOH A 818 1555 1555 2.10
CISPEP 1 HIS A 308 TYR A 309 0 14.90
SITE 1 AC1 18 ASN A 58 GLY A 59 THR A 60 THR A 84
SITE 2 AC1 18 TYR A 85 ALA A 87 VAL A 130 ASP A 156
SITE 3 AC1 18 ALA A 158 GLN A 159 SER A 180 ASN A 227
SITE 4 AC1 18 TYR A 309 HOH A 374 HOH A 506 HOH A 584
SITE 5 AC1 18 HOH A 632 HOH A 642
SITE 1 AC2 3 HOH A 564 HOH A 592 HOH A 818
CRYST1 56.783 93.570 77.067 90.00 115.58 90.00 C 1 2 1 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 0.017611 0.000000 0.008430 0.00000
SCALE2 0.000000 0.010687 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014386 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
