HEADER LYASE 21-DEC-17 6FCS
TITLE THE X-RAY STRUCTURE OF LYTIC TRANSGLYCOSYLASE SLT INACTIVE MUTANT
TITLE 2 E503Q FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH NAG-
TITLE 3 NAMPENTAPEPTIDE-NAG-NAMPENTAPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.2.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALA-DGL-API-DAL-DAL;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: SLT, AOY09_04369, PAMH19_2049;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 9 ORGANISM_TAXID: 287;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LYTIC TRANSGLYCOSYLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.T.BATUECAS,T.DOMINGUEZ-GIL,J.A.HERMOSO
REVDAT 6 17-JAN-24 6FCS 1 REMARK
REVDAT 5 15-NOV-23 6FCS 1 LINK ATOM
REVDAT 4 30-MAR-22 6FCS 1 HETSYN LINK
REVDAT 3 29-JUL-20 6FCS 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 02-MAY-18 6FCS 1 JRNL
REVDAT 1 18-APR-18 6FCS 0
JRNL AUTH M.LEE,M.T.BATUECAS,S.TOMOSHIGE,T.DOMINGUEZ-GIL,
JRNL AUTH 2 K.V.MAHASENAN,D.A.DIK,D.HESEK,C.MILLAN,I.USON,E.LASTOCHKIN,
JRNL AUTH 3 J.A.HERMOSO,S.MOBASHERY
JRNL TITL EXOLYTIC AND ENDOLYTIC TURNOVER OF PEPTIDOGLYCAN BY LYTIC
JRNL TITL 2 TRANSGLYCOSYLASE SLT OFPSEUDOMONAS AERUGINOSA.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 4393 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29632171
JRNL DOI 10.1073/PNAS.1801298115
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 144.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 18599
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 972
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1387
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5008
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 143
REMARK 3 SOLVENT ATOMS : 54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.39000
REMARK 3 B22 (A**2) : -1.39000
REMARK 3 B33 (A**2) : 4.52000
REMARK 3 B12 (A**2) : -0.70000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.420
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.381
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.977
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5281 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4838 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7172 ; 1.361 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11152 ; 0.981 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 612 ; 5.858 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 263 ;35.644 ;22.471
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 846 ;18.107 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;17.809 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5833 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1190 ; 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): 2453 ; 2.412 ; 7.422
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2450 ; 2.392 ; 7.420
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3062 ; 3.979 ;11.130
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3063 ; 3.983 ;11.131
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2828 ; 2.481 ; 7.806
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2829 ; 2.481 ; 7.807
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4110 ; 4.290 ;11.596
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5992 ; 7.311 ;86.876
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5992 ; 7.312 ;86.892
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 : NULL
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 6FCS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1200008095.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19575
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 144.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
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 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: 5OHU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 80MM TRIS PH 8.5, 12% PEG 8000 AND
REMARK 280 160MM CALCIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,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 -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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.25450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.25450
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 27.25450
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: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 O HOH A 837 O HOH A 853 1.47
REMARK 500 O HOH A 836 O HOH A 851 1.99
REMARK 500 N ALA A 66 O HOH A 801 2.06
REMARK 500 O HOH A 838 O HOH A 844 2.19
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 A 824 O HOH A 842 6655 1.17
REMARK 500 O HOH A 805 O HOH A 828 6654 1.91
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 ASN A 193 CA ASN A 193 C -0.234
REMARK 500 DAL B 4 C DAL B 5 N 0.148
REMARK 500 DAL B 5 C DAL B 5 OXT 0.203
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 42 96.20 -56.97
REMARK 500 LYS A 43 80.15 60.35
REMARK 500 HIS A 139 35.29 -140.13
REMARK 500 ASP A 301 64.55 -152.26
REMARK 500 ASN A 391 94.19 -64.69
REMARK 500 ALA A 477 119.37 -20.05
REMARK 500 ARG A 511 116.79 -160.38
REMARK 500 ARG A 591 114.37 -161.30
REMARK 500 ASN A 626 57.23 31.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 6FCS A 30 642 UNP A0A069QJX4_PSEAI
DBREF2 6FCS A A0A069QJX4 30 642
DBREF 6FCS B 1 5 PDB 6FCS 6FCS 1 5
SEQADV 6FCS GLN A 503 UNP A0A069QJX GLU 503 ENGINEERED MUTATION
SEQRES 1 A 613 GLN ARG ARG LEU TYR ASP GLN ALA LYS ALA ALA LEU ALA
SEQRES 2 A 613 LYS GLY ASN SER ALA PRO TYR MET ALA SER ARG SER ALA
SEQRES 3 A 613 LEU ARG ASP TYR PRO LEU GLU PRO TYR LEU ALA TYR ASP
SEQRES 4 A 613 GLU LEU THR HIS ARG LEU LYS SER ALA SER ASN GLU GLU
SEQRES 5 A 613 VAL GLU ARG PHE LEU THR GLU HIS GLY ASP LEU PRO GLN
SEQRES 6 A 613 ILE GLY TRP LEU LYS LEU ARG TRP LEU ARG LEU LEU ALA
SEQRES 7 A 613 ASP ARG GLY ASP TRP LYS THR PHE VAL ASN TYR TYR ASP
SEQRES 8 A 613 PRO LYS LEU ASN PHE THR GLU LEU ASP CYS LEU TYR GLY
SEQRES 9 A 613 GLN TYR GLN LEU GLY HIS GLY GLN LYS ALA GLU GLY TYR
SEQRES 10 A 613 ALA THR SER GLU ARG LEU TRP LEU VAL GLY LYS SER GLN
SEQRES 11 A 613 PRO ALA ALA CYS ASP THR LEU PHE GLY LEU TRP GLN GLY
SEQRES 12 A 613 GLU GLY GLN LEU THR GLU GLU LYS VAL TRP LYS ARG LEU
SEQRES 13 A 613 LYS LEU ALA ALA GLU ALA ARG ASN TYR SER LEU ALA SER
SEQRES 14 A 613 HIS LEU ALA GLN ARG LEU PRO THR LEU GLY ASN GLN GLY
SEQRES 15 A 613 ALA LEU MET VAL SER VAL ALA GLN ASN PRO ALA GLN LEU
SEQRES 16 A 613 SER GLN THR GLY ARG PHE SER GLN ARG ASP HIS ALA THR
SEQRES 17 A 613 ALA ASP VAL VAL GLY LEU GLY LEU ARG ARG LEU ALA ARG
SEQRES 18 A 613 GLN ASP PRO GLU LYS ALA LEU SER LEU LEU ASP TYR TYR
SEQRES 19 A 613 SER SER ALA LEU PRO PHE SER SER ASP GLU LYS VAL ALA
SEQRES 20 A 613 ILE ALA ARG GLU ILE GLY LEU SER LEU ALA LYS ARG PHE
SEQRES 21 A 613 ASP PRO ARG ALA LEU PRO LEU MET THR GLN TYR ASP PRO
SEQRES 22 A 613 GLY LEU ARG ASP ASN THR VAL THR GLU TRP ARG THR ARG
SEQRES 23 A 613 LEU LEU LEU ARG LEU GLY ARG TRP ASP GLU ALA TYR ALA
SEQRES 24 A 613 LEU THR ARG LYS LEU PRO GLN ASP LEU ALA ALA THR SER
SEQRES 25 A 613 ARG TRP ARG TYR TRP GLN ALA ARG SER LEU GLN LEU ALA
SEQRES 26 A 613 GLN PRO ASN SER LYS GLU PRO ILE ALA LEU TYR GLN LYS
SEQRES 27 A 613 LEU ALA GLY GLU ARG ASP PHE TYR GLY PHE LEU ALA ALA
SEQRES 28 A 613 ASP ARG LEU SER VAL PRO TYR LYS LEU GLY ASN ARG PRO
SEQRES 29 A 613 ALA HIS ILE ASP PRO ARG VAL LEU GLN ARG VAL ARG ASN
SEQRES 30 A 613 ALA ALA SER THR ARG ARG ALA MET GLU PHE PHE ASN ARG
SEQRES 31 A 613 GLY GLU VAL ILE ASN ALA ARG ARG GLU TRP TYR HIS ALA
SEQRES 32 A 613 ALA ARG LEU PHE ASP ARG ASP GLU LEU ILE ALA GLN ALA
SEQRES 33 A 613 ARG LEU ALA TYR ASP MET GLN TRP TYR PHE PRO ALA ILE
SEQRES 34 A 613 ARG SER ILE SER GLN ALA GLN TYR TRP ASP ASP LEU ASP
SEQRES 35 A 613 ILE ARG PHE PRO MET ALA HIS ARG ALA THR LEU VAL ARG
SEQRES 36 A 613 GLU ALA LYS ASN ARG GLY LEU HIS SER SER TRP ILE PHE
SEQRES 37 A 613 ALA ILE THR ARG GLN GLN SER ALA PHE MET SER ASP ALA
SEQRES 38 A 613 ARG SER GLY VAL GLY ALA THR GLY LEU MET GLN LEU MET
SEQRES 39 A 613 PRO GLY THR ALA LYS GLU THR SER ARG LYS PHE GLY ILE
SEQRES 40 A 613 PRO LEU ALA SER THR GLN GLN LEU ILE VAL PRO ASP VAL
SEQRES 41 A 613 ASN ILE ARG LEU GLY ALA ALA TYR LEU SER GLN VAL HIS
SEQRES 42 A 613 SER GLN PHE ASN GLY ASN ARG VAL LEU ALA SER ALA ALA
SEQRES 43 A 613 TYR ASN ALA GLY PRO GLY ARG VAL ARG GLN TRP LEU LYS
SEQRES 44 A 613 ASP THR ARG HIS LEU ALA PHE ASP VAL TRP ILE GLU THR
SEQRES 45 A 613 ILE PRO PHE ASP GLU THR ARG GLN TYR VAL GLN ASN VAL
SEQRES 46 A 613 LEU SER TYR ALA VAL ILE TYR GLY GLN LYS LEU ASN ALA
SEQRES 47 A 613 PRO GLN PRO ILE VAL ASP TRP HIS GLU ARG TYR PHE ASP
SEQRES 48 A 613 ASP PHE
SEQRES 1 B 5 ALA DGL API DAL DAL
HET DGL B 2 8
HET API B 3 12
HET DAL B 4 5
HET DAL B 5 6
HET MAG C 1 16
HET NAG C 2 14
HET AMU C 3 18
HET NAG C 4 14
HET AMV D 1 20
HET NAG D 2 14
HET NM6 D 3 19
HET NAG D 4 14
HET ACT A 701 4
HET ACT A 702 4
HET 66N A 707 6
HETNAM DGL D-GLUTAMIC ACID
HETNAM API 2,6-DIAMINOPIMELIC ACID
HETNAM DAL D-ALANINE
HETNAM MAG METHYL 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM AMU N-ACETYL-BETA-MURAMIC ACID
HETNAM AMV METHYL 2-ACETAMIDO-3-O-[(1R)-1-CARBOXYETHYL]-2-DEOXY-
HETNAM 2 AMV BETA-D-GLUCOPYRANOSIDE
HETNAM NM6 2-ACETAMIDO-3-O-[(2R)-1-AMINO-1-OXOPROPAN-2-YL]-2-
HETNAM 2 NM6 DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ACT ACETATE ION
HETNAM 66N L-ALANINAMIDE
HETSYN MAG BETA-METHYL-N-ACETYL-D-GLUCOSAMINE; METHYL 2-ACETAMIDO-
HETSYN 2 MAG 2-DEOXY-BETA-D-GLUCOSIDE; METHYL 2-ACETAMIDO-2-DEOXY-
HETSYN 3 MAG D-GLUCOSIDE; METHYL 2-ACETAMIDO-2-DEOXY-GLUCOSIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN AMU N-ACETYL-MURAMIC ACID; BETA-N-ACETYLMURAMIC ACID
HETSYN AMV METHYL 2-(ACETYLAMINO)-3-O-[(1R)-1-CARBOXYETHYL]-2-
HETSYN 2 AMV DEOXY-BETA-D-GLUCOPYRANOSIDE; METHYL 2-ACETAMIDO-3-O-
HETSYN 3 AMV [(1R)-1-CARBOXYETHYL]-2-DEOXY-BETA-D-GLUCOSIDE; METHYL
HETSYN 4 AMV 2-ACETAMIDO-3-O-[(1R)-1-CARBOXYETHYL]-2-DEOXY-D-
HETSYN 5 AMV GLUCOSIDE; METHYL 2-ACETAMIDO-3-O-[(1R)-1-
HETSYN 6 AMV CARBOXYETHYL]-2-DEOXY-GLUCOSIDE
HETSYN NM6 (2R)-2-[(2R,3S,4R,5R,6R)-5-ACETAMIDO-2-(HYDROXYMETHYL)-
HETSYN 2 NM6 3,6-BIS(OXIDANYL)OXAN-4-YL]OXYPROPANAMIDE; N-ACETYL-3-
HETSYN 3 NM6 O-[(2R)-1-AMINO-1-OXOPROPAN-2-YL]-BETA-D-GLUCOSAMINE;
HETSYN 4 NM6 2-ACETAMIDO-3-O-[(2R)-1-AMINO-1-OXOPROPAN-2-YL]-2-
HETSYN 5 NM6 DEOXY-BETA-D-GLUCOSE; 2-ACETAMIDO-3-O-[(2R)-1-AMINO-1-
HETSYN 6 NM6 OXOPROPAN-2-YL]-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-3-O-
HETSYN 7 NM6 [(2R)-1-AMINO-1-OXOPROPAN-2-YL]-2-DEOXY-GLUCOSE
FORMUL 2 DGL C5 H9 N O4
FORMUL 2 API C7 H14 N2 O4
FORMUL 2 DAL 2(C3 H7 N O2)
FORMUL 3 MAG C9 H17 N O6
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 AMU C11 H19 N O8
FORMUL 4 AMV C12 H21 N O8
FORMUL 4 NM6 C11 H20 N2 O7
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 7 66N C3 H8 N2 O
FORMUL 8 HOH *54(H2 O)
HELIX 1 AA1 TYR A 34 ALA A 42 1 9
HELIX 2 AA2 SER A 46 ARG A 57 1 12
HELIX 3 AA3 LEU A 61 ARG A 73 1 13
HELIX 4 AA4 SER A 78 GLY A 90 1 13
HELIX 5 AA5 GLN A 94 ARG A 109 1 16
HELIX 6 AA6 ASP A 111 TYR A 119 1 9
HELIX 7 AA7 ASP A 120 ASN A 124 5 5
HELIX 8 AA8 PHE A 125 GLY A 138 1 14
HELIX 9 AA9 GLN A 141 LEU A 154 1 14
HELIX 10 AB1 PRO A 160 GLU A 173 1 14
HELIX 11 AB2 THR A 177 ARG A 192 1 16
HELIX 12 AB3 ASN A 193 GLN A 202 1 10
HELIX 13 AB4 LEU A 207 ASN A 220 1 14
HELIX 14 AB5 PRO A 221 SER A 231 5 11
HELIX 15 AB6 ASP A 234 ASP A 252 1 19
HELIX 16 AB7 ASP A 252 LEU A 267 1 16
HELIX 17 AB8 SER A 270 ARG A 288 1 19
HELIX 18 AB9 PHE A 289 PRO A 291 5 3
HELIX 19 AC1 ARG A 292 ASP A 301 1 10
HELIX 20 AC2 ASP A 306 GLY A 321 1 16
HELIX 21 AC3 ARG A 322 LYS A 332 1 11
HELIX 22 AC4 PRO A 334 ALA A 339 1 6
HELIX 23 AC5 THR A 340 GLN A 355 1 16
HELIX 24 AC6 LYS A 359 ALA A 369 1 11
HELIX 25 AC7 ASP A 373 SER A 384 1 12
HELIX 26 AC8 ASP A 397 ALA A 407 1 11
HELIX 27 AC9 ALA A 407 GLY A 420 1 14
HELIX 28 AD1 GLU A 421 ARG A 434 1 14
HELIX 29 AD2 ASP A 437 ASP A 450 1 14
HELIX 30 AD3 TRP A 453 GLN A 465 1 13
HELIX 31 AD4 ASP A 469 PHE A 474 1 6
HELIX 32 AD5 HIS A 478 ARG A 489 1 12
HELIX 33 AD6 HIS A 492 SER A 504 1 13
HELIX 34 AD7 MET A 523 PHE A 534 1 12
HELIX 35 AD8 SER A 540 ILE A 545 5 6
HELIX 36 AD9 VAL A 546 PHE A 565 1 20
HELIX 37 AE1 ASN A 568 GLY A 579 1 12
HELIX 38 AE2 GLY A 579 TRP A 586 1 8
HELIX 39 AE3 PHE A 595 THR A 601 1 7
HELIX 40 AE4 PHE A 604 LEU A 625 1 22
HELIX 41 AE5 ASP A 633 GLU A 636 5 4
SHEET 1 AA1 2 LEU A 593 ALA A 594 0
SHEET 2 AA1 2 TYR A 638 PHE A 639 -1 O PHE A 639 N LEU A 593
SSBOND 1 CYS A 130 CYS A 163 1555 1555 2.03
LINK N11 66N A 707 C10 AMU C 3 1555 1555 1.48
LINK C ALA B 1 N DGL B 2 1555 1555 1.46
LINK N ALA B 1 C10 AMV D 1 1555 1555 1.47
LINK CD DGL B 2 N API B 3 1555 1555 1.47
LINK C API B 3 N DAL B 4 1555 1555 1.47
LINK C DAL B 4 N DAL B 5 1555 1555 1.48
LINK O4 MAG C 1 C1 NAG C 2 1555 1555 1.43
LINK O4 NAG C 2 C1 AMU C 3 1555 1555 1.40
LINK O4 AMU C 3 C1 NAG C 4 1555 1555 1.42
LINK O4 AMV D 1 C1 NAG D 2 1555 1555 1.42
LINK O4 NAG D 2 C1 NM6 D 3 1555 1555 1.41
LINK O4 NM6 D 3 C1 NAG D 4 1555 1555 1.42
CRYST1 166.873 166.873 54.509 90.00 90.00 120.00 P 63 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 0.005993 0.003460 0.000000 0.00000
SCALE2 0.000000 0.006920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
