HEADER LIGASE 11-DEC-09 3L1A
TITLE STRUCTURAL ORDERING OF DISORDERED LIGAND BINDING LOOPS OF BIOTIN
TITLE 2 PROTEIN LIGASE INTO ACTIVE CONFORMATIONS AS A CONSEQUENCE OF
TITLE 3 DEHYDRATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIRA BIFUNCTIONAL PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BIOTIN PROTEIN LIGASE;
COMPND 5 EC: 6.3.4.15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: BIRA, MT3379, RV3279C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PASK-IBA43PLUS
KEYWDS BIOTIN PROTEIN LIGASE, DEHYDRATED CRYSTALS, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.GUPTA
REVDAT 2 01-NOV-23 3L1A 1 REMARK
REVDAT 1 09-MAR-10 3L1A 0
JRNL AUTH V.GUPTA,R.K.GUPTA,G.KHARE,D.M.SALUNKE,A.SUROLIA,A.K.TYAGI
JRNL TITL STRUCTURAL ORDERING OF DISORDERED LIGAND-BINDING LOOPS OF
JRNL TITL 2 BIOTIN PROTEIN LIGASE INTO ACTIVE CONFORMATIONS AS A
JRNL TITL 3 CONSEQUENCE OF DEHYDRATION.
JRNL REF PLOS ONE V. 5 E9222 2010
JRNL REFN ESSN 1932-6203
JRNL PMID 20169168
JRNL DOI 10.1371/JOURNAL.PONE.0009222
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 11423
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.313
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1145
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 23.9898 - 5.3624 0.98 1362 152 0.2143 0.2363
REMARK 3 2 5.3624 - 4.2641 1.00 1297 146 0.1869 0.2626
REMARK 3 3 4.2641 - 3.7274 1.00 1305 140 0.2198 0.3087
REMARK 3 4 3.7274 - 3.3876 1.00 1277 144 0.2256 0.3431
REMARK 3 5 3.3876 - 3.1454 1.00 1272 139 0.2359 0.3242
REMARK 3 6 3.1454 - 2.9603 0.99 1265 145 0.2714 0.3788
REMARK 3 7 2.9603 - 2.8123 0.99 1255 134 0.2747 0.3748
REMARK 3 8 2.8123 - 2.6900 0.99 1245 145 0.2664 0.3744
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 43.11
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.790
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.34940
REMARK 3 B22 (A**2) : 5.75590
REMARK 3 B33 (A**2) : -2.40650
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 3643
REMARK 3 ANGLE : 1.353 4982
REMARK 3 CHIRALITY : 0.087 604
REMARK 3 PLANARITY : 0.006 660
REMARK 3 DIHEDRAL : 17.810 1296
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 46:57 OR RESSEQ
REMARK 3 80:114 OR RESSEQ 125:143 OR RESSEQ 153:
REMARK 3 159 OR RESSEQ 180:221 OR RESSEQ 237:247 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 46:57 OR RESSEQ
REMARK 3 80:114 OR RESSEQ 125:143 OR RESSEQ 153:
REMARK 3 159 OR RESSEQ 180:221 OR RESSEQ 237:247 )
REMARK 3 ATOM PAIRS NUMBER : 926
REMARK 3 RMSD : 0.092
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3L1A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056706.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOMAR
REMARK 200 DATA SCALING SOFTWARE : AUTOMAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13250
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690
REMARK 200 RESOLUTION RANGE LOW (A) : 23.989
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.25
REMARK 200 R MERGE FOR SHELL (I) : 0.34900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (AUTOMR)
REMARK 200 STARTING MODEL: 2CGH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-16% PEG 4000, PEG 8000, 0.1M HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.96650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.77700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.90100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.77700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.96650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.90100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 A 1
REMARK 465 THR A 2
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASP B 3
REMARK 465 ARG B 4
REMARK 465 ASP B 5
REMARK 465 ARG B 6
REMARK 465 LEU B 7
REMARK 465 ARG B 8
REMARK 465 PRO B 9
REMARK 465 PRO B 10
REMARK 465 LEU B 11
REMARK 465 ASP B 12
REMARK 465 GLU B 13
REMARK 465 ARG B 14
REMARK 465 SER B 15
REMARK 465 LEU B 16
REMARK 465 ARG B 17
REMARK 465 ASP B 18
REMARK 465 GLN B 19
REMARK 465 GLU B 61
REMARK 465 HIS B 62
REMARK 465 GLN B 63
REMARK 465 THR B 64
REMARK 465 ALA B 65
REMARK 465 GLY B 66
REMARK 465 ARG B 67
REMARK 465 GLY B 68
REMARK 465 ARG B 69
REMARK 465 HIS B 70
REMARK 465 GLY B 71
REMARK 465 ARG B 72
REMARK 465 GLY B 73
REMARK 465 TRP B 74
REMARK 465 ALA B 75
REMARK 465 ALA B 76
REMARK 465 THR B 77
REMARK 465 ALA B 78
REMARK 465 ARG B 79
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 ARG A 4 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 6 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 7 CG CD1 CD2
REMARK 470 ARG A 14 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 67 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 161 CG CD OE1 NE2
REMARK 470 LEU A 176 CG CD1 CD2
REMARK 470 GLN A 207 CG CD OE1 NE2
REMARK 470 LEU B 30 CG CD1 CD2
REMARK 470 ARG B 135 CD NE CZ NH1 NH2
REMARK 470 ARG B 192 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 253 CG CD NE CZ NH1 NH2
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 A 38 O ARG A 67 1.47
REMARK 500 O SER B 25 OE1 GLU B 195 1.65
REMARK 500 O THR A 64 O TRP A 74 1.85
REMARK 500 CB SER A 38 O ARG A 67 1.97
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 LEU A 265 O GLN B 35 2444 2.17
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 GLU A 164 CD GLU A 164 OE2 0.076
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 PRO A 10 C - N - CD ANGL. DEV. = -18.2 DEGREES
REMARK 500 PRO A 163 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG B 238 NE - CZ - NH1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG B 238 NE - CZ - NH2 ANGL. DEV. = 6.3 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 ASP A 5 144.08 168.98
REMARK 500 ARG A 6 -169.13 167.04
REMARK 500 LEU A 7 -139.40 70.51
REMARK 500 ARG A 8 150.38 94.09
REMARK 500 ALA A 23 -125.95 42.09
REMARK 500 ARG A 67 -166.84 177.67
REMARK 500 ARG A 69 93.79 -21.72
REMARK 500 HIS A 70 138.89 84.75
REMARK 500 ARG A 72 -145.30 -84.75
REMARK 500 ALA A 76 -156.97 -133.77
REMARK 500 ALA A 122 -124.25 -57.26
REMARK 500 ALA A 147 75.44 -155.03
REMARK 500 GLN A 148 134.91 -33.34
REMARK 500 PRO A 149 31.46 -91.58
REMARK 500 GLN A 161 -88.08 175.27
REMARK 500 GLU A 165 74.24 -156.29
REMARK 500 VAL A 166 -42.00 -175.01
REMARK 500 ASP A 167 21.17 85.99
REMARK 500 ASP A 169 18.29 -156.89
REMARK 500 ALA A 170 -176.46 -63.74
REMARK 500 ALA A 180 59.20 -142.53
REMARK 500 PRO A 228 128.74 -34.14
REMARK 500 ASP A 239 173.70 173.89
REMARK 500 ALA B 23 63.99 -162.96
REMARK 500 TRP B 27 176.97 49.66
REMARK 500 ARG B 28 -9.89 -149.09
REMARK 500 GLN B 35 -83.34 -74.73
REMARK 500 PRO B 115 7.02 -65.49
REMARK 500 ALA B 147 76.17 -155.40
REMARK 500 GLN B 148 125.55 -15.45
REMARK 500 GLN B 161 -155.76 -97.74
REMARK 500 PRO B 163 -157.55 -97.82
REMARK 500 GLU B 165 8.27 -154.49
REMARK 500 ASP B 167 45.97 16.35
REMARK 500 ASP B 169 6.62 83.25
REMARK 500 ASP B 242 1.15 -61.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CGH RELATED DB: PDB
REMARK 900 DEHYDRATED STUCTURE OF BIRA FROM M. TUBERCULOSIS
REMARK 900 RELATED ID: 3L2Z RELATED DB: PDB
DBREF 3L1A A 1 266 UNP P96884 P96884_MYCTU 1 266
DBREF 3L1A B 1 266 UNP P96884 P96884_MYCTU 1 266
SEQRES 1 A 266 MET THR ASP ARG ASP ARG LEU ARG PRO PRO LEU ASP GLU
SEQRES 2 A 266 ARG SER LEU ARG ASP GLN LEU ILE GLY ALA GLY SER GLY
SEQRES 3 A 266 TRP ARG GLN LEU ASP VAL VAL ALA GLN THR GLY SER THR
SEQRES 4 A 266 ASN ALA ASP LEU LEU ALA ARG ALA ALA SER GLY ALA ASP
SEQRES 5 A 266 ILE ASP GLY VAL VAL LEU ILE ALA GLU HIS GLN THR ALA
SEQRES 6 A 266 GLY ARG GLY ARG HIS GLY ARG GLY TRP ALA ALA THR ALA
SEQRES 7 A 266 ARG ALA GLN ILE ILE LEU SER VAL GLY VAL ARG VAL VAL
SEQRES 8 A 266 ASP VAL PRO VAL GLN ALA TRP GLY TRP LEU SER LEU ALA
SEQRES 9 A 266 ALA GLY LEU ALA VAL LEU ASP SER VAL ALA PRO LEU ILE
SEQRES 10 A 266 ALA VAL PRO PRO ALA GLU THR GLY LEU LYS TRP PRO ASN
SEQRES 11 A 266 ASP VAL LEU ALA ARG GLY GLY LYS LEU ALA GLY ILE LEU
SEQRES 12 A 266 ALA GLU VAL ALA GLN PRO PHE VAL VAL LEU GLY VAL GLY
SEQRES 13 A 266 LEU ASN VAL THR GLN ALA PRO GLU GLU VAL ASP PRO ASP
SEQRES 14 A 266 ALA THR SER LEU LEU ASP LEU GLY VAL ALA ALA PRO ASP
SEQRES 15 A 266 ARG ASN ARG ILE ALA SER ARG LEU LEU ARG GLU LEU GLU
SEQRES 16 A 266 ALA ARG ILE ILE GLN TRP ARG ASN ALA ASN PRO GLN LEU
SEQRES 17 A 266 ALA ALA ASP TYR ARG ALA ARG SER LEU THR ILE GLY SER
SEQRES 18 A 266 ARG VAL ARG VAL GLU LEU PRO GLY GLY GLN ASP VAL VAL
SEQRES 19 A 266 GLY ILE ALA ARG ASP ILE ASP ASP GLN GLY ARG LEU CYS
SEQRES 20 A 266 LEU ASP VAL GLY GLY ARG THR VAL VAL VAL SER ALA GLY
SEQRES 21 A 266 ASP VAL VAL HIS LEU ARG
SEQRES 1 B 266 MET THR ASP ARG ASP ARG LEU ARG PRO PRO LEU ASP GLU
SEQRES 2 B 266 ARG SER LEU ARG ASP GLN LEU ILE GLY ALA GLY SER GLY
SEQRES 3 B 266 TRP ARG GLN LEU ASP VAL VAL ALA GLN THR GLY SER THR
SEQRES 4 B 266 ASN ALA ASP LEU LEU ALA ARG ALA ALA SER GLY ALA ASP
SEQRES 5 B 266 ILE ASP GLY VAL VAL LEU ILE ALA GLU HIS GLN THR ALA
SEQRES 6 B 266 GLY ARG GLY ARG HIS GLY ARG GLY TRP ALA ALA THR ALA
SEQRES 7 B 266 ARG ALA GLN ILE ILE LEU SER VAL GLY VAL ARG VAL VAL
SEQRES 8 B 266 ASP VAL PRO VAL GLN ALA TRP GLY TRP LEU SER LEU ALA
SEQRES 9 B 266 ALA GLY LEU ALA VAL LEU ASP SER VAL ALA PRO LEU ILE
SEQRES 10 B 266 ALA VAL PRO PRO ALA GLU THR GLY LEU LYS TRP PRO ASN
SEQRES 11 B 266 ASP VAL LEU ALA ARG GLY GLY LYS LEU ALA GLY ILE LEU
SEQRES 12 B 266 ALA GLU VAL ALA GLN PRO PHE VAL VAL LEU GLY VAL GLY
SEQRES 13 B 266 LEU ASN VAL THR GLN ALA PRO GLU GLU VAL ASP PRO ASP
SEQRES 14 B 266 ALA THR SER LEU LEU ASP LEU GLY VAL ALA ALA PRO ASP
SEQRES 15 B 266 ARG ASN ARG ILE ALA SER ARG LEU LEU ARG GLU LEU GLU
SEQRES 16 B 266 ALA ARG ILE ILE GLN TRP ARG ASN ALA ASN PRO GLN LEU
SEQRES 17 B 266 ALA ALA ASP TYR ARG ALA ARG SER LEU THR ILE GLY SER
SEQRES 18 B 266 ARG VAL ARG VAL GLU LEU PRO GLY GLY GLN ASP VAL VAL
SEQRES 19 B 266 GLY ILE ALA ARG ASP ILE ASP ASP GLN GLY ARG LEU CYS
SEQRES 20 B 266 LEU ASP VAL GLY GLY ARG THR VAL VAL VAL SER ALA GLY
SEQRES 21 B 266 ASP VAL VAL HIS LEU ARG
FORMUL 3 HOH *31(H2 O)
HELIX 1 1 ASP A 12 ILE A 21 1 10
HELIX 2 2 SER A 38 SER A 49 1 12
HELIX 3 3 PRO A 94 TRP A 98 5 5
HELIX 4 4 GLY A 99 ALA A 114 1 16
HELIX 5 5 PRO A 115 ILE A 117 5 3
HELIX 6 6 SER A 172 GLY A 177 5 6
HELIX 7 7 ASP A 182 ALA A 204 1 23
HELIX 8 8 ASN A 205 ARG A 215 1 11
HELIX 9 9 SER B 38 SER B 49 1 12
HELIX 10 10 PRO B 94 TRP B 98 5 5
HELIX 11 11 GLY B 99 ALA B 114 1 16
HELIX 12 12 PRO B 115 ILE B 117 5 3
HELIX 13 13 PRO B 120 ALA B 122 5 3
HELIX 14 14 ASP B 182 ALA B 204 1 23
HELIX 15 15 ASN B 205 ARG B 215 1 11
SHEET 1 A 7 GLN A 29 VAL A 33 0
SHEET 2 A 7 VAL A 56 ALA A 60 1 O VAL A 57 N GLN A 29
SHEET 3 A 7 ILE A 82 ARG A 89 -1 O SER A 85 N LEU A 58
SHEET 4 A 7 PHE A 150 LEU A 157 -1 O LEU A 157 N ILE A 82
SHEET 5 A 7 GLY A 137 ALA A 147 -1 N LEU A 143 O GLY A 154
SHEET 6 A 7 ASP A 131 ALA A 134 -1 N VAL A 132 O LEU A 139
SHEET 7 A 7 GLY A 125 LYS A 127 -1 N LYS A 127 O ASP A 131
SHEET 1 B10 ASP A 261 HIS A 264 0
SHEET 2 B10 ARG A 222 GLU A 226 -1 N GLU A 226 O ASP A 261
SHEET 3 B10 ASP A 232 ILE A 240 -1 O VAL A 233 N VAL A 225
SHEET 4 B10 LEU A 246 VAL A 250 -1 O CYS A 247 N ASP A 239
SHEET 5 B10 ARG A 253 VAL A 257 -1 O VAL A 255 N LEU A 248
SHEET 6 B10 ARG B 253 VAL B 257 -1 O VAL B 256 N VAL A 256
SHEET 7 B10 LEU B 246 VAL B 250 -1 N LEU B 248 O VAL B 255
SHEET 8 B10 GLN B 231 ILE B 240 -1 N ARG B 238 O CYS B 247
SHEET 9 B10 ARG B 222 LEU B 227 -1 N LEU B 227 O GLN B 231
SHEET 10 B10 VAL B 262 HIS B 264 -1 O VAL B 263 N ARG B 224
SHEET 1 C 7 GLN B 29 VAL B 32 0
SHEET 2 C 7 VAL B 56 ILE B 59 1 O VAL B 57 N GLN B 29
SHEET 3 C 7 GLN B 81 ARG B 89 -1 O SER B 85 N LEU B 58
SHEET 4 C 7 PHE B 150 ASN B 158 -1 O LEU B 157 N ILE B 82
SHEET 5 C 7 GLY B 137 ALA B 147 -1 N LEU B 143 O GLY B 154
SHEET 6 C 7 ASP B 131 ALA B 134 -1 N VAL B 132 O LEU B 139
SHEET 7 C 7 THR B 124 LYS B 127 -1 N LYS B 127 O ASP B 131
CISPEP 1 TRP A 128 PRO A 129 0 3.16
CISPEP 2 GLN A 148 PRO A 149 0 7.95
CISPEP 3 PRO A 163 GLU A 164 0 -0.02
CISPEP 4 VAL A 166 ASP A 167 0 0.33
CISPEP 5 ALA B 23 GLY B 24 0 0.02
CISPEP 6 THR B 36 GLY B 37 0 5.60
CISPEP 7 TRP B 128 PRO B 129 0 3.87
CISPEP 8 GLN B 148 PRO B 149 0 -3.07
CRYST1 59.933 63.802 103.554 90.00 90.00 90.00 P 21 21 21 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 0.016685 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015673 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009657 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
