HEADER HYDROLASE ACTIVATOR 19-NOV-14 4WZF
TITLE CRYSTAL STRUCTURAL BASIS FOR RV0315, AN IMMUNOSTIMULATORY ANTIGEN AND
TITLE 2 PSEUDO BETA-1, 3-GLUCANASE OF MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,3-BETA-GLUCANASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-1,3-GLUCANASE,POSSIBLE BETA-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: RV0315, RVBD_0315, LH57_01715, P425_00327;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS MYCOBACTERIUM TUBERCULOSIS, RV0315, GH16 LAMINARINASES, BETA-1, 3-
KEYWDS 2 GLUCANASE, DC MATURATION, HYDROLASE ACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR W.Y.DONG,Z.F.FU,G.Q.PENG
REVDAT 2 20-MAR-24 4WZF 1 REMARK LINK
REVDAT 1 09-DEC-15 4WZF 0
JRNL AUTH W.DONG,J.HUANG,Y.LI,Y.TAN,Z.SHEN,Y.SONG,D.WANG,S.XIAO,
JRNL AUTH 2 H.CHEN,Z.F.FU,G.PENG
JRNL TITL CRYSTAL STRUCTURAL BASIS FOR RV0315, AN IMMUNOSTIMULATORY
JRNL TITL 2 ANTIGEN AND INACTIVE BETA-1,3-GLUCANASE OF MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS.
JRNL REF SCI REP V. 5 15073 2015
JRNL REFN ESSN 2045-2322
JRNL PMID 26469317
JRNL DOI 10.1038/SREP15073
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 61817
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3096
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 24.7860 - 4.7501 0.87 2453 126 0.2070 0.2447
REMARK 3 2 4.7501 - 3.7746 0.91 2500 119 0.1639 0.1960
REMARK 3 3 3.7746 - 3.2987 0.95 2609 143 0.1705 0.1761
REMARK 3 4 3.2987 - 2.9976 0.98 2667 139 0.1721 0.1828
REMARK 3 5 2.9976 - 2.7831 0.99 2701 140 0.1848 0.2195
REMARK 3 6 2.7831 - 2.6192 1.00 2719 159 0.1865 0.1896
REMARK 3 7 2.6192 - 2.4882 1.00 2696 145 0.1856 0.2077
REMARK 3 8 2.4882 - 2.3799 1.00 2712 152 0.1918 0.2135
REMARK 3 9 2.3799 - 2.2884 1.00 2714 148 0.1873 0.2578
REMARK 3 10 2.2884 - 2.2095 1.00 2675 143 0.1830 0.2549
REMARK 3 11 2.2095 - 2.1404 1.00 2703 163 0.1816 0.2105
REMARK 3 12 2.1404 - 2.0793 1.00 2746 133 0.1756 0.2245
REMARK 3 13 2.0793 - 2.0246 0.99 2687 153 0.1712 0.1967
REMARK 3 14 2.0246 - 1.9752 1.00 2703 116 0.1768 0.1989
REMARK 3 15 1.9752 - 1.9303 1.00 2670 139 0.1778 0.2440
REMARK 3 16 1.9303 - 1.8892 1.00 2736 144 0.1857 0.2209
REMARK 3 17 1.8892 - 1.8515 1.00 2696 160 0.1877 0.2095
REMARK 3 18 1.8515 - 1.8165 1.00 2698 137 0.1838 0.2139
REMARK 3 19 1.8165 - 1.7841 1.00 2652 156 0.1902 0.2227
REMARK 3 20 1.7841 - 1.7539 1.00 2744 131 0.1897 0.2641
REMARK 3 21 1.7539 - 1.7256 1.00 2691 127 0.1948 0.2319
REMARK 3 22 1.7256 - 1.6990 0.94 2549 123 0.2054 0.2242
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.880
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 3983
REMARK 3 ANGLE : 1.171 5448
REMARK 3 CHIRALITY : 0.050 513
REMARK 3 PLANARITY : 0.007 729
REMARK 3 DIHEDRAL : 13.520 1368
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WZF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204717.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97917
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62875
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.699
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.22800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM PHOSPHATE MONOBASIC, 20%
REMARK 280 PEG 3350, PH 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 67.56650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.92350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.56650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.92350
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 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 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 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 HOH A 503 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 MET A 1
REMARK 465 LEU A 2
REMARK 465 MET A 3
REMARK 465 PRO A 4
REMARK 465 GLU A 5
REMARK 465 MET A 6
REMARK 465 ASP A 7
REMARK 465 ARG A 8
REMARK 465 ARG A 9
REMARK 465 ARG A 10
REMARK 465 MET A 11
REMARK 465 MET A 12
REMARK 465 MET A 13
REMARK 465 MET A 14
REMARK 465 ALA A 15
REMARK 465 GLY A 16
REMARK 465 PHE A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 LEU A 24
REMARK 465 PRO A 25
REMARK 465 ALA A 26
REMARK 465 PRO A 27
REMARK 465 THR A 28
REMARK 465 ALA A 29
REMARK 465 TRP A 30
REMARK 465 ALA A 31
REMARK 465 ASP A 32
REMARK 465 PRO A 33
REMARK 465 SER A 34
REMARK 465 ARG A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 PRO A 39
REMARK 465 ALA A 40
REMARK 465 GLY A 41
REMARK 465 PRO A 42
REMARK 465 THR A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 PRO A 46
REMARK 465 ALA A 47
REMARK 465 ALA A 48
REMARK 465 PRO A 49
REMARK 465 ALA A 50
REMARK 465 ALA A 51
REMARK 465 ALA A 52
REMARK 465 THR A 53
REMARK 465 ILE A 242
REMARK 465 GLU A 243
REMARK 465 ASP A 244
REMARK 465 LEU A 245
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 MET B 3
REMARK 465 PRO B 4
REMARK 465 GLU B 5
REMARK 465 MET B 6
REMARK 465 ASP B 7
REMARK 465 ARG B 8
REMARK 465 ARG B 9
REMARK 465 ARG B 10
REMARK 465 MET B 11
REMARK 465 MET B 12
REMARK 465 MET B 13
REMARK 465 MET B 14
REMARK 465 ALA B 15
REMARK 465 GLY B 16
REMARK 465 PHE B 17
REMARK 465 GLY B 18
REMARK 465 ALA B 19
REMARK 465 LEU B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 ALA B 23
REMARK 465 LEU B 24
REMARK 465 PRO B 25
REMARK 465 ALA B 26
REMARK 465 PRO B 27
REMARK 465 THR B 28
REMARK 465 ALA B 29
REMARK 465 TRP B 30
REMARK 465 ALA B 31
REMARK 465 ASP B 32
REMARK 465 PRO B 33
REMARK 465 SER B 34
REMARK 465 ARG B 35
REMARK 465 PRO B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 PRO B 39
REMARK 465 ALA B 40
REMARK 465 GLY B 41
REMARK 465 PRO B 42
REMARK 465 THR B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 PRO B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 PRO B 49
REMARK 465 ALA B 50
REMARK 465 ALA B 51
REMARK 465 ALA B 52
REMARK 465 THR B 53
REMARK 465 ILE B 242
REMARK 465 GLU B 243
REMARK 465 ASP B 244
REMARK 465 LEU B 245
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
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 OE1 GLU A 247 O HOH A 501 2.07
REMARK 500 O HOH B 760 O HOH B 795 2.13
REMARK 500 OE2 GLU A 247 O HOH A 502 2.14
REMARK 500 O ILE A 231 O HOH A 750 2.16
REMARK 500 O HOH B 712 O HOH B 813 2.17
REMARK 500 O HOH A 567 O HOH A 581 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 572 O HOH B 556 2555 2.17
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 SER A 112 30.13 70.52
REMARK 500 ASN A 149 46.42 -96.36
REMARK 500 CYS A 150 25.26 -153.01
REMARK 500 ARG A 168 30.38 -150.38
REMARK 500 TRP A 252 98.71 -164.88
REMARK 500 ASP B 71 110.44 -38.26
REMARK 500 ASN B 149 44.51 -99.51
REMARK 500 CYS B 150 25.42 -150.38
REMARK 500 TRP B 156 77.32 -150.50
REMARK 500 ARG B 168 32.16 -149.05
REMARK 500 THR B 182 -40.75 -130.79
REMARK 500 TRP B 252 99.13 -163.96
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 A 785 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 818 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B 825 DISTANCE = 5.90 ANGSTROMS
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 61 O
REMARK 620 2 SER A 112 O 88.5
REMARK 620 3 SER A 112 OG 73.4 74.5
REMARK 620 4 ASP A 289 O 79.2 88.5 147.9
REMARK 620 5 ASP A 289 OD1 155.1 90.4 129.9 76.0
REMARK 620 6 HOH A 502 O 91.2 177.9 103.4 93.5 90.7
REMARK 620 7 HOH A 531 O 135.3 106.0 70.4 141.5 68.6 72.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 61 O
REMARK 620 2 SER B 112 O 88.0
REMARK 620 3 SER B 112 OG 74.1 76.0
REMARK 620 4 ASP B 289 O 79.6 87.0 149.0
REMARK 620 5 ASP B 289 OD1 154.8 88.3 128.8 75.2
REMARK 620 6 HOH B 507 O 91.4 178.8 104.8 91.9 91.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
DBREF 4WZF A 1 294 UNP O07242 O07242_MYCTU 1 294
DBREF 4WZF B 1 294 UNP O07242 O07242_MYCTU 1 294
SEQADV 4WZF GLY A 295 UNP O07242 EXPRESSION TAG
SEQADV 4WZF SER A 296 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS A 297 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS A 298 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS A 299 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS A 300 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS A 301 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS A 302 UNP O07242 EXPRESSION TAG
SEQADV 4WZF GLY B 295 UNP O07242 EXPRESSION TAG
SEQADV 4WZF SER B 296 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS B 297 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS B 298 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS B 299 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS B 300 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS B 301 UNP O07242 EXPRESSION TAG
SEQADV 4WZF HIS B 302 UNP O07242 EXPRESSION TAG
SEQRES 1 A 302 MET LEU MET PRO GLU MET ASP ARG ARG ARG MET MET MET
SEQRES 2 A 302 MET ALA GLY PHE GLY ALA LEU ALA ALA ALA LEU PRO ALA
SEQRES 3 A 302 PRO THR ALA TRP ALA ASP PRO SER ARG PRO ALA ALA PRO
SEQRES 4 A 302 ALA GLY PRO THR PRO ALA PRO ALA ALA PRO ALA ALA ALA
SEQRES 5 A 302 THR GLY GLY LEU LEU PHE HIS ASP GLU PHE ASP GLY PRO
SEQRES 6 A 302 ALA GLY SER VAL PRO ASP PRO SER LYS TRP GLN VAL SER
SEQRES 7 A 302 ASN HIS ARG THR PRO ILE LYS ASN PRO VAL GLY PHE ASP
SEQRES 8 A 302 ARG PRO GLN PHE PHE GLY GLN TYR ARG ASP SER ARG GLN
SEQRES 9 A 302 ASN VAL PHE LEU ASP GLY ASN SER ASN LEU VAL LEU ARG
SEQRES 10 A 302 ALA THR ARG GLU GLY ASN ARG TYR PHE GLY GLY LEU VAL
SEQRES 11 A 302 HIS GLY LEU TRP ARG GLY GLY ILE GLY THR THR TRP GLU
SEQRES 12 A 302 ALA ARG ILE LYS PHE ASN CYS LEU ALA PRO GLY MET TRP
SEQRES 13 A 302 PRO ALA TRP TRP LEU SER ASN ASP ASP PRO GLY ARG SER
SEQRES 14 A 302 GLY GLU ILE ASP LEU ILE GLU TRP TYR GLY ASN GLY THR
SEQRES 15 A 302 TRP PRO SER GLY THR THR VAL HIS ALA ASN PRO ASP GLY
SEQRES 16 A 302 THR ALA PHE GLU THR CYS PRO ILE GLY VAL ASP GLY GLY
SEQRES 17 A 302 TRP HIS ASN TRP ARG VAL THR TRP ASN PRO SER GLY MET
SEQRES 18 A 302 TYR PHE TRP LEU ASP TYR ALA ASP GLY ILE GLU PRO TYR
SEQRES 19 A 302 PHE SER VAL PRO ALA THR GLY ILE GLU ASP LEU ASN GLU
SEQRES 20 A 302 PRO ILE ARG GLU TRP PRO PHE ASN ASP PRO GLY TYR LYS
SEQRES 21 A 302 VAL PHE PRO VAL LEU ASN LEU ALA VAL GLY GLY SER GLY
SEQRES 22 A 302 GLY GLY ASP PRO ALA THR GLY SER TYR PRO GLN GLU MET
SEQRES 23 A 302 LEU VAL ASP TRP VAL ARG VAL PHE GLY SER HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
SEQRES 1 B 302 MET LEU MET PRO GLU MET ASP ARG ARG ARG MET MET MET
SEQRES 2 B 302 MET ALA GLY PHE GLY ALA LEU ALA ALA ALA LEU PRO ALA
SEQRES 3 B 302 PRO THR ALA TRP ALA ASP PRO SER ARG PRO ALA ALA PRO
SEQRES 4 B 302 ALA GLY PRO THR PRO ALA PRO ALA ALA PRO ALA ALA ALA
SEQRES 5 B 302 THR GLY GLY LEU LEU PHE HIS ASP GLU PHE ASP GLY PRO
SEQRES 6 B 302 ALA GLY SER VAL PRO ASP PRO SER LYS TRP GLN VAL SER
SEQRES 7 B 302 ASN HIS ARG THR PRO ILE LYS ASN PRO VAL GLY PHE ASP
SEQRES 8 B 302 ARG PRO GLN PHE PHE GLY GLN TYR ARG ASP SER ARG GLN
SEQRES 9 B 302 ASN VAL PHE LEU ASP GLY ASN SER ASN LEU VAL LEU ARG
SEQRES 10 B 302 ALA THR ARG GLU GLY ASN ARG TYR PHE GLY GLY LEU VAL
SEQRES 11 B 302 HIS GLY LEU TRP ARG GLY GLY ILE GLY THR THR TRP GLU
SEQRES 12 B 302 ALA ARG ILE LYS PHE ASN CYS LEU ALA PRO GLY MET TRP
SEQRES 13 B 302 PRO ALA TRP TRP LEU SER ASN ASP ASP PRO GLY ARG SER
SEQRES 14 B 302 GLY GLU ILE ASP LEU ILE GLU TRP TYR GLY ASN GLY THR
SEQRES 15 B 302 TRP PRO SER GLY THR THR VAL HIS ALA ASN PRO ASP GLY
SEQRES 16 B 302 THR ALA PHE GLU THR CYS PRO ILE GLY VAL ASP GLY GLY
SEQRES 17 B 302 TRP HIS ASN TRP ARG VAL THR TRP ASN PRO SER GLY MET
SEQRES 18 B 302 TYR PHE TRP LEU ASP TYR ALA ASP GLY ILE GLU PRO TYR
SEQRES 19 B 302 PHE SER VAL PRO ALA THR GLY ILE GLU ASP LEU ASN GLU
SEQRES 20 B 302 PRO ILE ARG GLU TRP PRO PHE ASN ASP PRO GLY TYR LYS
SEQRES 21 B 302 VAL PHE PRO VAL LEU ASN LEU ALA VAL GLY GLY SER GLY
SEQRES 22 B 302 GLY GLY ASP PRO ALA THR GLY SER TYR PRO GLN GLU MET
SEQRES 23 B 302 LEU VAL ASP TRP VAL ARG VAL PHE GLY SER HIS HIS HIS
SEQRES 24 B 302 HIS HIS HIS
HET CA A 401 1
HET EDO A 402 4
HET EDO A 403 4
HET CA B 401 1
HET EDO B 402 4
HETNAM CA CALCIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CA 2(CA 2+)
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 8 HOH *659(H2 O)
HELIX 1 AA1 VAL A 88 PHE A 96 5 9
HELIX 2 AA2 ASP A 276 GLY A 280 5 5
HELIX 3 AA3 VAL B 88 PHE B 96 5 9
HELIX 4 AA4 ASP B 276 GLY B 280 5 5
SHEET 1 AA1 4 TRP A 75 VAL A 77 0
SHEET 2 AA1 4 ARG A 124 GLY A 132 -1 O HIS A 131 N GLN A 76
SHEET 3 AA1 4 LYS A 260 VAL A 269 -1 O PRO A 263 N GLY A 132
SHEET 4 AA1 4 GLY A 136 GLY A 137 -1 N GLY A 136 O VAL A 261
SHEET 1 AA2 3 TRP A 75 VAL A 77 0
SHEET 2 AA2 3 ARG A 124 GLY A 132 -1 O HIS A 131 N GLN A 76
SHEET 3 AA2 3 GLN A 98 TYR A 99 1 N GLN A 98 O GLY A 127
SHEET 1 AA3 4 GLN A 98 TYR A 99 0
SHEET 2 AA3 4 ARG A 124 GLY A 132 1 O GLY A 127 N GLN A 98
SHEET 3 AA3 4 LEU A 114 GLU A 121 -1 N GLU A 121 O ARG A 124
SHEET 4 AA3 4 VAL A 106 LEU A 108 -1 N PHE A 107 O VAL A 115
SHEET 1 AA4 4 VAL A 106 LEU A 108 0
SHEET 2 AA4 4 LEU A 114 GLU A 121 -1 O VAL A 115 N PHE A 107
SHEET 3 AA4 4 GLN A 284 PHE A 294 -1 O MET A 286 N LEU A 116
SHEET 4 AA4 4 LEU A 56 ASP A 60 -1 N LEU A 57 O VAL A 293
SHEET 1 AA512 PHE A 198 PRO A 202 0
SHEET 2 AA512 GLY A 186 HIS A 190 -1 N THR A 187 O CYS A 201
SHEET 3 AA512 GLY A 170 GLU A 176 -1 N GLU A 171 O HIS A 190
SHEET 4 AA512 MET A 155 ASN A 163 -1 N LEU A 161 O ILE A 172
SHEET 5 AA512 LYS A 260 VAL A 269 -1 O VAL A 264 N TRP A 160
SHEET 6 AA512 ARG A 124 GLY A 132 -1 N GLY A 132 O PRO A 263
SHEET 7 AA512 LEU A 114 GLU A 121 -1 N GLU A 121 O ARG A 124
SHEET 8 AA512 GLN A 284 PHE A 294 -1 O MET A 286 N LEU A 116
SHEET 9 AA512 THR A 140 ASN A 149 -1 N LYS A 147 O LEU A 287
SHEET 10 AA512 TRP A 209 ASN A 217 -1 O TRP A 216 N THR A 140
SHEET 11 AA512 GLY A 220 LEU A 225 -1 O GLY A 220 N ASN A 217
SHEET 12 AA512 PHE A 235 PRO A 238 -1 O VAL A 237 N MET A 221
SHEET 1 AA6 7 PHE B 198 PRO B 202 0
SHEET 2 AA6 7 GLY B 186 HIS B 190 -1 N THR B 187 O CYS B 201
SHEET 3 AA6 7 GLY B 170 GLU B 176 -1 N ASP B 173 O THR B 188
SHEET 4 AA6 7 MET B 155 ASN B 163 -1 N LEU B 161 O ILE B 172
SHEET 5 AA6 7 PHE B 262 VAL B 269 -1 O VAL B 264 N TRP B 160
SHEET 6 AA6 7 ARG B 124 GLY B 132 -1 N GLY B 132 O PRO B 263
SHEET 7 AA6 7 TRP B 75 VAL B 77 -1 N GLN B 76 O HIS B 131
SHEET 1 AA7 3 TRP B 75 VAL B 77 0
SHEET 2 AA7 3 ARG B 124 GLY B 132 -1 O HIS B 131 N GLN B 76
SHEET 3 AA7 3 GLN B 98 TYR B 99 1 N GLN B 98 O GLY B 127
SHEET 1 AA8 4 GLN B 98 TYR B 99 0
SHEET 2 AA8 4 ARG B 124 GLY B 132 1 O GLY B 127 N GLN B 98
SHEET 3 AA8 4 LEU B 114 GLU B 121 -1 N GLU B 121 O ARG B 124
SHEET 4 AA8 4 VAL B 106 LEU B 108 -1 N PHE B 107 O VAL B 115
SHEET 1 AA9 4 VAL B 106 LEU B 108 0
SHEET 2 AA9 4 LEU B 114 GLU B 121 -1 O VAL B 115 N PHE B 107
SHEET 3 AA9 4 GLN B 284 GLY B 295 -1 O VAL B 288 N LEU B 114
SHEET 4 AA9 4 LEU B 56 ASP B 60 -1 N PHE B 58 O VAL B 293
SHEET 1 AB112 PHE B 198 PRO B 202 0
SHEET 2 AB112 GLY B 186 HIS B 190 -1 N THR B 187 O CYS B 201
SHEET 3 AB112 GLY B 170 GLU B 176 -1 N ASP B 173 O THR B 188
SHEET 4 AB112 MET B 155 ASN B 163 -1 N LEU B 161 O ILE B 172
SHEET 5 AB112 PHE B 262 VAL B 269 -1 O VAL B 264 N TRP B 160
SHEET 6 AB112 ARG B 124 GLY B 132 -1 N GLY B 132 O PRO B 263
SHEET 7 AB112 LEU B 114 GLU B 121 -1 N GLU B 121 O ARG B 124
SHEET 8 AB112 GLN B 284 GLY B 295 -1 O VAL B 288 N LEU B 114
SHEET 9 AB112 THR B 140 ASN B 149 -1 N LYS B 147 O LEU B 287
SHEET 10 AB112 TRP B 209 ASN B 217 -1 O TRP B 216 N THR B 140
SHEET 11 AB112 GLY B 220 LEU B 225 -1 O GLY B 220 N ASN B 217
SHEET 12 AB112 PHE B 235 PRO B 238 -1 O VAL B 237 N MET B 221
LINK O GLU A 61 CA CA A 401 1555 1555 2.42
LINK O SER A 112 CA CA A 401 1555 1555 2.31
LINK OG SER A 112 CA CA A 401 1555 1555 2.33
LINK O ASP A 289 CA CA A 401 1555 1555 2.35
LINK OD1 ASP A 289 CA CA A 401 1555 1555 2.22
LINK CA CA A 401 O HOH A 502 1555 4545 2.27
LINK CA CA A 401 O HOH A 531 1555 1555 2.63
LINK O GLU B 61 CA CA B 401 1555 1555 2.40
LINK O SER B 112 CA CA B 401 1555 1555 2.31
LINK OG SER B 112 CA CA B 401 1555 1555 2.29
LINK O ASP B 289 CA CA B 401 1555 1555 2.37
LINK OD1 ASP B 289 CA CA B 401 1555 1555 2.25
LINK CA CA B 401 O HOH B 507 1555 1555 2.32
CISPEP 1 GLU A 247 PRO A 248 0 -2.15
CISPEP 2 TYR A 282 PRO A 283 0 5.53
CISPEP 3 GLU B 247 PRO B 248 0 -1.77
CISPEP 4 TYR B 282 PRO B 283 0 7.17
SITE 1 AC1 5 GLU A 61 SER A 112 ASP A 289 HOH A 502
SITE 2 AC1 5 HOH A 531
SITE 1 AC2 8 TRP A 156 ALA A 158 TRP A 160 GLU A 171
SITE 2 AC2 8 GLU A 176 HOH A 618 HOH A 703 HOH A 710
SITE 1 AC3 4 LEU A 129 HIS A 131 HOH A 728 HOH A 761
SITE 1 AC4 4 GLU B 61 SER B 112 ASP B 289 HOH B 507
SITE 1 AC5 8 TRP B 156 ALA B 158 TRP B 160 GLU B 171
SITE 2 AC5 8 GLU B 176 HOH B 607 HOH B 675 HOH B 730
CRYST1 135.133 65.847 67.449 90.00 105.17 90.00 C 1 2 1 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 0.007400 0.000000 0.002006 0.00000
SCALE2 0.000000 0.015187 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015361 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
