HEADER TRANSPORT PROTEIN 12-MAY-16 5JX2
TITLE CRYSTAL STRUCTURE OF MGLB-2 (TP0684) FROM TREPONEMA PALLIDUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE/GALACTOSE-BINDING LIPOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TREPONEMA PALLIDUM (STRAIN NICHOLS);
SOURCE 3 ORGANISM_TAXID: 243276;
SOURCE 4 STRAIN: NICHOLS;
SOURCE 5 GENE: MGLB, TPP38, TP_0684;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUCOSE-BINDING PROTEIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.BRAUTIGAM,R.K.DEKA,M.V.NORGARD
REVDAT 4 15-NOV-23 5JX2 1 ATOM
REVDAT 3 11-DEC-19 5JX2 1 REMARK
REVDAT 2 06-SEP-17 5JX2 1 REMARK
REVDAT 1 31-AUG-16 5JX2 0
JRNL AUTH C.A.BRAUTIGAM,R.K.DEKA,W.Z.LIU,M.V.NORGARD
JRNL TITL THE TP0684 (MGLB-2) LIPOPROTEIN OF TREPONEMA PALLIDUM: A
JRNL TITL 2 GLUCOSE-BINDING PROTEIN WITH DIVERGENT TOPOLOGY.
JRNL REF PLOS ONE V. 11 61022 2016
JRNL REFN ESSN 1932-6203
JRNL PMID 27536942
JRNL DOI 10.1371/JOURNAL.PONE.0161022
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 27622
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1393
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 36.7913 - 4.4152 1.00 2811 165 0.1477 0.1786
REMARK 3 2 4.4152 - 3.5054 1.00 2729 138 0.1602 0.2279
REMARK 3 3 3.5054 - 3.0625 1.00 2692 152 0.1909 0.2238
REMARK 3 4 3.0625 - 2.7826 1.00 2677 153 0.2107 0.2327
REMARK 3 5 2.7826 - 2.5832 1.00 2675 136 0.1951 0.2416
REMARK 3 6 2.5832 - 2.4310 1.00 2673 134 0.1876 0.2530
REMARK 3 7 2.4310 - 2.3092 1.00 2681 137 0.1956 0.2050
REMARK 3 8 2.3092 - 2.2087 0.90 2409 115 0.3183 0.3494
REMARK 3 9 2.2087 - 2.1237 0.94 2486 135 0.2134 0.2513
REMARK 3 10 2.1237 - 2.0504 0.91 2396 128 0.2582 0.3033
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.190
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 : 0.003 2845
REMARK 3 ANGLE : 0.735 3851
REMARK 3 CHIRALITY : 0.027 423
REMARK 3 PLANARITY : 0.003 507
REMARK 3 DIHEDRAL : 14.159 1037
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.4943 10.6314 25.4780
REMARK 3 T TENSOR
REMARK 3 T11: 0.3533 T22: 0.3271
REMARK 3 T33: 0.3650 T12: -0.0399
REMARK 3 T13: -0.0129 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.8341 L22: 2.5318
REMARK 3 L33: 2.8875 L12: -1.0936
REMARK 3 L13: 0.7487 L23: -1.4841
REMARK 3 S TENSOR
REMARK 3 S11: 0.1443 S12: -0.1290 S13: -0.7285
REMARK 3 S21: 0.0166 S22: 0.0101 S23: 0.2855
REMARK 3 S31: 0.4273 S32: 0.0591 S33: -0.2011
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 78.8146 27.5709 4.5208
REMARK 3 T TENSOR
REMARK 3 T11: 0.2562 T22: 0.3615
REMARK 3 T33: 0.2332 T12: -0.0194
REMARK 3 T13: 0.0047 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 2.1447 L22: 1.9283
REMARK 3 L33: 2.3713 L12: 0.2550
REMARK 3 L13: -0.0042 L23: -0.7267
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: 0.2864 S13: -0.0789
REMARK 3 S21: -0.2144 S22: 0.0873 S23: 0.0730
REMARK 3 S31: 0.0437 S32: -0.1976 S33: -0.0873
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 258 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.9290 23.4040 19.7599
REMARK 3 T TENSOR
REMARK 3 T11: 0.1844 T22: 0.2861
REMARK 3 T33: 0.2466 T12: -0.0153
REMARK 3 T13: 0.0227 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 1.5553 L22: 0.9732
REMARK 3 L33: 2.6196 L12: -0.6793
REMARK 3 L13: 0.9340 L23: -0.7143
REMARK 3 S TENSOR
REMARK 3 S11: -0.0082 S12: -0.0078 S13: -0.1033
REMARK 3 S21: -0.0028 S22: -0.0022 S23: -0.0887
REMARK 3 S31: 0.0505 S32: 0.2549 S33: 0.0159
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 259 THROUGH 293 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.3748 22.4775 24.2909
REMARK 3 T TENSOR
REMARK 3 T11: 0.2359 T22: 0.3583
REMARK 3 T33: 0.2258 T12: 0.0257
REMARK 3 T13: 0.0160 T23: -0.0671
REMARK 3 L TENSOR
REMARK 3 L11: 2.8356 L22: 3.9179
REMARK 3 L33: 3.7653 L12: -0.0719
REMARK 3 L13: 0.8800 L23: -2.1891
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: -0.1005 S13: -0.0559
REMARK 3 S21: -0.0156 S22: 0.0080 S23: -0.0187
REMARK 3 S31: -0.0897 S32: 0.4150 S33: -0.0529
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 294 THROUGH 378 )
REMARK 3 ORIGIN FOR THE GROUP (A): 105.4524 3.3169 22.8695
REMARK 3 T TENSOR
REMARK 3 T11: 0.5290 T22: 0.5425
REMARK 3 T33: 0.5886 T12: 0.1806
REMARK 3 T13: 0.0374 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.8024 L22: 3.3247
REMARK 3 L33: 3.6470 L12: 0.2432
REMARK 3 L13: 0.4899 L23: -0.4464
REMARK 3 S TENSOR
REMARK 3 S11: 0.1349 S12: 0.2062 S13: -0.8634
REMARK 3 S21: -0.3110 S22: -0.0888 S23: -0.1533
REMARK 3 S31: 1.0069 S32: 0.4420 S33: -0.0372
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 5JX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221366.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-15
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 : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97932
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28333
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 36.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.07500
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: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5 20% PEG MME
REMARK 280 5000, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 44.12500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.12500
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.77800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.01250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.77800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.01250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.12500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.77800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.01250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.12500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.77800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.01250
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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 672 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 -8
REMARK 465 GLY A -7
REMARK 465 SER A -6
REMARK 465 ASP A -5
REMARK 465 LYS A -4
REMARK 465 ILE A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 GLU A 4
REMARK 465 ASN A 5
REMARK 465 LEU A 6
REMARK 465 TYR A 7
REMARK 465 PHE A 8
REMARK 465 GLN A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 26
REMARK 465 THR A 27
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 ASN A 19 -40.03 69.14
REMARK 500 ASN A 36 31.40 -97.83
REMARK 500 ASP A 86 113.09 -167.16
REMARK 500 GLN A 114 73.98 -107.68
REMARK 500 ALA A 162 -121.86 48.35
REMARK 500 ASP A 195 -31.50 132.02
REMARK 500 GLU A 208 -76.84 -104.52
REMARK 500 ASN A 279 17.54 -152.37
REMARK 500 ALA A 317 -57.88 -121.16
REMARK 500 SER A 368 30.07 -94.82
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 71 OD1
REMARK 620 2 ASN A 73 OD1 77.5
REMARK 620 3 ASP A 75 OD1 82.5 67.6
REMARK 620 4 ILE A 77 O 85.2 146.9 82.5
REMARK 620 5 ASP A 166 OD2 99.7 139.0 153.3 71.3
REMARK 620 6 HOH A 505 O 93.4 66.2 133.4 143.7 73.2
REMARK 620 7 HOH A 516 O 177.0 105.3 99.2 92.6 77.7 87.2
REMARK 620 N 1 2 3 4 5 6
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 BTB 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 EDO A 404
DBREF 5JX2 A 11 378 UNP Q08255 MGLB_TREPA 36 403
SEQADV 5JX2 MET A -8 UNP Q08255 INITIATING METHIONINE
SEQADV 5JX2 GLY A -7 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 SER A -6 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 ASP A -5 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 LYS A -4 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 ILE A -3 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 HIS A -2 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 HIS A -1 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 HIS A 0 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 HIS A 1 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 HIS A 2 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 HIS A 3 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 GLU A 4 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 ASN A 5 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 LEU A 6 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 TYR A 7 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 PHE A 8 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 GLN A 9 UNP Q08255 EXPRESSION TAG
SEQADV 5JX2 GLY A 10 UNP Q08255 EXPRESSION TAG
SEQRES 1 A 387 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU
SEQRES 2 A 387 ASN LEU TYR PHE GLN GLY ARG ASP LYS PRO LEU VAL PHE
SEQRES 3 A 387 PHE ASN ARG GLN PRO SER ASP PRO LEU THR GLY LYS VAL
SEQRES 4 A 387 ASP MET ALA ALA MET ASN TRP ASN ASP LYS THR TYR TYR
SEQRES 5 A 387 VAL GLY PHE ASP ALA LYS PHE GLY GLY SER ILE GLN GLY
SEQRES 6 A 387 LYS MET ILE LEU ASP PHE LEU ALA SER SER GLU SER SER
SEQRES 7 A 387 VAL ASP ARG ASN GLY ASP GLY ILE ILE GLY TYR VAL LEU
SEQRES 8 A 387 CYS ILE GLY ASP VAL GLY HIS ASN ASP SER LYS VAL ARG
SEQRES 9 A 387 THR GLU GLY ILE ARG ARG ALA LEU GLY THR TRP THR GLY
SEQRES 10 A 387 SER SER ASP PRO GLY GLN ALA LYS GLU GLY GLN ALA VAL
SEQRES 11 A 387 VAL GLY GLY LYS SER TYR LYS VAL VAL GLU LEU GLU GLY
SEQRES 12 A 387 LYS ALA MET THR GLY THR ASP GLY SER THR TRP ASN THR
SEQRES 13 A 387 ASN SER ALA THR GLU SER MET GLY SER TRP VAL ALA LYS
SEQRES 14 A 387 PHE ALA ASP LYS ILE ASP LEU VAL ILE SER ASN ASN ASP
SEQRES 15 A 387 GLY MET ALA MET GLY CYS LEU GLN ALA SER ASN TYR PRO
SEQRES 16 A 387 ARG GLY LEU PRO ILE PHE GLY TYR ASP ALA ASN ALA ASP
SEQRES 17 A 387 ALA VAL GLU SER VAL GLY LYS GLY GLU LEU THR GLY THR
SEQRES 18 A 387 VAL SER GLN ASN VAL ASP ALA GLN ALA VAL ALA VAL LEU
SEQRES 19 A 387 GLN ILE ILE ARG ASN LEU LEU ASP GLY SER SER GLY GLU
SEQRES 20 A 387 ASP VAL VAL ALA ASN GLY ILE SER ARG PRO ASP ALA HIS
SEQRES 21 A 387 GLY ASN ALY ILE SER ALA PRO VAL GLN TYR TRP GLU ASP
SEQRES 22 A 387 VAL LYS ALA ILE MET ALA ASP ASN SER GLU VAL THR SER
SEQRES 23 A 387 ALA ASN TRP LYS GLU TYR THR ARG GLY ALA ARG ASP ALA
SEQRES 24 A 387 GLY VAL ARG GLN VAL SER ALA PRO THR LYS LYS VAL LEU
SEQRES 25 A 387 LEU THR VAL HIS ASN ALA SER ASN ASP PHE LEU ALA SER
SEQRES 26 A 387 ALA TYR LEU PRO ALA LEU LYS HIS TYR ALA PRO LEU LEU
SEQRES 27 A 387 ASN VAL ASP LEU THR VAL VAL GLN GLY ASP GLY GLN ASN
SEQRES 28 A 387 GLU LEU SER CYS LEU ASP LYS PHE THR ASN LEU ASP MET
SEQRES 29 A 387 PHE ASP ALA PHE ALA VAL ASN MET VAL LYS THR ASN SER
SEQRES 30 A 387 GLY ALA ASP TYR THR ASP LYS LEU LYS TYR
MODRES 5JX2 ALY A 254 LYS MODIFIED RESIDUE
HET ALY A 254 22
HET CA A 401 1
HET BTB A 402 33
HET EDO A 403 10
HET EDO A 404 10
HETNAM ALY N(6)-ACETYLLYSINE
HETNAM CA CALCIUM ION
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN BTB BIS-TRIS BUFFER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 ALY C8 H16 N2 O3
FORMUL 2 CA CA 2+
FORMUL 3 BTB C8 H19 N O5
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 6 HOH *194(H2 O)
HELIX 1 AA1 ASP A 31 ASN A 36 1 6
HELIX 2 AA2 PHE A 50 SER A 65 1 16
HELIX 3 AA3 GLU A 67 ASP A 71 5 5
HELIX 4 AA4 HIS A 89 LEU A 103 1 15
HELIX 5 AA5 ASN A 146 ALA A 162 1 17
HELIX 6 AA6 ASN A 172 LEU A 180 1 9
HELIX 7 AA7 ASN A 197 LYS A 206 1 10
HELIX 8 AA8 ASN A 216 ASP A 233 1 18
HELIX 9 AA9 GLY A 237 ASN A 243 1 7
HELIX 10 AB1 GLU A 263 VAL A 265 5 3
HELIX 11 AB2 ASN A 279 TYR A 283 5 5
HELIX 12 AB3 ASN A 311 ALA A 317 1 7
HELIX 13 AB4 ALA A 317 ALA A 326 1 10
HELIX 14 AB5 PRO A 327 LEU A 329 5 3
HELIX 15 AB6 GLU A 343 ASP A 348 1 6
HELIX 16 AB7 ASN A 352 PHE A 356 5 5
HELIX 17 AB8 SER A 368 LEU A 376 1 9
SHEET 1 AA1 7 VAL A 259 TRP A 262 0
SHEET 2 AA1 7 ALA A 267 ALA A 270 -1 O ALA A 267 N TRP A 262
SHEET 3 AA1 7 THR A 41 PHE A 46 1 N TYR A 43 O ILE A 268
SHEET 4 AA1 7 LEU A 15 PHE A 18 1 N PHE A 17 O TYR A 42
SHEET 5 AA1 7 ALA A 358 VAL A 361 1 O PHE A 359 N VAL A 16
SHEET 6 AA1 7 LYS A 300 VAL A 306 1 N THR A 305 O ALA A 360
SHEET 7 AA1 7 VAL A 331 GLN A 337 1 O THR A 334 N LEU A 304
SHEET 1 AA2 5 GLY A 118 VAL A 122 0
SHEET 2 AA2 5 LYS A 125 ALA A 136 -1 O VAL A 129 N GLY A 118
SHEET 3 AA2 5 ILE A 77 ILE A 84 1 N ILE A 78 O LYS A 128
SHEET 4 AA2 5 ILE A 165 SER A 170 1 O ASP A 166 N GLY A 79
SHEET 5 AA2 5 ILE A 191 PHE A 192 1 O PHE A 192 N VAL A 168
SHEET 1 AA3 2 THR A 212 SER A 214 0
SHEET 2 AA3 2 SER A 273 VAL A 275 -1 O SER A 273 N SER A 214
LINK C ASN A 253 N ALY A 254 1555 1555 1.33
LINK C ALY A 254 N ILE A 255 1555 1555 1.33
LINK OD1 ASP A 71 CA CA A 401 1555 1555 2.37
LINK OD1 ASN A 73 CA CA A 401 1555 1555 2.50
LINK OD1 ASP A 75 CA CA A 401 1555 1555 2.45
LINK O ILE A 77 CA CA A 401 1555 1555 2.30
LINK OD2 ASP A 166 CA CA A 401 1555 1555 2.66
LINK CA CA A 401 O HOH A 505 1555 1555 2.51
LINK CA CA A 401 O HOH A 516 1555 1555 2.46
SITE 1 AC1 7 ASP A 71 ASN A 73 ASP A 75 ILE A 77
SITE 2 AC1 7 ASP A 166 HOH A 505 HOH A 516
SITE 1 AC2 5 HIS A 89 ASP A 91 ARG A 95 ASN A 172
SITE 2 AC2 5 ASP A 195
SITE 1 AC3 4 ALA A 48 ASP A 91 ARG A 95 TYR A 194
SITE 1 AC4 5 PHE A 50 GLU A 97 ARG A 101 TRP A 262
SITE 2 AC4 5 HOH A 538
CRYST1 77.556 130.025 88.250 90.00 90.00 90.00 C 2 2 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 0.012894 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007691 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END