HEADER HYDROLASE 27-FEB-17 5X7U
TITLE TREHALOSE SYNTHASE FROM THERMOBACULUM TERRENUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TREHALOSE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 5-551;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBACULUM TERRENUM;
SOURCE 3 ORGANISM_TAXID: 525904;
SOURCE 4 STRAIN: ATCC BAA-798 / YNP1;
SOURCE 5 GENE: TTER_0330;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS TREHALOSE SYNATHASE, GH13 FAMILY, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SU,F.WANG
REVDAT 2 27-MAR-24 5X7U 1 REMARK
REVDAT 1 28-FEB-18 5X7U 0
JRNL AUTH J.WANG,X.REN,R.WANG,J.SU,F.WANG
JRNL TITL STRUCTURAL CHARACTERISTICS AND FUNCTION OF A NEW KIND OF
JRNL TITL 2 THERMOSTABLE TREHALOSE SYNTHASE FROM THERMOBACULUM TERRENUM.
JRNL REF J. AGRIC. FOOD CHEM. V. 65 7726 2017
JRNL REFN ESSN 1520-5118
JRNL PMID 28809106
JRNL DOI 10.1021/ACS.JAFC.7B02732
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 34034
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1727
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 39.7990 - 5.7210 1.00 2892 128 0.1704 0.2126
REMARK 3 2 5.7210 - 4.5430 1.00 2739 147 0.1442 0.1676
REMARK 3 3 4.5430 - 3.9693 1.00 2724 146 0.1326 0.1720
REMARK 3 4 3.9693 - 3.6067 1.00 2677 164 0.1536 0.1924
REMARK 3 5 3.6067 - 3.3483 1.00 2672 163 0.1727 0.2174
REMARK 3 6 3.3483 - 3.1510 1.00 2650 146 0.1895 0.2213
REMARK 3 7 3.1510 - 2.9932 1.00 2678 151 0.1916 0.2182
REMARK 3 8 2.9932 - 2.8630 1.00 2668 143 0.1987 0.2613
REMARK 3 9 2.8630 - 2.7528 1.00 2676 130 0.1859 0.2145
REMARK 3 10 2.7528 - 2.6578 1.00 2662 129 0.2009 0.2745
REMARK 3 11 2.6578 - 2.5747 1.00 2659 145 0.2024 0.2558
REMARK 3 12 2.5747 - 2.5011 0.98 2610 135 0.1996 0.2512
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.630
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 4694
REMARK 3 ANGLE : 0.966 6387
REMARK 3 CHIRALITY : 0.056 652
REMARK 3 PLANARITY : 0.007 838
REMARK 3 DIHEDRAL : 14.717 2778
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 5X7U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300003057.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AICHISR
REMARK 200 BEAMLINE : BL2S1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34034
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 63.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
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 (%): 67.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE MONOHYDRATE, 0.1 M
REMARK 280 TRIS PH 8.5, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-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 -1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 79.58800
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.40750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.20375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 79.58800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 114.61125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 114.61125
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 79.58800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 38.20375
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 79.58800
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.40750
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 79.58800
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 76.40750
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 79.58800
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 114.61125
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 38.20375
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 79.58800
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 38.20375
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 114.61125
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 79.58800
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 79.58800
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 76.40750
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: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 805 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 814 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 920 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 947 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 ASN A 2
REMARK 465 ASP A 3
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 N ASP A 4 O HOH A 701 2.09
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 950 O HOH A 950 10655 1.97
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 CYS A 262 N - CA - CB ANGL. DEV. = 9.0 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 PHE A 21 -60.63 -93.22
REMARK 500 ASP A 69 110.25 -162.97
REMARK 500 PRO A 120 -5.34 -58.29
REMARK 500 PHE A 166 -135.64 -113.75
REMARK 500 LEU A 207 -71.31 -55.80
REMARK 500 GLU A 261 -69.62 -126.24
REMARK 500 ALA A 330 57.94 -146.88
REMARK 500 ASN A 338 -128.33 55.52
REMARK 500 LEU A 339 68.58 -106.28
REMARK 500 ASP A 388 -126.99 48.56
REMARK 500 GLN A 481 -120.34 50.24
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 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 23 OD1
REMARK 620 2 ASN A 25 OD1 71.7
REMARK 620 3 ASP A 27 OD1 75.9 78.7
REMARK 620 4 SER A 29 O 73.7 144.8 87.4
REMARK 620 5 ASP A 31 OD2 88.8 89.4 162.9 95.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 104 OD1
REMARK 620 2 ASP A 172 OD2 88.3
REMARK 620 3 TYR A 206 O 65.4 107.8
REMARK 620 4 LEU A 207 O 103.5 165.4 70.5
REMARK 620 5 GLU A 209 OE1 136.6 84.7 76.2 80.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 604
DBREF 5X7U A 2 548 UNP D1CE96 D1CE96_THET1 5 551
SEQADV 5X7U MET A 1 UNP D1CE96 EXPRESSION TAG
SEQADV 5X7U HIS A 549 UNP D1CE96 EXPRESSION TAG
SEQRES 1 A 549 MET ASN ASP ASP PRO THR TRP TYR LYS ASP ALA ILE ILE
SEQRES 2 A 549 TYR GLU VAL GLY VAL ARG CYS PHE PHE ASP SER ASN ASN
SEQRES 3 A 549 ASP GLY SER GLY ASP ILE PRO GLY LEU THR ALA LYS LEU
SEQRES 4 A 549 ASP TYR ILE GLU SER LEU GLY VAL THR ALA ILE TRP LEU
SEQRES 5 A 549 LEU PRO PHE TYR ALA SER PRO LEU LYS ASP GLY GLY TYR
SEQRES 6 A 549 ASP ILE SER ASP TYR ARG SER LEU HIS PRO ASP PHE GLY
SEQRES 7 A 549 THR ILE GLU ASP PHE LYS VAL PHE LEU ASP GLU ALA HIS
SEQRES 8 A 549 ARG ARG GLY ILE ARG VAL ILE THR GLU LEU VAL LEU ASN
SEQRES 9 A 549 HIS THR SER ASP GLN HIS GLN TRP PHE ARG GLU ALA ARG
SEQRES 10 A 549 SER ASN PRO ASN SER PRO TYR ARG ASP TYR TYR VAL TRP
SEQRES 11 A 549 SER ASP THR ASP ASP LYS TYR LYS ASP ALA ARG ILE ILE
SEQRES 12 A 549 PHE ILE ASP THR GLU ARG SER ASN TRP THR TRP ASP GLN
SEQRES 13 A 549 GLU ALA GLY LYS TYR TYR TRP HIS ARG PHE PHE SER HIS
SEQRES 14 A 549 GLN PRO ASP LEU ASN TYR ASP ASN PRO LYS VAL GLN GLN
SEQRES 15 A 549 GLU ILE LEU ASP ILE VAL GLY TYR TRP LEU ASP MET GLY
SEQRES 16 A 549 VAL ASP GLY LEU ARG LEU ASP ALA VAL PRO TYR LEU TYR
SEQRES 17 A 549 GLU ARG GLU GLY THR ASN CYS GLU ASN LEU PRO GLU THR
SEQRES 18 A 549 HIS GLU PHE LEU LYS LYS LEU ARG LYS PHE VAL ASP ASP
SEQRES 19 A 549 ASN TRP PRO ASN ARG MET LEU LEU ALA GLU ALA ASN GLN
SEQRES 20 A 549 TRP PRO GLU ASP VAL VAL ALA TYR PHE GLY ASN GLY ASP
SEQRES 21 A 549 GLU CYS HIS MET ALA TYR HIS PHE PRO ILE MET PRO ARG
SEQRES 22 A 549 MET TYR MET ALA LEU ARG ARG GLU ASP ARG HIS PRO ILE
SEQRES 23 A 549 THR GLU ILE LEU ARG ARG THR PRO PRO ILE PRO GLU THR
SEQRES 24 A 549 CYS GLN TRP ALA LEU PHE LEU ARG ASN HIS ASP GLU LEU
SEQRES 25 A 549 THR LEU GLU MET VAL THR ASP GLU GLU ARG ASP TYR MET
SEQRES 26 A 549 TYR HIS GLU TYR ALA LYS ASP PRO ARG MET ARG LEU ASN
SEQRES 27 A 549 LEU GLY ILE ARG ARG ARG LEU ALA PRO LEU LEU ASP ASN
SEQRES 28 A 549 SER GLU ARG ARG ILE GLN LEU MET HIS LEU LEU LEU PHE
SEQRES 29 A 549 THR LEU PRO GLY THR PRO ILE ILE TYR TYR GLY ASP GLU
SEQRES 30 A 549 ILE GLY MET GLY ASP ASN VAL TYR LEU GLY ASP ARG ASP
SEQRES 31 A 549 GLY VAL ARG THR PRO MET GLN TRP SER GLY ASP ARG ASN
SEQRES 32 A 549 ALA GLY PHE SER ARG ALA ASN PRO GLN ALA LEU TYR LEU
SEQRES 33 A 549 PRO PRO ILE ARG ASP PRO VAL PHE THR TYR GLU ALA VAL
SEQRES 34 A 549 ASN VAL GLU ALA GLN GLU GLN VAL PRO THR SER LEU LEU
SEQRES 35 A 549 ASN TRP MET LYS ARG THR ILE GLN ILE ARG LYS LYS TYR
SEQRES 36 A 549 PRO VAL PHE GLY ARG GLY SER ILE ARG PHE LEU GLN PRO
SEQRES 37 A 549 SER ASN ARG ALA VAL LEU ALA TYR ILE ARG GLN TYR GLN
SEQRES 38 A 549 ASP THR THR ILE LEU CYS ALA CYS ASN LEU SER ARG PHE
SEQRES 39 A 549 CYS GLN ALA ALA GLU LEU ASP LEU SER ASP PHE LYS GLY
SEQRES 40 A 549 LEU TYR PRO VAL GLU LEU TYR GLY LYS THR VAL PHE PRO
SEQRES 41 A 549 GLN ILE GLY GLU LEU PRO TYR LEU LEU THR PHE GLY PRO
SEQRES 42 A 549 HIS VAL PHE TYR TRP PHE GLU LEU LYS PRO GLN GLU GLN
SEQRES 43 A 549 LEU PRO HIS
HET TRS A 600 8
HET MG A 601 1
HET MG A 602 1
HET MG A 603 1
HET MG A 604 1
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM MG MAGNESIUM ION
HETSYN TRS TRIS BUFFER
FORMUL 2 TRS C4 H12 N O3 1+
FORMUL 3 MG 4(MG 2+)
FORMUL 7 HOH *250(H2 O)
HELIX 1 AA1 THR A 6 ALA A 11 5 6
HELIX 2 AA2 GLY A 17 PHE A 22 1 6
HELIX 3 AA3 ASP A 31 LYS A 38 1 8
HELIX 4 AA4 LYS A 38 GLY A 46 1 9
HELIX 5 AA5 PRO A 75 GLY A 78 5 4
HELIX 6 AA6 THR A 79 ARG A 93 1 15
HELIX 7 AA7 HIS A 110 ARG A 117 1 8
HELIX 8 AA8 TYR A 124 TYR A 128 5 5
HELIX 9 AA9 ASN A 177 MET A 194 1 18
HELIX 10 AB1 ALA A 203 LEU A 207 5 5
HELIX 11 AB2 LEU A 218 TRP A 236 1 19
HELIX 12 AB3 TRP A 248 ALA A 254 1 7
HELIX 13 AB4 TYR A 255 GLY A 257 5 3
HELIX 14 AB5 PRO A 269 GLU A 281 1 13
HELIX 15 AB6 ARG A 283 ARG A 292 1 10
HELIX 16 AB7 THR A 318 ALA A 330 1 13
HELIX 17 AB8 ASP A 332 ARG A 336 5 5
HELIX 18 AB9 ARG A 344 LEU A 349 1 6
HELIX 19 AC1 SER A 352 LEU A 366 1 15
HELIX 20 AC2 GLY A 375 GLY A 379 5 5
HELIX 21 AC3 ARG A 389 ARG A 393 5 5
HELIX 22 AC4 ASP A 401 PHE A 406 5 6
HELIX 23 AC5 ASN A 410 LEU A 414 5 5
HELIX 24 AC6 ASN A 430 GLN A 436 1 7
HELIX 25 AC7 SER A 440 LYS A 454 1 15
HELIX 26 AC8 PRO A 456 GLY A 461 1 6
HELIX 27 AC9 LEU A 502 LYS A 506 5 5
HELIX 28 AD1 PRO A 543 LEU A 547 5 5
SHEET 1 AA1 9 ILE A 13 VAL A 16 0
SHEET 2 AA1 9 ALA A 49 LEU A 52 1 O ALA A 49 N TYR A 14
SHEET 3 AA1 9 ARG A 96 LEU A 101 1 O ILE A 98 N LEU A 52
SHEET 4 AA1 9 GLY A 198 LEU A 201 1 O ARG A 200 N THR A 99
SHEET 5 AA1 9 MET A 240 ALA A 243 1 O LEU A 242 N LEU A 201
SHEET 6 AA1 9 MET A 264 TYR A 266 1 O MET A 264 N ALA A 243
SHEET 7 AA1 9 GLN A 301 PHE A 305 1 O ALA A 303 N ALA A 265
SHEET 8 AA1 9 THR A 369 TYR A 373 1 O THR A 369 N LEU A 304
SHEET 9 AA1 9 ILE A 13 VAL A 16 1 N ILE A 13 O ILE A 372
SHEET 1 AA2 2 TYR A 56 ALA A 57 0
SHEET 2 AA2 2 ASP A 69 LEU A 73 -1 O SER A 72 N ALA A 57
SHEET 1 AA3 3 TRP A 130 SER A 131 0
SHEET 2 AA3 3 LYS A 160 TRP A 163 -1 O TYR A 161 N SER A 131
SHEET 3 AA3 3 TRP A 152 ASP A 155 -1 N THR A 153 O TYR A 162
SHEET 1 AA4 2 LEU A 312 THR A 313 0
SHEET 2 AA4 2 GLY A 340 ILE A 341 -1 O ILE A 341 N LEU A 312
SHEET 1 AA5 6 SER A 462 PHE A 465 0
SHEET 2 AA5 6 VAL A 473 TYR A 480 -1 O ILE A 477 N ARG A 464
SHEET 3 AA5 6 THR A 483 ASN A 490 -1 O ILE A 485 N ARG A 478
SHEET 4 AA5 6 PHE A 536 LYS A 542 -1 O TYR A 537 N ALA A 488
SHEET 5 AA5 6 TYR A 509 GLU A 512 -1 N VAL A 511 O GLU A 540
SHEET 6 AA5 6 THR A 517 VAL A 518 -1 O THR A 517 N GLU A 512
SHEET 1 AA6 2 GLN A 496 LEU A 500 0
SHEET 2 AA6 2 TYR A 527 PHE A 531 -1 O PHE A 531 N GLN A 496
LINK OD1 ASP A 23 MG MG A 601 1555 1555 2.23
LINK OD1 ASN A 25 MG MG A 601 1555 1555 2.30
LINK OD1 ASP A 27 MG MG A 601 1555 1555 2.41
LINK O SER A 29 MG MG A 601 1555 1555 2.26
LINK OD2 ASP A 31 MG MG A 601 1555 1555 2.29
LINK OD1 ASN A 104 MG MG A 604 1555 1555 2.68
LINK OD2 ASP A 172 MG MG A 604 1555 1555 2.32
LINK O TYR A 206 MG MG A 604 1555 1555 2.40
LINK O LEU A 207 MG MG A 604 1555 1555 2.44
LINK OE1 GLU A 209 MG MG A 604 1555 1555 2.37
LINK MG MG A 603 O HOH A 873 1555 1555 2.92
SITE 1 AC1 8 ASP A 62 TYR A 65 HIS A 105 PHE A 166
SITE 2 AC1 8 ASP A 202 GLU A 244 ARG A 389 HOH A 761
SITE 1 AC2 5 ASP A 23 ASN A 25 ASP A 27 SER A 29
SITE 2 AC2 5 ASP A 31
SITE 1 AC3 4 ARG A 283 THR A 287 ARG A 291 ARG A 471
SITE 1 AC4 4 SER A 352 ARG A 355 HIS A 534 HOH A 873
SITE 1 AC5 5 ASN A 104 ASP A 172 TYR A 206 LEU A 207
SITE 2 AC5 5 GLU A 209
CRYST1 159.176 159.176 152.815 90.00 90.00 90.00 I 41 2 2 16
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 0.006282 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006544 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
