HEADER HYDROLASE 31-MAY-17 5O4Z
TITLE STRUCTURE OF THE INACTIVE T.MARITIMA PDE (TM1595) D80N D154N MUTANT
TITLE 2 WITH SUBSTRATE 5'-PAPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DHH/DHHA1-TYPE PHOSPHODIESTERASE TM1595;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM_1595;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHODIESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.WITTE,D.DREXLER,M.MUELLER
REVDAT 5 17-JAN-24 5O4Z 1 REMARK
REVDAT 4 20-FEB-19 5O4Z 1 SOURCE
REVDAT 3 13-DEC-17 5O4Z 1 JRNL
REVDAT 2 15-NOV-17 5O4Z 1 JRNL
REVDAT 1 25-OCT-17 5O4Z 0
JRNL AUTH D.J.DREXLER,M.MULLER,C.A.ROJAS-CORDOVA,A.M.BANDERA,G.WITTE
JRNL TITL STRUCTURAL AND BIOPHYSICAL ANALYSIS OF THE SOLUBLE
JRNL TITL 2 DHH/DHHA1-TYPE PHOSPHODIESTERASE TM1595 FROM THERMOTOGA
JRNL TITL 3 MARITIMA.
JRNL REF STRUCTURE V. 25 1887 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 29107484
JRNL DOI 10.1016/J.STR.2017.10.001
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 42286
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760
REMARK 3 FREE R VALUE TEST SET COUNT : 2014
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 43.9296 - 4.0961 1.00 3074 152 0.1513 0.1677
REMARK 3 2 4.0961 - 3.2516 1.00 2979 135 0.1432 0.1563
REMARK 3 3 3.2516 - 2.8406 1.00 2943 129 0.1650 0.1925
REMARK 3 4 2.8406 - 2.5809 1.00 2910 145 0.1689 0.2052
REMARK 3 5 2.5809 - 2.3960 1.00 2894 177 0.1688 0.1915
REMARK 3 6 2.3960 - 2.2547 0.99 2886 134 0.1709 0.1904
REMARK 3 7 2.2547 - 2.1418 0.99 2877 148 0.1911 0.2324
REMARK 3 8 2.1418 - 2.0486 0.99 2847 155 0.2061 0.2109
REMARK 3 9 2.0486 - 1.9697 0.99 2859 152 0.2008 0.2156
REMARK 3 10 1.9697 - 1.9017 0.95 2758 116 0.2836 0.3301
REMARK 3 11 1.9017 - 1.8423 0.95 2732 143 0.2730 0.3196
REMARK 3 12 1.8423 - 1.7896 0.99 2837 152 0.2632 0.3003
REMARK 3 13 1.7896 - 1.7425 0.99 2891 129 0.3096 0.3414
REMARK 3 14 1.7425 - 1.7000 0.98 2785 147 0.3714 0.3875
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.040
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 : 0.006 2748
REMARK 3 ANGLE : 0.763 3733
REMARK 3 CHIRALITY : 0.055 405
REMARK 3 PLANARITY : 0.005 473
REMARK 3 DIHEDRAL : 11.660 1622
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID -2 THROUGH 320)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5698 -9.7724 -14.4268
REMARK 3 T TENSOR
REMARK 3 T11: 0.2467 T22: 0.2740
REMARK 3 T33: 0.2264 T12: -0.0126
REMARK 3 T13: 0.0014 T23: -0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 0.8628 L22: 1.8985
REMARK 3 L33: 0.9496 L12: 0.7825
REMARK 3 L13: -0.0648 L23: 0.1099
REMARK 3 S TENSOR
REMARK 3 S11: 0.1237 S12: -0.1410 S13: 0.0020
REMARK 3 S21: 0.2119 S22: -0.1004 S23: 0.0152
REMARK 3 S31: -0.0483 S32: -0.0636 S33: -0.0269
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 2)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2838 -8.2628 -14.1779
REMARK 3 T TENSOR
REMARK 3 T11: 0.5590 T22: 0.4875
REMARK 3 T33: 0.4772 T12: -0.1133
REMARK 3 T13: -0.0573 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.3677 L22: 0.9397
REMARK 3 L33: 1.7081 L12: 0.1003
REMARK 3 L13: -0.3110 L23: 0.3632
REMARK 3 S TENSOR
REMARK 3 S11: 0.2090 S12: 0.0549 S13: -0.1101
REMARK 3 S21: 0.0370 S22: 0.0986 S23: 0.0383
REMARK 3 S31: 0.1102 S32: 0.0243 S33: -0.1989
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 5O4Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200005182.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-16
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9660
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42319
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 98.8
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 : 21.4000
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) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
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: 5O1U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M AMMONIUMSULFATE 0.1 M SODIUM
REMARK 280 CITRATE, VAPOR DIFFUSION, HANGING DROP, 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 61.21500
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 61.21500
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 35.83500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.91500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.83500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.91500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.21500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.83500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.91500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.21500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.83500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.91500
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: DIMERIC
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -61.21500
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 605 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 635 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 672 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 698 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 740 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 742 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 749 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 GLY A -4
REMARK 465 SER A -3
REMARK 465 GLU A 321
REMARK 465 SER A 322
REMARK 465 GLU A 323
REMARK 465 LYS A 324
REMARK 465 ILE A 325
REMARK 465 PRO A 326
REMARK 465 GLU A 327
REMARK 465 GLY A 328
REMARK 465 ASP A 329
REMARK 465 VAL A 330
REMARK 465 LEU A 331
REMARK 465 GLY A 332
REMARK 465 GLY A 333
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 O3' A A 401 P A A 402 1.62
REMARK 500 ND2 ASN A 80 O HOH A 501 2.12
REMARK 500 OD1 ASP A 221 O HOH A 502 2.16
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 PRO A 258 -166.38 -68.43
REMARK 500 TRP A 271 -23.72 -148.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 A A 402
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue A A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue A A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 411
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5O1U RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH AMP/MN
REMARK 900 RELATED ID: 5O25 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN APO-STATE
DBREF 5O4Z A 1 333 UNP Q9X1T1 Q9X1T1_THEMA 1 333
SEQADV 5O4Z GLY A -4 UNP Q9X1T1 EXPRESSION TAG
SEQADV 5O4Z SER A -3 UNP Q9X1T1 EXPRESSION TAG
SEQADV 5O4Z GLY A -2 UNP Q9X1T1 EXPRESSION TAG
SEQADV 5O4Z SER A -1 UNP Q9X1T1 EXPRESSION TAG
SEQADV 5O4Z GLY A 0 UNP Q9X1T1 EXPRESSION TAG
SEQADV 5O4Z ASN A 80 UNP Q9X1T1 ASP 80 ENGINEERED MUTATION
SEQADV 5O4Z ASN A 154 UNP Q9X1T1 ASP 154 ENGINEERED MUTATION
SEQRES 1 A 338 GLY SER GLY SER GLY MET ASP GLU ILE VAL LYS VAL LEU
SEQRES 2 A 338 SER GLN HIS ASP ARG ILE LEU VAL VAL GLY HIS ILE MET
SEQRES 3 A 338 PRO ASP GLY ASP CYS VAL SER SER VAL LEU SER LEU THR
SEQRES 4 A 338 LEU GLY LEU GLU LYS LEU GLY LYS GLU VAL LYS ALA ALA
SEQRES 5 A 338 VAL ASP TYR LYS ILE PRO TYR VAL PHE GLU LYS PHE PRO
SEQRES 6 A 338 TYR ILE ASP LYS ILE GLU GLU ASN PRO ASN PHE ASP PRO
SEQRES 7 A 338 GLU LEU LEU VAL VAL VAL ASN ALA SER SER PRO ASP ARG
SEQRES 8 A 338 ILE GLY LYS PHE GLN ASP LEU LEU ASP LYS VAL PRO SER
SEQRES 9 A 338 VAL VAL ILE ASP HIS HIS SER THR ASN THR ASN PHE GLY
SEQRES 10 A 338 ASN TRP ASN TRP VAL ASP PRO SER PHE ALA ALA THR ALA
SEQRES 11 A 338 GLN MET ILE PHE ARG ILE ASN LYS ALA LEU GLY VAL GLU
SEQRES 12 A 338 TYR ASP SER ASN LEU ALA THR LEU ASN TYR LEU GLY ILE
SEQRES 13 A 338 ALA THR ASN THR GLY PHE PHE ARG HIS SER ASN ALA ASP
SEQRES 14 A 338 VAL ARG VAL PHE GLU ASP ALA TYR LYS LEU VAL LYS MET
SEQRES 15 A 338 GLY ALA ASP ALA HIS PHE VAL ALA LYS GLU ILE LEU GLU
SEQRES 16 A 338 ASN LYS ARG PHE GLU GLN PHE LYS LEU PHE ALA GLU VAL
SEQRES 17 A 338 LEU GLU ARG LEU GLN LEU LEU GLU ASN GLY LYS ILE ALA
SEQRES 18 A 338 TYR SER TYR ILE ASP TYR ASP THR TYR LEU ARG HIS ASN
SEQRES 19 A 338 CYS THR ASP GLU ASP SER ALA GLY PHE VAL GLY GLU LEU
SEQRES 20 A 338 ARG SER ILE ARG GLY VAL GLU VAL ALA VAL LEU PHE MET
SEQRES 21 A 338 GLU PHE PRO ARG GLY LYS ILE HIS VAL SER MET ARG SER
SEQRES 22 A 338 LYS ASP TRP PHE ASN VAL ASN GLU VAL ALA PHE GLU LEU
SEQRES 23 A 338 GLY GLY GLY GLY HIS PRO ARG ALA ALA GLY VAL THR PHE
SEQRES 24 A 338 GLU GLY LYS LYS ILE GLU GLU VAL ILE PRO ARG VAL ILE
SEQRES 25 A 338 ASN HIS LEU LEU LYS LYS PHE LYS GLU GLY VAL GLU SER
SEQRES 26 A 338 GLU SER GLU LYS ILE PRO GLU GLY ASP VAL LEU GLY GLY
HET A A 401 23
HET A A 402 22
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 405 5
HET SO4 A 406 5
HET SO4 A 407 5
HET SO4 A 408 5
HET GOL A 409 6
HET GOL A 410 6
HET CL A 411 1
HET CL A 412 1
HETNAM A ADENOSINE-5'-MONOPHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 A 2(C10 H14 N5 O7 P)
FORMUL 4 SO4 6(O4 S 2-)
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 12 CL 2(CL 1-)
FORMUL 14 HOH *249(H2 O)
HELIX 1 AA1 GLY A 0 HIS A 11 1 12
HELIX 2 AA2 ASP A 23 LEU A 40 1 18
HELIX 3 AA3 PRO A 53 GLU A 57 5 5
HELIX 4 AA4 TYR A 61 ASP A 63 5 3
HELIX 5 AA5 SER A 83 LYS A 96 5 14
HELIX 6 AA6 ALA A 123 GLY A 136 1 14
HELIX 7 AA7 ASP A 140 THR A 155 1 16
HELIX 8 AA8 ASP A 164 MET A 177 1 14
HELIX 9 AA9 ASP A 180 GLU A 190 1 11
HELIX 10 AB1 ARG A 193 LEU A 207 1 15
HELIX 11 AB2 ASP A 221 HIS A 228 1 8
HELIX 12 AB3 GLY A 237 SER A 244 1 8
HELIX 13 AB4 ASN A 273 LEU A 281 1 9
HELIX 14 AB5 LYS A 298 GLU A 319 1 22
SHEET 1 AA1 6 ILE A 65 GLU A 66 0
SHEET 2 AA1 6 GLU A 43 ALA A 47 1 N ALA A 46 O GLU A 66
SHEET 3 AA1 6 ARG A 13 VAL A 17 1 N VAL A 16 O LYS A 45
SHEET 4 AA1 6 LEU A 75 VAL A 79 1 O VAL A 77 N VAL A 17
SHEET 5 AA1 6 SER A 99 ASP A 103 1 O VAL A 100 N VAL A 78
SHEET 6 AA1 6 TRP A 114 VAL A 117 1 O TRP A 116 N VAL A 101
SHEET 1 AA2 6 GLN A 208 LEU A 210 0
SHEET 2 AA2 6 ILE A 215 ILE A 220 -1 O TYR A 217 N GLN A 208
SHEET 3 AA2 6 VAL A 250 GLU A 256 1 O GLU A 256 N ILE A 220
SHEET 4 AA2 6 LYS A 261 SER A 268 -1 O HIS A 263 N MET A 255
SHEET 5 AA2 6 ALA A 289 GLU A 295 -1 O VAL A 292 N VAL A 264
SHEET 6 AA2 6 GLY A 284 HIS A 286 -1 N HIS A 286 O ALA A 289
CISPEP 1 PHE A 257 PRO A 258 0 -8.06
SITE 1 AC1 20 HIS A 105 HIS A 263 SER A 265 ARG A 267
SITE 2 AC1 20 GLY A 283 GLY A 284 GLY A 285 HIS A 286
SITE 3 AC1 20 ALA A 289 ALA A 290 GLY A 291 THR A 293
SITE 4 AC1 20 A A 402 GOL A 409 HOH A 511 HOH A 546
SITE 5 AC1 20 HOH A 611 HOH A 616 HOH A 621 HOH A 629
SITE 1 AC2 17 HIS A 104 HIS A 105 THR A 153 ASN A 154
SITE 2 AC2 17 GLY A 156 HIS A 160 SER A 161 ASN A 162
SITE 3 AC2 17 ARG A 267 HIS A 286 ARG A 288 ALA A 289
SITE 4 AC2 17 A A 401 SO4 A 407 HOH A 579 HOH A 603
SITE 5 AC2 17 HOH A 638
SITE 1 AC3 4 GLU A 66 GLU A 67 ASN A 68 HOH A 552
SITE 1 AC4 3 ARG A 130 ARG A 166 HOH A 640
SITE 1 AC5 3 ASP A 140 SER A 141 HOH A 505
SITE 1 AC6 2 LYS A 192 GLU A 241
SITE 1 AC7 8 ARG A 159 HIS A 160 GLY A 237 GLY A 240
SITE 2 AC7 8 ARG A 243 ARG A 267 A A 402 HOH A 606
SITE 1 AC8 6 LEU A 281 GLY A 282 VAL A 292 THR A 293
SITE 2 AC8 6 PHE A 294 HOH A 636
SITE 1 AC9 4 ARG A 86 A A 401 HOH A 568 HOH A 621
SITE 1 AD1 5 GLY A 41 TYR A 219 HOH A 525 HOH A 557
SITE 2 AD1 5 HOH A 631
SITE 1 AD2 1 TYR A 61
CRYST1 71.670 87.830 122.430 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 0.013953 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011386 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008168 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
