HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-APR-12 4EOH
TITLE CRYSTAL STRUCTURE OF HUMAN PL KINASE WITH BOUND THEOPHYLLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIDOXAL KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PL KINASE, PYRIDOXINE KINASE;
COMPND 5 EC: 2.7.1.35;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDXK, C21ORF124, C21ORF97, PKH, PNK, PRED79;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.SAFO,A.K.GANDHI,F.N.MUSAYEV
REVDAT 2 22-AUG-12 4EOH 1 JRNL
REVDAT 1 02-MAY-12 4EOH 0
SPRSDE 02-MAY-12 4EOH 3KBI
JRNL AUTH A.K.GANDHI,J.V.DESAI,M.S.GHATGE,M.L.DI SALVO,S.DI BIASE,
JRNL AUTH 2 R.DANSO-DANQUAH,F.N.MUSAYEV,R.CONTESTABILE,V.SCHIRCH,
JRNL AUTH 3 M.K.SAFO
JRNL TITL CRYSTAL STRUCTURES OF HUMAN PYRIDOXAL KINASE IN COMPLEX WITH
JRNL TITL 2 THE NEUROTOXINS, GINKGOTOXIN AND THEOPHYLLINE: INSIGHTS INTO
JRNL TITL 3 PYRIDOXAL KINASE INHIBITION.
JRNL REF PLOS ONE V. 7 40954 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22879864
JRNL DOI 10.1371/JOURNAL.PONE.0040954
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2572397.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 52986
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2688
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4941
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 264
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4818
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 175
REMARK 3 SOLVENT ATOMS : 355
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.05000
REMARK 3 B22 (A**2) : -2.66000
REMARK 3 B33 (A**2) : -8.39000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.35
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.22
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 5.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.360 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.550 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.000 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 74.36
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : SULFATE.PAR
REMARK 3 PARAMETER FILE 4 : MPD.PAR
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : &_1_TOPOLOGY_INFILE_1
REMARK 3 TOPOLOGY FILE 2 : &_1_TOPOLOGY_INFILE_2
REMARK 3 TOPOLOGY FILE 3 : &_1_TOPOLOGY_INFILE_3
REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4EOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071873.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52989
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 37.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.970
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.84
REMARK 200 R MERGE FOR SHELL (I) : 0.24100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 3FHX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 48-50% MPD, PH 7.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+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 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 46.15100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.92400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 85.95200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.15100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.92400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 85.95200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.15100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.92400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 85.95200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.15100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.92400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 85.95200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -270.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 B 502 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 501 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 GLU A 2
REMARK 465 GLU A 3
REMARK 465 ARG A 208
REMARK 465 ASN A 209
REMARK 465 PRO A 210
REMARK 465 ALA A 211
REMARK 465 GLY A 212
REMARK 465 SER A 213
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 280
REMARK 465 GLY B 281
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 B 188 N ILE B 200 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 B 503 O HOH B 503 3555 1.84
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 TRP A 52 143.53 -173.18
REMARK 500 ASN A 75 49.82 -96.11
REMARK 500 LEU A 116 -42.56 -132.69
REMARK 500 TRP A 120 -103.46 -73.00
REMARK 500 ASP A 121 -70.68 -54.93
REMARK 500 VAL A 140 -70.37 -70.39
REMARK 500 THR B 47 4.16 -64.10
REMARK 500 TRP B 52 145.85 -170.25
REMARK 500 ASN B 75 60.46 -102.42
REMARK 500 LEU B 116 -33.48 -134.41
REMARK 500 TRP B 120 23.28 -156.49
REMARK 500 ASP B 121 -82.36 -159.00
REMARK 500 SER B 188 -98.97 -119.02
REMARK 500 ASP B 189 54.45 88.50
REMARK 500 GLN B 277 20.19 -71.45
REMARK 500 ALA B 278 -126.29 165.15
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 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 645 O
REMARK 620 2 HOH A 537 O 125.4
REMARK 620 3 HOH A 539 O 95.8 112.5
REMARK 620 4 HOH A 536 O 95.3 106.0 122.1
REMARK 620 5 HOH A 538 O 55.1 168.7 77.9 63.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 691 O
REMARK 620 2 HOH B 615 O 105.0
REMARK 620 3 HOH B 628 O 76.6 174.9
REMARK 620 4 HOH B 690 O 90.8 97.5 87.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEP A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD 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 SO4 A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEP B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 415
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KBI RELATED DB: PDB
REMARK 900 RELATED ID: 4EN4 RELATED DB: PDB
DBREF 4EOH A 1 312 UNP O00764 PDXK_HUMAN 1 312
DBREF 4EOH B 1 312 UNP O00764 PDXK_HUMAN 1 312
SEQRES 1 A 312 MET GLU GLU GLU CYS ARG VAL LEU SER ILE GLN SER HIS
SEQRES 2 A 312 VAL ILE ARG GLY TYR VAL GLY ASN ARG ALA ALA THR PHE
SEQRES 3 A 312 PRO LEU GLN VAL LEU GLY PHE GLU ILE ASP ALA VAL ASN
SEQRES 4 A 312 SER VAL GLN PHE SER ASN HIS THR GLY TYR ALA HIS TRP
SEQRES 5 A 312 LYS GLY GLN VAL LEU ASN SER ASP GLU LEU GLN GLU LEU
SEQRES 6 A 312 TYR GLU GLY LEU ARG LEU ASN ASN MET ASN LYS TYR ASP
SEQRES 7 A 312 TYR VAL LEU THR GLY TYR THR ARG ASP LYS SER PHE LEU
SEQRES 8 A 312 ALA MET VAL VAL ASP ILE VAL GLN GLU LEU LYS GLN GLN
SEQRES 9 A 312 ASN PRO ARG LEU VAL TYR VAL CYS ASP PRO VAL LEU GLY
SEQRES 10 A 312 ASP LYS TRP ASP GLY GLU GLY SER MET TYR VAL PRO GLU
SEQRES 11 A 312 ASP LEU LEU PRO VAL TYR LYS GLU LYS VAL VAL PRO LEU
SEQRES 12 A 312 ALA ASP ILE ILE THR PRO ASN GLN PHE GLU ALA GLU LEU
SEQRES 13 A 312 LEU SER GLY ARG LYS ILE HIS SER GLN GLU GLU ALA LEU
SEQRES 14 A 312 ARG VAL MET ASP MET LEU HIS SER MET GLY PRO ASP THR
SEQRES 15 A 312 VAL VAL ILE THR SER SER ASP LEU PRO SER PRO GLN GLY
SEQRES 16 A 312 SER ASN TYR LEU ILE VAL LEU GLY SER GLN ARG ARG ARG
SEQRES 17 A 312 ASN PRO ALA GLY SER VAL VAL MET GLU ARG ILE ARG MET
SEQRES 18 A 312 ASP ILE ARG LYS VAL ASP ALA VAL PHE VAL GLY THR GLY
SEQRES 19 A 312 ASP LEU PHE ALA ALA MET LEU LEU ALA TRP THR HIS LYS
SEQRES 20 A 312 HIS PRO ASN ASN LEU LYS VAL ALA CYS GLU LYS THR VAL
SEQRES 21 A 312 SER THR LEU HIS HIS VAL LEU GLN ARG THR ILE GLN CYS
SEQRES 22 A 312 ALA LYS ALA GLN ALA GLY GLU GLY VAL ARG PRO SER PRO
SEQRES 23 A 312 MET GLN LEU GLU LEU ARG MET VAL GLN SER LYS ARG ASP
SEQRES 24 A 312 ILE GLU ASP PRO GLU ILE VAL VAL GLN ALA THR VAL LEU
SEQRES 1 B 312 MET GLU GLU GLU CYS ARG VAL LEU SER ILE GLN SER HIS
SEQRES 2 B 312 VAL ILE ARG GLY TYR VAL GLY ASN ARG ALA ALA THR PHE
SEQRES 3 B 312 PRO LEU GLN VAL LEU GLY PHE GLU ILE ASP ALA VAL ASN
SEQRES 4 B 312 SER VAL GLN PHE SER ASN HIS THR GLY TYR ALA HIS TRP
SEQRES 5 B 312 LYS GLY GLN VAL LEU ASN SER ASP GLU LEU GLN GLU LEU
SEQRES 6 B 312 TYR GLU GLY LEU ARG LEU ASN ASN MET ASN LYS TYR ASP
SEQRES 7 B 312 TYR VAL LEU THR GLY TYR THR ARG ASP LYS SER PHE LEU
SEQRES 8 B 312 ALA MET VAL VAL ASP ILE VAL GLN GLU LEU LYS GLN GLN
SEQRES 9 B 312 ASN PRO ARG LEU VAL TYR VAL CYS ASP PRO VAL LEU GLY
SEQRES 10 B 312 ASP LYS TRP ASP GLY GLU GLY SER MET TYR VAL PRO GLU
SEQRES 11 B 312 ASP LEU LEU PRO VAL TYR LYS GLU LYS VAL VAL PRO LEU
SEQRES 12 B 312 ALA ASP ILE ILE THR PRO ASN GLN PHE GLU ALA GLU LEU
SEQRES 13 B 312 LEU SER GLY ARG LYS ILE HIS SER GLN GLU GLU ALA LEU
SEQRES 14 B 312 ARG VAL MET ASP MET LEU HIS SER MET GLY PRO ASP THR
SEQRES 15 B 312 VAL VAL ILE THR SER SER ASP LEU PRO SER PRO GLN GLY
SEQRES 16 B 312 SER ASN TYR LEU ILE VAL LEU GLY SER GLN ARG ARG ARG
SEQRES 17 B 312 ASN PRO ALA GLY SER VAL VAL MET GLU ARG ILE ARG MET
SEQRES 18 B 312 ASP ILE ARG LYS VAL ASP ALA VAL PHE VAL GLY THR GLY
SEQRES 19 B 312 ASP LEU PHE ALA ALA MET LEU LEU ALA TRP THR HIS LYS
SEQRES 20 B 312 HIS PRO ASN ASN LEU LYS VAL ALA CYS GLU LYS THR VAL
SEQRES 21 B 312 SER THR LEU HIS HIS VAL LEU GLN ARG THR ILE GLN CYS
SEQRES 22 B 312 ALA LYS ALA GLN ALA GLY GLU GLY VAL ARG PRO SER PRO
SEQRES 23 B 312 MET GLN LEU GLU LEU ARG MET VAL GLN SER LYS ARG ASP
SEQRES 24 B 312 ILE GLU ASP PRO GLU ILE VAL VAL GLN ALA THR VAL LEU
HET NA A 401 1
HET TEP A 402 13
HET MPD A 403 8
HET MPD A 404 8
HET MPD A 405 8
HET MPD A 406 8
HET MPD A 407 8
HET SO4 A 408 5
HET SO4 A 409 5
HET SO4 A 410 5
HET NA B 401 1
HET TEP B 402 13
HET MPD B 403 8
HET MPD B 404 8
HET MPD B 405 8
HET MPD B 406 8
HET MPD B 407 8
HET MPD B 408 8
HET MPD B 409 8
HET MPD B 410 8
HET MPD B 411 8
HET SO4 B 412 5
HET SO4 B 413 5
HET SO4 B 414 5
HET SO4 B 415 5
HETNAM NA SODIUM ION
HETNAM TEP THEOPHYLLINE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM SO4 SULFATE ION
FORMUL 3 NA 2(NA 1+)
FORMUL 4 TEP 2(C7 H8 N4 O2)
FORMUL 5 MPD 14(C6 H14 O2)
FORMUL 10 SO4 7(O4 S 2-)
FORMUL 28 HOH *355(H2 O)
HELIX 1 1 GLY A 20 LEU A 31 1 12
HELIX 2 2 ASN A 58 ASN A 72 1 15
HELIX 3 3 ASP A 87 ASN A 105 1 19
HELIX 4 4 LEU A 132 LYS A 139 1 8
HELIX 5 5 LYS A 139 ALA A 144 1 6
HELIX 6 6 ASN A 150 GLY A 159 1 10
HELIX 7 7 SER A 164 GLY A 179 1 16
HELIX 8 8 GLY A 232 HIS A 248 1 17
HELIX 9 9 ASN A 251 ALA A 278 1 28
HELIX 10 10 MET A 293 GLN A 295 5 3
HELIX 11 11 SER A 296 ASP A 302 1 7
HELIX 12 12 GLY B 20 LEU B 31 1 12
HELIX 13 13 ASN B 58 ASN B 72 1 15
HELIX 14 14 ASP B 87 ASN B 105 1 19
HELIX 15 15 PRO B 129 ASP B 131 5 3
HELIX 16 16 LEU B 132 LYS B 139 1 8
HELIX 17 17 LYS B 139 ALA B 144 1 6
HELIX 18 18 ASN B 150 GLY B 159 1 10
HELIX 19 19 SER B 164 GLY B 179 1 16
HELIX 20 20 GLY B 232 HIS B 248 1 17
HELIX 21 21 ASN B 251 GLN B 277 1 27
HELIX 22 22 MET B 293 GLN B 295 5 3
HELIX 23 23 SER B 296 ASP B 302 1 7
SHEET 1 A10 GLY A 54 VAL A 56 0
SHEET 2 A10 GLU A 34 PHE A 43 -1 N GLN A 42 O GLN A 55
SHEET 3 A10 ARG A 6 VAL A 14 1 N VAL A 7 O ASP A 36
SHEET 4 A10 TYR A 79 THR A 82 1 O LEU A 81 N LEU A 8
SHEET 5 A10 VAL A 109 CYS A 112 1 O VAL A 111 N VAL A 80
SHEET 6 A10 ILE A 146 ILE A 147 1 O ILE A 146 N CYS A 112
SHEET 7 A10 THR A 182 ILE A 185 1 O THR A 182 N ILE A 147
SHEET 8 A10 TYR A 198 ARG A 206 -1 O LEU A 202 N ILE A 185
SHEET 9 A10 MET A 216 ARG A 224 -1 O ILE A 223 N LEU A 199
SHEET 10 A10 THR A 310 VAL A 311 -1 O THR A 310 N ARG A 220
SHEET 1 B 2 GLY A 117 LYS A 119 0
SHEET 2 B 2 GLY A 124 MET A 126 -1 O SER A 125 N ASP A 118
SHEET 1 C10 GLY B 54 VAL B 56 0
SHEET 2 C10 GLU B 34 PHE B 43 -1 N GLN B 42 O GLN B 55
SHEET 3 C10 ARG B 6 VAL B 14 1 N VAL B 7 O ASP B 36
SHEET 4 C10 TYR B 79 THR B 82 1 O LEU B 81 N LEU B 8
SHEET 5 C10 VAL B 109 CYS B 112 1 O VAL B 111 N VAL B 80
SHEET 6 C10 ILE B 146 ILE B 147 1 O ILE B 146 N CYS B 112
SHEET 7 C10 THR B 182 ILE B 185 1 O THR B 182 N ILE B 147
SHEET 8 C10 TYR B 198 ARG B 208 -1 O SER B 204 N VAL B 183
SHEET 9 C10 VAL B 214 ARG B 224 -1 O ILE B 223 N LEU B 199
SHEET 10 C10 THR B 310 VAL B 311 -1 O THR B 310 N ARG B 220
SHEET 1 D 2 GLY B 117 ASP B 118 0
SHEET 2 D 2 SER B 125 MET B 126 -1 O SER B 125 N ASP B 118
LINK NA NA A 401 O HOH A 645 1555 1555 2.56
LINK NA NA B 401 O HOH B 691 1555 1555 2.64
LINK NA NA A 401 O HOH A 537 1555 1555 2.66
LINK NA NA B 401 O HOH B 615 1555 1555 2.68
LINK NA NA A 401 O HOH A 539 1555 1555 2.84
LINK NA NA A 401 O HOH A 536 1555 1555 2.85
LINK NA NA B 401 O HOH B 628 1555 1555 2.86
LINK NA NA B 401 O HOH B 690 1555 1555 2.87
LINK NA NA A 401 O HOH A 538 1555 1555 3.08
SITE 1 AC1 6 GLU A 153 HOH A 536 HOH A 537 HOH A 538
SITE 2 AC1 6 HOH A 539 HOH A 645
SITE 1 AC2 7 SER A 12 GLY A 20 VAL A 231 ASP A 235
SITE 2 AC2 7 HOH A 546 HOH A 631 HOH A 633
SITE 1 AC3 5 SER A 12 PHE A 43 HIS A 46 THR A 47
SITE 2 AC3 5 HOH A 647
SITE 1 AC4 3 THR A 186 GLY A 234 LEU A 263
SITE 1 AC5 5 LYS A 76 TYR A 77 ASP A 78 ASN A 105
SITE 2 AC5 5 HOH A 636
SITE 1 AC6 5 ILE A 223 ARG A 224 VAL A 226 HIS A 264
SITE 2 AC6 5 HOH A 541
SITE 1 AC7 4 CYS A 5 LEU A 31 GLY A 32 LYS A 247
SITE 1 AC8 2 LEU A 156 LYS A 161
SITE 1 AC9 3 ARG A 70 MET A 93 GLU A 100
SITE 1 BC1 7 SER A 40 VAL A 56 THR A 85 ARG A 86
SITE 2 BC1 7 ASP A 87 PHE A 90 HOH A 600
SITE 1 BC2 5 GLU B 153 HOH B 615 HOH B 628 HOH B 690
SITE 2 BC2 5 HOH B 691
SITE 1 BC3 7 SER B 12 TYR B 84 VAL B 231 ASP B 235
SITE 2 BC3 7 HOH B 630 HOH B 660 HOH B 693
SITE 1 BC4 4 HIS B 46 THR B 47 TYR B 84 MPD B 407
SITE 1 BC5 2 ASP B 181 ARG B 208
SITE 1 BC6 1 PRO B 193
SITE 1 BC7 4 MET B 126 GLU B 130 LEU B 156 HOH B 636
SITE 1 BC8 6 SER A 192 PRO A 193 PHE B 43 TYR B 84
SITE 2 BC8 6 ARG B 86 MPD B 403
SITE 1 BC9 2 THR B 186 THR B 233
SITE 1 CC1 7 VAL B 109 THR B 245 PRO B 249 HOH B 514
SITE 2 CC1 7 HOH B 572 HOH B 678 HOH B 684
SITE 1 CC2 5 ILE B 223 ARG B 224 VAL B 226 HIS B 264
SITE 2 CC2 5 LEU B 267
SITE 1 CC3 5 ILE B 223 ARG B 224 HIS B 264 VAL B 306
SITE 2 CC3 5 VAL B 307
SITE 1 CC4 3 GLN B 63 GLU B 100 HOH B 689
SITE 1 CC5 6 GLU B 4 CYS B 5 ASP B 78 HIS B 246
SITE 2 CC5 6 HOH B 581 HOH B 663
SITE 1 CC6 6 CYS B 5 LEU B 31 GLY B 32 PHE B 33
SITE 2 CC6 6 HIS B 246 LYS B 247
SITE 1 CC7 2 GLU B 155 LEU B 156
CRYST1 92.302 115.848 171.904 90.00 90.00 90.00 I 2 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 0.010834 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005817 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
