HEADER TRANSCRIPTION 27-APR-09 3H7H
TITLE CRYSTAL STRUCTURE OF THE HUMAN TRANSCRIPTION ELONGATION FACTOR DSIF,
TITLE 2 HSPT4/HSPT5 (176-273)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION ELONGATION FACTOR SPT4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HSPT4, DRB SENSITIVITY-INDUCING FACTOR SMALL SUBUNIT, DSIF
COMPND 5 SMALL SUBUNIT, DSIF P14;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRANSCRIPTION ELONGATION FACTOR SPT5;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 176-273;
COMPND 11 SYNONYM: HSPT5, DRB SENSITIVITY-INDUCING FACTOR LARGE SUBUNIT, DSIF
COMPND 12 LARGE SUBUNIT, DSIF P160, TAT-COTRANSACTIVATOR 1 PROTEIN, TAT-CT1
COMPND 13 PROTEIN;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETGB_1A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS HELICES SURROUNDING BETA SHEET, TRANSCRIPTION, ACTIVATOR, METAL-
KEYWDS 2 BINDING, NUCLEUS, REPRESSOR, TRANSCRIPTION REGULATION, ZINC-FINGER,
KEYWDS 3 METHYLATION, PHOSPHOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WENZEL,B.M.WOHRL,P.ROSCH,B.M.MARTINS
REVDAT 3 20-MAR-24 3H7H 1 REMARK SEQADV
REVDAT 2 21-JUL-10 3H7H 1 JRNL
REVDAT 1 08-DEC-09 3H7H 0
JRNL AUTH S.WENZEL,B.M.MARTINS,P.ROSCH,B.M.WOHRL
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN TRANSCRIPTION ELONGATION
JRNL TITL 2 FACTOR DSIF HSPT4 SUBUNIT IN COMPLEX WITH THE HSPT5
JRNL TITL 3 DIMERIZATION INTERFACE
JRNL REF BIOCHEM.J. V. 425 373 2010
JRNL REFN ISSN 0264-6021
JRNL PMID 19860741
JRNL DOI 10.1042/BJ20091422
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 28930
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : 5%
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1523
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.62000
REMARK 3 B33 (A**2) : -0.61000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.010 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.277 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3H7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052788.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.283
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28930
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 3350, TRIS/HCL,
REMARK 280 BETA-MERCAPTOETHANOL, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 20.54800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.54950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.04550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.54950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.54800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.04550
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 -2
REMARK 465 ALA A -1
REMARK 465 GLY B 172
REMARK 465 SER B 173
REMARK 465 HIS B 174
REMARK 465 VAL B 270
REMARK 465 ALA B 271
REMARK 465 ASN B 272
REMARK 465 LEU B 273
REMARK 465 GLY B 274
REMARK 465 SER B 275
REMARK 465 GLY B 276
REMARK 465 CYS B 277
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 O ARG A 104 N GLY A 105 1.72
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 154 O HOH B 373 3645 2.19
REMARK 500 N MET B 175 O HOH B 345 3645 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 104 C GLY A 105 N -0.185
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 ARG A 104 CB - CA - C ANGL. DEV. = -19.4 DEGREES
REMARK 500 ARG A 104 N - CA - C ANGL. DEV. = 29.4 DEGREES
REMARK 500 ARG A 104 CA - C - N ANGL. DEV. = 31.9 DEGREES
REMARK 500 ARG A 104 O - C - N ANGL. DEV. = -31.0 DEGREES
REMARK 500 ARG A 104 O - C - N ANGL. DEV. = -15.2 DEGREES
REMARK 500 GLY A 105 C - N - CA ANGL. DEV. = 29.9 DEGREES
REMARK 500 GLY A 105 C - N - CA ANGL. DEV. = -13.9 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 ASP A 68 53.76 -143.92
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 ZN A 119 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 16 SG
REMARK 620 2 CYS A 19 SG 108.9
REMARK 620 3 CYS A 33 SG 116.5 98.5
REMARK 620 4 CYS A 36 SG 111.5 107.3 112.9
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 BME A 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 119
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EXU RELATED DB: PDB
DBREF 3H7H A 2 117 UNP P63272 SPT4H_HUMAN 2 117
DBREF 3H7H B 176 273 UNP O00267 SPT5H_HUMAN 176 273
SEQADV 3H7H GLY A -2 UNP P63272 EXPRESSION TAG
SEQADV 3H7H ALA A -1 UNP P63272 EXPRESSION TAG
SEQADV 3H7H MET A 0 UNP P63272 EXPRESSION TAG
SEQADV 3H7H GLY A 1 UNP P63272 EXPRESSION TAG
SEQADV 3H7H GLY B 172 UNP O00267 EXPRESSION TAG
SEQADV 3H7H SER B 173 UNP O00267 EXPRESSION TAG
SEQADV 3H7H HIS B 174 UNP O00267 EXPRESSION TAG
SEQADV 3H7H MET B 175 UNP O00267 EXPRESSION TAG
SEQADV 3H7H GLY B 274 UNP O00267 EXPRESSION TAG
SEQADV 3H7H SER B 275 UNP O00267 EXPRESSION TAG
SEQADV 3H7H GLY B 276 UNP O00267 EXPRESSION TAG
SEQADV 3H7H CYS B 277 UNP O00267 EXPRESSION TAG
SEQRES 1 A 120 GLY ALA MET GLY ALA LEU GLU THR VAL PRO LYS ASP LEU
SEQRES 2 A 120 ARG HIS LEU ARG ALA CYS LEU LEU CYS SER LEU VAL LYS
SEQRES 3 A 120 THR ILE ASP GLN PHE GLU TYR ASP GLY CYS ASP ASN CYS
SEQRES 4 A 120 ASP ALA TYR LEU GLN MET LYS GLY ASN ARG GLU MET VAL
SEQRES 5 A 120 TYR ASP CYS THR SER SER SER PHE ASP GLY ILE ILE ALA
SEQRES 6 A 120 MET MET SER PRO GLU ASP SER TRP VAL SER LYS TRP GLN
SEQRES 7 A 120 ARG VAL SER ASN PHE LYS PRO GLY VAL TYR ALA VAL SER
SEQRES 8 A 120 VAL THR GLY ARG LEU PRO GLN GLY ILE VAL ARG GLU LEU
SEQRES 9 A 120 LYS SER ARG GLY VAL ALA TYR LYS SER ARG ASP THR ALA
SEQRES 10 A 120 ILE LYS THR
SEQRES 1 B 106 GLY SER HIS MET ASP PRO ASN LEU TRP THR VAL LYS CYS
SEQRES 2 B 106 LYS ILE GLY GLU GLU ARG ALA THR ALA ILE SER LEU MET
SEQRES 3 B 106 ARG LYS PHE ILE ALA TYR GLN PHE THR ASP THR PRO LEU
SEQRES 4 B 106 GLN ILE LYS SER VAL VAL ALA PRO GLU HIS VAL LYS GLY
SEQRES 5 B 106 TYR ILE TYR VAL GLU ALA TYR LYS GLN THR HIS VAL LYS
SEQRES 6 B 106 GLN ALA ILE GLU GLY VAL GLY ASN LEU ARG LEU GLY TYR
SEQRES 7 B 106 TRP ASN GLN GLN MET VAL PRO ILE LYS GLU MET THR ASP
SEQRES 8 B 106 VAL LEU LYS VAL VAL LYS GLU VAL ALA ASN LEU GLY SER
SEQRES 9 B 106 GLY CYS
HET BME A 118 8
HET ZN A 119 1
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM ZN ZINC ION
FORMUL 3 BME C2 H6 O S
FORMUL 4 ZN ZN 2+
FORMUL 5 HOH *196(H2 O)
HELIX 1 1 ALA A 2 VAL A 6 5 5
HELIX 2 2 ILE A 25 GLY A 32 1 8
HELIX 3 3 CYS A 36 GLN A 41 1 6
HELIX 4 4 ASN A 45 CYS A 52 1 8
HELIX 5 5 SER A 65 ASP A 68 5 4
HELIX 6 6 SER A 69 GLN A 75 1 7
HELIX 7 7 PRO A 94 ARG A 104 1 11
HELIX 8 8 GLU B 188 GLN B 204 1 17
HELIX 9 9 LYS B 231 GLU B 240 1 10
HELIX 10 10 VAL B 242 TYR B 249 5 8
HELIX 11 11 PRO B 256 MET B 260 5 5
HELIX 12 12 THR B 261 LYS B 265 5 5
SHEET 1 A 3 VAL A 22 THR A 24 0
SHEET 2 A 3 LEU A 13 CYS A 16 -1 N ARG A 14 O LYS A 23
SHEET 3 A 3 THR A 53 SER A 54 -1 O SER A 54 N ALA A 15
SHEET 1 B 6 GLY A 83 VAL A 89 0
SHEET 2 B 6 PHE A 57 MET A 63 -1 N MET A 63 O GLY A 83
SHEET 3 B 6 SER B 214 ALA B 217 -1 O ALA B 217 N ILE A 60
SHEET 4 B 6 TYR B 224 ALA B 229 -1 O GLU B 228 N SER B 214
SHEET 5 B 6 ASN B 178 LYS B 183 -1 N TRP B 180 O VAL B 227
SHEET 6 B 6 GLN B 253 MET B 254 -1 O GLN B 253 N THR B 181
SHEET 1 C 2 ILE A 115 LYS A 116 0
SHEET 2 C 2 VAL B 267 LYS B 268 1 O LYS B 268 N ILE A 115
LINK SG CYS A 16 ZN ZN A 119 1555 1555 2.36
LINK SG CYS A 19 ZN ZN A 119 1555 1555 2.36
LINK SG CYS A 33 ZN ZN A 119 1555 1555 2.33
LINK SG CYS A 36 ZN ZN A 119 1555 1555 2.36
CISPEP 1 ARG A 104 GLY A 105 0 -11.94
SITE 1 AC1 6 ASN A 35 CYS A 36 TYR A 39 VAL A 106
SITE 2 AC1 6 HOH A 174 HOH A 200
SITE 1 AC2 4 CYS A 16 CYS A 19 CYS A 33 CYS A 36
CRYST1 41.096 52.091 97.099 90.00 90.00 90.00 P 21 21 21 4
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 0.024333 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010299 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
