HEADER TRANSFERASE 15-MAY-07 2Z1V
TITLE TRNA GUANINE TRANSGLYCOSYLASE E235Q MUTANT APO STRUCTURE, PH 8.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: QUEUINE TRNA-RIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRNA-GUANINE TRANSGLYCOSYLASE, GUANINE INSERTION ENZYME,
COMPND 5 TGT;
COMPND 6 EC: 2.4.2.29;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZYMOMONAS MOBILIS;
SOURCE 3 ORGANISM_TAXID: 542;
SOURCE 4 GENE: TGT;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET9D
KEYWDS TRNA GUANINE TRANSGLYCOSYLASE, TGT, E235Q MUTANT, APO, PH 8.5,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.TIDTEN,B.STENGL,A.HEINE,G.A.GARCIA,G.KLEBE,K.REUTER
REVDAT 6 01-NOV-23 2Z1V 1 REMARK
REVDAT 5 10-NOV-21 2Z1V 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2Z1V 1 VERSN
REVDAT 3 24-FEB-09 2Z1V 1 VERSN
REVDAT 2 13-NOV-07 2Z1V 1 JRNL
REVDAT 1 06-NOV-07 2Z1V 0
JRNL AUTH N.TIDTEN,B.STENGL,A.HEINE,G.A.GARCIA,G.KLEBE,K.REUTER
JRNL TITL GLUTAMATE VERSUS GLUTAMINE EXCHANGE SWAPS SUBSTRATE
JRNL TITL 2 SELECTIVITY IN TRNA-GUANINE TRANSGLYCOSYLASE: INSIGHT INTO
JRNL TITL 3 THE REGULATION OF SUBSTRATE SELECTIVITY BY KINETIC AND
JRNL TITL 4 CRYSTALLOGRAPHIC STUDIES
JRNL REF J.MOL.BIOL. V. 374 764 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17949745
JRNL DOI 10.1016/J.JMB.2007.09.062
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.144
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.143
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.143
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.141
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 49614
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2859
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 305
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3205.5
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2823.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 7
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 29142
REMARK 3 NUMBER OF RESTRAINTS : 36058
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.028
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.025
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.053
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.053
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.029
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.003
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.051
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.072
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: BABINET (SWAT)
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Z1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000027415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 113.0
REMARK 200 PH : 8.50
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56093
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2OKO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 8000, 100MM TRIS/HCL PH 8.5,
REMARK 280 1MM DTT, 10% DMSO, PH 8.50, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 45.37850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.58750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.37850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.58750
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 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 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 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 885 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 VAL A 2
REMARK 465 GLU A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 GLN A 7
REMARK 465 GLU A 8
REMARK 465 THR A 9
REMARK 465 ASP A 10
REMARK 465 LEU A 128
REMARK 465 ASP A 129
REMARK 465 GLY A 130
REMARK 465 SER A 131
REMARK 465 ARG A 384
REMARK 465 ASN A 385
REMARK 465 SER A 386
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 LYS A 125 CG CD CE NZ
REMARK 470 ARG A 132 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 GLN A 324 CG CD OE1 NE2
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 21 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 60 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 GLN A 203 C - N - CA ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 211 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 PHE A 246 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TYR A 258 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 274 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 303 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 336 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 336 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH1 ANGL. DEV. = 4.7 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 THR A 47 -85.59 -70.46
REMARK 500 ALA A 53 10.82 80.05
REMARK 500 LEU A 114 45.55 39.22
REMARK 500 SER A 205 -133.28 52.33
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 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 318 SG
REMARK 620 2 CYS A 320 SG 105.4
REMARK 620 3 CYS A 323 SG 116.5 117.4
REMARK 620 4 HIS A 349 ND1 103.4 113.2 100.1
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 ZN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 717
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P0B RELATED DB: PDB
REMARK 900 WILD TYPE ENZYME
REMARK 900 RELATED ID: 2OKO RELATED DB: PDB
REMARK 900 E235Q MUTANT OF THE SAME PROTEIN, APO STRUCTURE AT PH 5.5
REMARK 900 RELATED ID: 2Z1W RELATED DB: PDB
REMARK 900 E235Q MUTANT OF THE SAME PROTEIN, IN COMPLEX WITH BDI (2-BUTYL-5,6-
REMARK 900 DIHYDRO-1H-IMIDAZO[4,5-D]PYRIDAZINE-4,7-DIONE)
REMARK 900 RELATED ID: 2Z1X RELATED DB: PDB
REMARK 900 E235Q MUTANT OF THE SAME PROTEIN, IN COMPLEX WITH PREQ1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICT INVOLVING RESIDUE 312 IS CONSISTENT WITH
REMARK 999 THE REF. 1 AND 2 IN THE UNIPROT SEQUENCE DATABASE,
REMARK 999 TGT_ZYMMO.
DBREF 2Z1V A 1 386 UNP P28720 TGT_ZYMMO 1 386
SEQADV 2Z1V GLN A 235 UNP P28720 GLU 235 ENGINEERED MUTATION
SEQADV 2Z1V LYS A 312 UNP P28720 THR 312 SEE REMARK 999
SEQRES 1 A 386 MET VAL GLU ALA THR ALA GLN GLU THR ASP ARG PRO ARG
SEQRES 2 A 386 PHE SER PHE SER ILE ALA ALA ARG GLU GLY LYS ALA ARG
SEQRES 3 A 386 THR GLY THR ILE GLU MET LYS ARG GLY VAL ILE ARG THR
SEQRES 4 A 386 PRO ALA PHE MET PRO VAL GLY THR ALA ALA THR VAL LYS
SEQRES 5 A 386 ALA LEU LYS PRO GLU THR VAL ARG ALA THR GLY ALA ASP
SEQRES 6 A 386 ILE ILE LEU GLY ASN THR TYR HIS LEU MET LEU ARG PRO
SEQRES 7 A 386 GLY ALA GLU ARG ILE ALA LYS LEU GLY GLY LEU HIS SER
SEQRES 8 A 386 PHE MET GLY TRP ASP ARG PRO ILE LEU THR ASP SER GLY
SEQRES 9 A 386 GLY TYR GLN VAL MET SER LEU SER SER LEU THR LYS GLN
SEQRES 10 A 386 SER GLU GLU GLY VAL THR PHE LYS SER HIS LEU ASP GLY
SEQRES 11 A 386 SER ARG HIS MET LEU SER PRO GLU ARG SER ILE GLU ILE
SEQRES 12 A 386 GLN HIS LEU LEU GLY SER ASP ILE VAL MET ALA PHE ASP
SEQRES 13 A 386 GLU CYS THR PRO TYR PRO ALA THR PRO SER ARG ALA ALA
SEQRES 14 A 386 SER SER MET GLU ARG SER MET ARG TRP ALA LYS ARG SER
SEQRES 15 A 386 ARG ASP ALA PHE ASP SER ARG LYS GLU GLN ALA GLU ASN
SEQRES 16 A 386 ALA ALA LEU PHE GLY ILE GLN GLN GLY SER VAL PHE GLU
SEQRES 17 A 386 ASN LEU ARG GLN GLN SER ALA ASP ALA LEU ALA GLU ILE
SEQRES 18 A 386 GLY PHE ASP GLY TYR ALA VAL GLY GLY LEU ALA VAL GLY
SEQRES 19 A 386 GLN GLY GLN ASP GLU MET PHE ARG VAL LEU ASP PHE SER
SEQRES 20 A 386 VAL PRO MET LEU PRO ASP ASP LYS PRO HIS TYR LEU MET
SEQRES 21 A 386 GLY VAL GLY LYS PRO ASP ASP ILE VAL GLY ALA VAL GLU
SEQRES 22 A 386 ARG GLY ILE ASP MET PHE ASP CYS VAL LEU PRO THR ARG
SEQRES 23 A 386 SER GLY ARG ASN GLY GLN ALA PHE THR TRP ASP GLY PRO
SEQRES 24 A 386 ILE ASN ILE ARG ASN ALA ARG PHE SER GLU ASP LEU LYS
SEQRES 25 A 386 PRO LEU ASP SER GLU CYS HIS CYS ALA VAL CYS GLN LYS
SEQRES 26 A 386 TRP SER ARG ALA TYR ILE HIS HIS LEU ILE ARG ALA GLY
SEQRES 27 A 386 GLU ILE LEU GLY ALA MET LEU MET THR GLU HIS ASN ILE
SEQRES 28 A 386 ALA PHE TYR GLN GLN LEU MET GLN LYS ILE ARG ASP SER
SEQRES 29 A 386 ILE SER GLU GLY ARG PHE SER GLN PHE ALA GLN ASP PHE
SEQRES 30 A 386 ARG ALA ARG TYR PHE ALA ARG ASN SER
HET ZN A 400 1
HET GOL A 702 6
HET GOL A 704 6
HET GOL A 706 6
HET GOL A 717 6
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 7 HOH *305(H2 O)
HELIX 1 1 LYS A 55 THR A 62 1 8
HELIX 2 2 ASN A 70 ARG A 77 1 8
HELIX 3 3 GLY A 79 LEU A 86 1 8
HELIX 4 4 GLY A 88 GLY A 94 1 7
HELIX 5 5 GLY A 104 SER A 112 1 9
HELIX 6 6 SER A 136 GLY A 148 1 13
HELIX 7 7 THR A 164 ARG A 189 1 26
HELIX 8 8 ARG A 189 ALA A 196 1 8
HELIX 9 9 PHE A 207 GLY A 222 1 16
HELIX 10 10 GLY A 236 VAL A 248 1 13
HELIX 11 11 PRO A 249 LEU A 251 5 3
HELIX 12 12 LYS A 264 GLU A 273 1 10
HELIX 13 13 VAL A 282 GLY A 291 1 10
HELIX 14 14 ASN A 304 SER A 308 5 5
HELIX 15 15 CYS A 320 TRP A 326 1 7
HELIX 16 16 SER A 327 ALA A 337 1 11
HELIX 17 17 GLU A 339 GLU A 367 1 29
HELIX 18 18 ARG A 369 PHE A 382 1 14
SHEET 1 A 3 SER A 15 GLU A 22 0
SHEET 2 A 3 ALA A 25 MET A 32 -1 O GLU A 31 N SER A 15
SHEET 3 A 3 GLY A 35 THR A 39 -1 O ILE A 37 N ILE A 30
SHEET 1 B 9 ALA A 41 MET A 43 0
SHEET 2 B 9 MET A 278 ASP A 280 1 O PHE A 279 N MET A 43
SHEET 3 B 9 HIS A 257 LEU A 259 1 N LEU A 259 O MET A 278
SHEET 4 B 9 GLY A 225 VAL A 228 1 N VAL A 228 O TYR A 258
SHEET 5 B 9 ALA A 197 GLN A 202 1 N GLN A 202 O ALA A 227
SHEET 6 B 9 ILE A 151 MET A 153 1 N VAL A 152 O ALA A 197
SHEET 7 B 9 ILE A 99 THR A 101 1 N THR A 101 O ILE A 151
SHEET 8 B 9 ILE A 67 GLY A 69 1 N GLY A 69 O LEU A 100
SHEET 9 B 9 VAL A 45 GLY A 46 1 N GLY A 46 O LEU A 68
SHEET 1 C 3 SER A 113 SER A 118 0
SHEET 2 C 3 GLY A 121 LYS A 125 -1 O THR A 123 N LYS A 116
SHEET 3 C 3 ARG A 132 LEU A 135 -1 O HIS A 133 N PHE A 124
SHEET 1 D 2 GLN A 292 ALA A 293 0
SHEET 2 D 2 ILE A 300 ASN A 301 -1 O ILE A 300 N ALA A 293
LINK SG CYS A 318 ZN ZN A 400 1555 1555 2.33
LINK SG CYS A 320 ZN ZN A 400 1555 1555 2.33
LINK SG CYS A 323 ZN ZN A 400 1555 1555 2.31
LINK ND1 HIS A 349 ZN ZN A 400 1555 1555 2.15
CISPEP 1 THR A 39 PRO A 40 0 -6.02
CISPEP 2 ARG A 77 PRO A 78 0 7.65
CISPEP 3 TYR A 161 PRO A 162 0 -6.24
CISPEP 4 VAL A 262 GLY A 263 0 -6.94
SITE 1 AC1 4 CYS A 318 CYS A 320 CYS A 323 HIS A 349
SITE 1 AC2 8 PRO A 56 GLU A 57 GLY A 94 TRP A 95
SITE 2 AC2 8 ASP A 96 ARG A 97 HOH A 929 HOH A1001
SITE 1 AC3 6 GLN A 117 ARG A 174 PRO A 252 ASP A 254
SITE 2 AC3 6 LYS A 255 HOH A 820
SITE 1 AC4 6 GLU A 317 LYS A 360 PHE A 373 ARG A 380
SITE 2 AC4 6 HOH A 743 HOH A 922
SITE 1 AC5 6 PRO A 249 MET A 250 LEU A 251 PRO A 252
SITE 2 AC5 6 ASP A 253 HOH A 932
CRYST1 90.757 65.175 70.455 90.00 96.12 90.00 C 1 2 1 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 0.011018 0.000000 0.001181 0.00000
SCALE2 0.000000 0.015343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014275 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
