HEADER LYASE 03-FEB-03 1NVF
TITLE CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX WITH
TITLE 2 ZN2+, ADP AND CARBAPHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-DEHYDROQUINATE SYNTHASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: DHQS;
COMPND 5 EC: 4.2.3.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EMERICELLA NIDULANS;
SOURCE 3 ORGANISM_TAXID: 162425;
SOURCE 4 GENE: AROMA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GLW38 (AROB-);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PTRC99A;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTR51
KEYWDS SHIKIMATE PATHWAY, AROMATIC AMINO ACID BIOSYNTHESIS, DHQS, CLOSED
KEYWDS 2 FORM, FORM H, DOMAIN MOVEMENT, CYCLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.NICHOLS,J.REN,H.K.LAMB,A.R.HAWKINS,D.K.STAMMERS
REVDAT 3 25-OCT-23 1NVF 1 REMARK LINK
REVDAT 2 24-FEB-09 1NVF 1 VERSN
REVDAT 1 18-MAR-03 1NVF 0
JRNL AUTH C.E.NICHOLS,J.REN,H.K.LAMB,A.R.HAWKINS,D.K.STAMMERS
JRNL TITL LIGAND-INDUCED CONFORMATIONAL CHANGES AND A MECHANISM FOR
JRNL TITL 2 DOMAIN CLOSURE IN ASPERGILLUS NIDULANS DEHYDROQUINATE
JRNL TITL 3 SYNTHASE
JRNL REF J.MOL.BIOL. V. 327 129 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12614613
JRNL DOI 10.1016/S0022-2836(03)00086-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.E.NICHOLS,J.REN,H.LAMB,F.HALDANE,A.R.HAWKINS,D.K.STAMMERS
REMARK 1 TITL IDENTIFICATION OF MANY CRYSTAL FORMS OF ASPERGILLUS NIDULANS
REMARK 1 TITL 2 DEHYDROQUINATE SYNTHASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 57 306 2001
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900019429
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1921937.040
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 27530
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) : 0.184
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1347
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2390
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE : 0.4140
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8919
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 139
REMARK 3 SOLVENT ATOMS : 442
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.73000
REMARK 3 B22 (A**2) : -0.69000
REMARK 3 B33 (A**2) : 13.42000
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) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.36
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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) : 3.350 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.240 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 8.560 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 11.010; 10.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 22.87
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 : LIG.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : LIG.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018246.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MULTILAYER OPTICS
REMARK 200 OPTICS : OSMIC MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27530
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.120
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.37
REMARK 200 R MERGE FOR SHELL (I) : 0.21700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1NR5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, DMSO, ETHYLENE GLYCOL, MEGA7,
REMARK 280 HEPES, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+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 103.25000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 103.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER, CHAINS A AND B FORM ONE
REMARK 300 CRYSTALLOGRAPHIC DIMER EQUIVALENT TO THIS BIOLOGICAL DIMER AND
REMARK 300 CHAIN C LIES ACROSS A CRYSTALLOGRAPHIC 2-FOLD GENERATING A 2ND HOMO-
REMARK 300 SYMETRIC BIOLOGICAL DIMER.
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: 6410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 136.40000
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 CL CL C 603 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C2690 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 SER A 2
REMARK 465 ASN A 3
REMARK 465 ALA A 392
REMARK 465 PRO A 393
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASN B 3
REMARK 465 ALA B 392
REMARK 465 PRO B 393
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ASN C 3
REMARK 465 ALA C 392
REMARK 465 PRO C 393
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 ARG A 77 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 391 O
REMARK 470 ARG B 77 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 391 O
REMARK 470 ARG C 77 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 391 O
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 TYR A 25 -68.42 -177.94
REMARK 500 ARG A 130 12.80 81.41
REMARK 500 ASP A 146 -73.65 -154.53
REMARK 500 ALA A 154 -179.23 -179.16
REMARK 500 ASP A 257 67.09 -157.99
REMARK 500 ARG A 259 39.94 -94.08
REMARK 500 GLU A 260 80.21 33.78
REMARK 500 ARG A 264 -12.91 -47.23
REMARK 500 ALA A 339 -49.58 76.85
REMARK 500 LYS A 356 -15.77 -45.20
REMARK 500 TYR B 25 -47.81 -179.72
REMARK 500 PRO B 70 -174.93 -68.81
REMARK 500 GLU B 81 12.91 -67.60
REMARK 500 GLN B 99 150.63 -49.06
REMARK 500 ARG B 105 -2.92 -56.69
REMARK 500 ARG B 130 14.91 80.92
REMARK 500 ASP B 146 -75.44 -150.44
REMARK 500 ALA B 214 -79.82 -31.82
REMARK 500 VAL B 225 126.46 73.82
REMARK 500 PRO B 227 84.58 -39.96
REMARK 500 ASP B 257 71.27 -157.56
REMARK 500 ALA B 339 -50.22 77.39
REMARK 500 TYR C 25 -42.87 -157.31
REMARK 500 PRO C 79 -9.18 -49.94
REMARK 500 LYS C 84 77.37 -100.50
REMARK 500 ARG C 130 15.64 80.05
REMARK 500 ASP C 146 -81.87 -146.95
REMARK 500 ALA C 154 172.42 175.95
REMARK 500 PHE C 232 49.74 -96.50
REMARK 500 ASP C 257 65.23 -156.06
REMARK 500 ARG C 259 34.88 -90.66
REMARK 500 GLU C 260 74.42 38.53
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 600 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 194 OE2
REMARK 620 2 HIS A 271 NE2 119.2
REMARK 620 3 HIS A 287 NE2 112.5 106.3
REMARK 620 4 CRB A 500 O4 71.5 88.2 158.7
REMARK 620 5 CRB A 500 O5 134.6 90.7 87.4 76.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 194 OE2
REMARK 620 2 HIS B 271 NE2 118.4
REMARK 620 3 HIS B 287 NE2 115.2 106.0
REMARK 620 4 CRB B 501 O4 70.9 89.2 156.0
REMARK 620 5 CRB B 501 O5 131.1 94.0 85.9 74.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 194 OE2
REMARK 620 2 HIS C 271 NE2 119.9
REMARK 620 3 HIS C 287 NE2 117.4 98.2
REMARK 620 4 CRB C 502 O5 138.6 84.4 88.3
REMARK 620 5 CRB C 502 O4 79.9 79.4 160.2 72.0
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 ZN A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 2605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CRB A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CRB B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CRB C 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NR5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+, NAD AND CARBAPHOSPHONATE, CRYSTAL FORM C, CLOSED FORM
REMARK 900 WITH COFACTOR
REMARK 900 RELATED ID: 1NRX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND NAD, CRYSTAL FORM F, OPEN FORM WITH COFACTOR
REMARK 900 RELATED ID: 1NVE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND NAD, CRYSTAL FORM E, OPEN FORM WITH COFACTOR
REMARK 900 RELATED ID: 1NVD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND CARBAPHOSPHONATE, CRYSTAL FORM B, CLOSED FORM WITH
REMARK 900 SUBSTRATE ANALOGUE AND REDUCED COFACTOR
REMARK 900 RELATED ID: 1NVB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND CARBAPHOSPHONATE, CRYSTAL FORM C, CLOSED FORM WITH
REMARK 900 SUBSTRATE ANALOGUE AND REDUCED CO-FACTOR
REMARK 900 RELATED ID: 1NUA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+, APO, CRYSTAL FORM D, OPEN FORM
REMARK 900 RELATED ID: 1NVA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX
REMARK 900 WITH ZN2+ AND ADP, CRYSTAL FORM D, OPEN FORM WITH CO-FACTOR ANALOGUE
DBREF 1NVF A 1 393 UNP P07547 ARO1_EMENI 1 393
DBREF 1NVF B 1 393 UNP P07547 ARO1_EMENI 1 393
DBREF 1NVF C 1 393 UNP P07547 ARO1_EMENI 1 393
SEQRES 1 A 393 MET SER ASN PRO THR LYS ILE SER ILE LEU GLY ARG GLU
SEQRES 2 A 393 SER ILE ILE ALA ASP PHE GLY LEU TRP ARG ASN TYR VAL
SEQRES 3 A 393 ALA LYS ASP LEU ILE SER ASP CYS SER SER THR THR TYR
SEQRES 4 A 393 VAL LEU VAL THR ASP THR ASN ILE GLY SER ILE TYR THR
SEQRES 5 A 393 PRO SER PHE GLU GLU ALA PHE ARG LYS ARG ALA ALA GLU
SEQRES 6 A 393 ILE THR PRO SER PRO ARG LEU LEU ILE TYR ASN ARG PRO
SEQRES 7 A 393 PRO GLY GLU VAL SER LYS SER ARG GLN THR LYS ALA ASP
SEQRES 8 A 393 ILE GLU ASP TRP MET LEU SER GLN ASN PRO PRO CYS GLY
SEQRES 9 A 393 ARG ASP THR VAL VAL ILE ALA LEU GLY GLY GLY VAL ILE
SEQRES 10 A 393 GLY ASP LEU THR GLY PHE VAL ALA SER THR TYR MET ARG
SEQRES 11 A 393 GLY VAL ARG TYR VAL GLN VAL PRO THR THR LEU LEU ALA
SEQRES 12 A 393 MET VAL ASP SER SER ILE GLY GLY LYS THR ALA ILE ASP
SEQRES 13 A 393 THR PRO LEU GLY LYS ASN LEU ILE GLY ALA ILE TRP GLN
SEQRES 14 A 393 PRO THR LYS ILE TYR ILE ASP LEU GLU PHE LEU GLU THR
SEQRES 15 A 393 LEU PRO VAL ARG GLU PHE ILE ASN GLY MET ALA GLU VAL
SEQRES 16 A 393 ILE LYS THR ALA ALA ILE SER SER GLU GLU GLU PHE THR
SEQRES 17 A 393 ALA LEU GLU GLU ASN ALA GLU THR ILE LEU LYS ALA VAL
SEQRES 18 A 393 ARG ARG GLU VAL THR PRO GLY GLU HIS ARG PHE GLU GLY
SEQRES 19 A 393 THR GLU GLU ILE LEU LYS ALA ARG ILE LEU ALA SER ALA
SEQRES 20 A 393 ARG HIS LYS ALA TYR VAL VAL SER ALA ASP GLU ARG GLU
SEQRES 21 A 393 GLY GLY LEU ARG ASN LEU LEU ASN TRP GLY HIS SER ILE
SEQRES 22 A 393 GLY HIS ALA ILE GLU ALA ILE LEU THR PRO GLN ILE LEU
SEQRES 23 A 393 HIS GLY GLU CYS VAL ALA ILE GLY MET VAL LYS GLU ALA
SEQRES 24 A 393 GLU LEU ALA ARG HIS LEU GLY ILE LEU LYS GLY VAL ALA
SEQRES 25 A 393 VAL SER ARG ILE VAL LYS CYS LEU ALA ALA TYR GLY LEU
SEQRES 26 A 393 PRO THR SER LEU LYS ASP ALA ARG ILE ARG LYS LEU THR
SEQRES 27 A 393 ALA GLY LYS HIS CYS SER VAL ASP GLN LEU MET PHE ASN
SEQRES 28 A 393 MET ALA LEU ASP LYS LYS ASN ASP GLY PRO LYS LYS LYS
SEQRES 29 A 393 ILE VAL LEU LEU SER ALA ILE GLY THR PRO TYR GLU THR
SEQRES 30 A 393 ARG ALA SER VAL VAL ALA ASN GLU ASP ILE ARG VAL VAL
SEQRES 31 A 393 LEU ALA PRO
SEQRES 1 B 393 MET SER ASN PRO THR LYS ILE SER ILE LEU GLY ARG GLU
SEQRES 2 B 393 SER ILE ILE ALA ASP PHE GLY LEU TRP ARG ASN TYR VAL
SEQRES 3 B 393 ALA LYS ASP LEU ILE SER ASP CYS SER SER THR THR TYR
SEQRES 4 B 393 VAL LEU VAL THR ASP THR ASN ILE GLY SER ILE TYR THR
SEQRES 5 B 393 PRO SER PHE GLU GLU ALA PHE ARG LYS ARG ALA ALA GLU
SEQRES 6 B 393 ILE THR PRO SER PRO ARG LEU LEU ILE TYR ASN ARG PRO
SEQRES 7 B 393 PRO GLY GLU VAL SER LYS SER ARG GLN THR LYS ALA ASP
SEQRES 8 B 393 ILE GLU ASP TRP MET LEU SER GLN ASN PRO PRO CYS GLY
SEQRES 9 B 393 ARG ASP THR VAL VAL ILE ALA LEU GLY GLY GLY VAL ILE
SEQRES 10 B 393 GLY ASP LEU THR GLY PHE VAL ALA SER THR TYR MET ARG
SEQRES 11 B 393 GLY VAL ARG TYR VAL GLN VAL PRO THR THR LEU LEU ALA
SEQRES 12 B 393 MET VAL ASP SER SER ILE GLY GLY LYS THR ALA ILE ASP
SEQRES 13 B 393 THR PRO LEU GLY LYS ASN LEU ILE GLY ALA ILE TRP GLN
SEQRES 14 B 393 PRO THR LYS ILE TYR ILE ASP LEU GLU PHE LEU GLU THR
SEQRES 15 B 393 LEU PRO VAL ARG GLU PHE ILE ASN GLY MET ALA GLU VAL
SEQRES 16 B 393 ILE LYS THR ALA ALA ILE SER SER GLU GLU GLU PHE THR
SEQRES 17 B 393 ALA LEU GLU GLU ASN ALA GLU THR ILE LEU LYS ALA VAL
SEQRES 18 B 393 ARG ARG GLU VAL THR PRO GLY GLU HIS ARG PHE GLU GLY
SEQRES 19 B 393 THR GLU GLU ILE LEU LYS ALA ARG ILE LEU ALA SER ALA
SEQRES 20 B 393 ARG HIS LYS ALA TYR VAL VAL SER ALA ASP GLU ARG GLU
SEQRES 21 B 393 GLY GLY LEU ARG ASN LEU LEU ASN TRP GLY HIS SER ILE
SEQRES 22 B 393 GLY HIS ALA ILE GLU ALA ILE LEU THR PRO GLN ILE LEU
SEQRES 23 B 393 HIS GLY GLU CYS VAL ALA ILE GLY MET VAL LYS GLU ALA
SEQRES 24 B 393 GLU LEU ALA ARG HIS LEU GLY ILE LEU LYS GLY VAL ALA
SEQRES 25 B 393 VAL SER ARG ILE VAL LYS CYS LEU ALA ALA TYR GLY LEU
SEQRES 26 B 393 PRO THR SER LEU LYS ASP ALA ARG ILE ARG LYS LEU THR
SEQRES 27 B 393 ALA GLY LYS HIS CYS SER VAL ASP GLN LEU MET PHE ASN
SEQRES 28 B 393 MET ALA LEU ASP LYS LYS ASN ASP GLY PRO LYS LYS LYS
SEQRES 29 B 393 ILE VAL LEU LEU SER ALA ILE GLY THR PRO TYR GLU THR
SEQRES 30 B 393 ARG ALA SER VAL VAL ALA ASN GLU ASP ILE ARG VAL VAL
SEQRES 31 B 393 LEU ALA PRO
SEQRES 1 C 393 MET SER ASN PRO THR LYS ILE SER ILE LEU GLY ARG GLU
SEQRES 2 C 393 SER ILE ILE ALA ASP PHE GLY LEU TRP ARG ASN TYR VAL
SEQRES 3 C 393 ALA LYS ASP LEU ILE SER ASP CYS SER SER THR THR TYR
SEQRES 4 C 393 VAL LEU VAL THR ASP THR ASN ILE GLY SER ILE TYR THR
SEQRES 5 C 393 PRO SER PHE GLU GLU ALA PHE ARG LYS ARG ALA ALA GLU
SEQRES 6 C 393 ILE THR PRO SER PRO ARG LEU LEU ILE TYR ASN ARG PRO
SEQRES 7 C 393 PRO GLY GLU VAL SER LYS SER ARG GLN THR LYS ALA ASP
SEQRES 8 C 393 ILE GLU ASP TRP MET LEU SER GLN ASN PRO PRO CYS GLY
SEQRES 9 C 393 ARG ASP THR VAL VAL ILE ALA LEU GLY GLY GLY VAL ILE
SEQRES 10 C 393 GLY ASP LEU THR GLY PHE VAL ALA SER THR TYR MET ARG
SEQRES 11 C 393 GLY VAL ARG TYR VAL GLN VAL PRO THR THR LEU LEU ALA
SEQRES 12 C 393 MET VAL ASP SER SER ILE GLY GLY LYS THR ALA ILE ASP
SEQRES 13 C 393 THR PRO LEU GLY LYS ASN LEU ILE GLY ALA ILE TRP GLN
SEQRES 14 C 393 PRO THR LYS ILE TYR ILE ASP LEU GLU PHE LEU GLU THR
SEQRES 15 C 393 LEU PRO VAL ARG GLU PHE ILE ASN GLY MET ALA GLU VAL
SEQRES 16 C 393 ILE LYS THR ALA ALA ILE SER SER GLU GLU GLU PHE THR
SEQRES 17 C 393 ALA LEU GLU GLU ASN ALA GLU THR ILE LEU LYS ALA VAL
SEQRES 18 C 393 ARG ARG GLU VAL THR PRO GLY GLU HIS ARG PHE GLU GLY
SEQRES 19 C 393 THR GLU GLU ILE LEU LYS ALA ARG ILE LEU ALA SER ALA
SEQRES 20 C 393 ARG HIS LYS ALA TYR VAL VAL SER ALA ASP GLU ARG GLU
SEQRES 21 C 393 GLY GLY LEU ARG ASN LEU LEU ASN TRP GLY HIS SER ILE
SEQRES 22 C 393 GLY HIS ALA ILE GLU ALA ILE LEU THR PRO GLN ILE LEU
SEQRES 23 C 393 HIS GLY GLU CYS VAL ALA ILE GLY MET VAL LYS GLU ALA
SEQRES 24 C 393 GLU LEU ALA ARG HIS LEU GLY ILE LEU LYS GLY VAL ALA
SEQRES 25 C 393 VAL SER ARG ILE VAL LYS CYS LEU ALA ALA TYR GLY LEU
SEQRES 26 C 393 PRO THR SER LEU LYS ASP ALA ARG ILE ARG LYS LEU THR
SEQRES 27 C 393 ALA GLY LYS HIS CYS SER VAL ASP GLN LEU MET PHE ASN
SEQRES 28 C 393 MET ALA LEU ASP LYS LYS ASN ASP GLY PRO LYS LYS LYS
SEQRES 29 C 393 ILE VAL LEU LEU SER ALA ILE GLY THR PRO TYR GLU THR
SEQRES 30 C 393 ARG ALA SER VAL VAL ALA ASN GLU ASP ILE ARG VAL VAL
SEQRES 31 C 393 LEU ALA PRO
HET ZN A 600 1
HET CL A 604 1
HET ADP A 400 27
HET CRB A 500 17
HET ZN B 601 1
HET ADP B 401 27
HET CRB B 501 17
HET ZN C 602 1
HET CL C 603 1
HET CL C2605 1
HET CL C2606 1
HET ADP C 402 27
HET CRB C 502 17
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM CRB [1R-(1ALPHA,3BETA,4ALPHA,5BETA)]-5-(PHOSPHONOMETHYL)-1,
HETNAM 2 CRB 3,4-TRIHYDROXYCYCLOHEXANE-1-CARBOXYLIC ACID
HETSYN CRB CARBAPHOSPHONATE
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 CL 4(CL 1-)
FORMUL 6 ADP 3(C10 H15 N5 O10 P2)
FORMUL 7 CRB 3(C8 H15 O8 P)
FORMUL 17 HOH *442(H2 O)
HELIX 1 1 TYR A 25 CYS A 34 1 10
HELIX 2 2 THR A 45 ALA A 64 1 20
HELIX 3 3 GLY A 80 LYS A 84 5 5
HELIX 4 4 SER A 85 SER A 98 1 14
HELIX 5 5 GLY A 114 TYR A 128 1 15
HELIX 6 6 MET A 129 GLY A 131 5 3
HELIX 7 7 THR A 140 ASP A 146 1 7
HELIX 8 8 GLU A 178 LEU A 183 5 6
HELIX 9 9 PRO A 184 ILE A 201 1 18
HELIX 10 10 SER A 203 ARG A 223 1 21
HELIX 11 11 THR A 235 ASP A 257 1 23
HELIX 12 12 GLY A 262 TRP A 269 5 8
HELIX 13 13 GLY A 270 THR A 282 1 13
HELIX 14 14 LEU A 286 LEU A 305 1 20
HELIX 15 15 LYS A 309 TYR A 323 1 15
HELIX 16 16 ASP A 331 ALA A 339 1 9
HELIX 17 17 SER A 344 MET A 352 1 9
HELIX 18 18 ALA A 383 VAL A 389 1 7
HELIX 19 19 TYR B 25 CYS B 34 1 10
HELIX 20 20 THR B 45 GLU B 65 1 21
HELIX 21 21 SER B 85 GLN B 99 1 15
HELIX 22 22 GLY B 114 TYR B 128 1 15
HELIX 23 23 MET B 129 GLY B 131 5 3
HELIX 24 24 THR B 140 ASP B 146 1 7
HELIX 25 25 GLU B 178 LEU B 183 5 6
HELIX 26 26 PRO B 184 ILE B 201 1 18
HELIX 27 27 SER B 203 ARG B 223 1 21
HELIX 28 28 THR B 235 ASP B 257 1 23
HELIX 29 29 GLY B 262 TRP B 269 5 8
HELIX 30 30 GLY B 270 THR B 282 1 13
HELIX 31 31 LEU B 286 LEU B 305 1 20
HELIX 32 32 LYS B 309 TYR B 323 1 15
HELIX 33 33 ASP B 331 ALA B 339 1 9
HELIX 34 34 SER B 344 ALA B 353 1 10
HELIX 35 35 ALA B 383 LEU B 391 1 9
HELIX 36 36 GLY C 20 TYR C 25 1 6
HELIX 37 37 TYR C 25 CYS C 34 1 10
HELIX 38 38 THR C 45 ALA C 64 1 20
HELIX 39 39 SER C 85 GLN C 99 1 15
HELIX 40 40 GLY C 114 TYR C 128 1 15
HELIX 41 41 MET C 129 GLY C 131 5 3
HELIX 42 42 THR C 140 ASP C 146 1 7
HELIX 43 43 GLU C 178 LEU C 183 5 6
HELIX 44 44 PRO C 184 ILE C 201 1 18
HELIX 45 45 SER C 203 ARG C 223 1 21
HELIX 46 46 THR C 235 ASP C 257 1 23
HELIX 47 47 GLY C 262 TRP C 269 5 8
HELIX 48 48 GLY C 270 THR C 282 1 13
HELIX 49 49 LEU C 286 LEU C 305 1 20
HELIX 50 50 LYS C 309 TYR C 323 1 15
HELIX 51 51 ASP C 331 LYS C 336 1 6
HELIX 52 52 SER C 344 ALA C 353 1 10
HELIX 53 53 ALA C 383 VAL C 389 1 7
SHEET 1 A 7 THR A 5 ILE A 9 0
SHEET 2 A 7 ARG A 12 ASP A 18 -1 O ALA A 17 N THR A 5
SHEET 3 A 7 LYS A 172 ASP A 176 1 O ILE A 175 N ILE A 16
SHEET 4 A 7 ARG A 133 PRO A 138 1 N GLN A 136 O TYR A 174
SHEET 5 A 7 VAL A 108 GLY A 113 1 N ALA A 111 O VAL A 135
SHEET 6 A 7 THR A 38 ASP A 44 1 N VAL A 40 O ILE A 110
SHEET 7 A 7 ARG A 71 ARG A 77 1 O TYR A 75 N LEU A 41
SHEET 1 B 2 LYS A 152 THR A 157 0
SHEET 2 B 2 GLY A 160 ILE A 167 -1 O ILE A 164 N ILE A 155
SHEET 1 C 2 LYS A 364 ILE A 365 0
SHEET 2 C 2 SER A 380 VAL A 381 -1 O SER A 380 N ILE A 365
SHEET 1 D 2 LEU A 368 ALA A 370 0
SHEET 2 D 2 THR A 373 PRO A 374 -1 O THR A 373 N ALA A 370
SHEET 1 E 7 THR B 5 ILE B 9 0
SHEET 2 E 7 ARG B 12 ASP B 18 -1 O ALA B 17 N THR B 5
SHEET 3 E 7 LYS B 172 ASP B 176 1 O ILE B 173 N ILE B 16
SHEET 4 E 7 ARG B 133 PRO B 138 1 N GLN B 136 O TYR B 174
SHEET 5 E 7 VAL B 108 GLY B 113 1 N ALA B 111 O VAL B 135
SHEET 6 E 7 THR B 38 ASP B 44 1 N VAL B 40 O ILE B 110
SHEET 7 E 7 ARG B 71 ARG B 77 1 O TYR B 75 N LEU B 41
SHEET 1 F 2 LYS B 152 THR B 157 0
SHEET 2 F 2 GLY B 160 ILE B 167 -1 O ILE B 164 N ILE B 155
SHEET 1 G 2 LYS B 364 ILE B 365 0
SHEET 2 G 2 SER B 380 VAL B 381 -1 O SER B 380 N ILE B 365
SHEET 1 H 2 LEU B 368 ALA B 370 0
SHEET 2 H 2 THR B 373 PRO B 374 -1 O THR B 373 N ALA B 370
SHEET 1 I 7 THR C 5 ILE C 9 0
SHEET 2 I 7 ARG C 12 ASP C 18 -1 O ALA C 17 N THR C 5
SHEET 3 I 7 LYS C 172 ASP C 176 1 O ILE C 173 N ILE C 16
SHEET 4 I 7 ARG C 133 PRO C 138 1 N GLN C 136 O TYR C 174
SHEET 5 I 7 VAL C 108 GLY C 113 1 N ALA C 111 O VAL C 135
SHEET 6 I 7 THR C 38 ASP C 44 1 N VAL C 40 O ILE C 110
SHEET 7 I 7 ARG C 71 ARG C 77 1 O TYR C 75 N LEU C 41
SHEET 1 J 2 LYS C 152 THR C 157 0
SHEET 2 J 2 GLY C 160 ILE C 167 -1 O ILE C 164 N ILE C 155
SHEET 1 K 2 LYS C 364 ILE C 365 0
SHEET 2 K 2 SER C 380 VAL C 381 -1 O SER C 380 N ILE C 365
SHEET 1 L 2 LEU C 368 ALA C 370 0
SHEET 2 L 2 THR C 373 PRO C 374 -1 O THR C 373 N ALA C 370
LINK OE2 GLU A 194 ZN ZN A 600 1555 1555 2.24
LINK NE2 HIS A 271 ZN ZN A 600 1555 1555 2.22
LINK NE2 HIS A 287 ZN ZN A 600 1555 1555 2.08
LINK O4 CRB A 500 ZN ZN A 600 1555 1555 2.39
LINK O5 CRB A 500 ZN ZN A 600 1555 1555 2.25
LINK OE2 GLU B 194 ZN ZN B 601 1555 1555 2.19
LINK NE2 HIS B 271 ZN ZN B 601 1555 1555 2.27
LINK NE2 HIS B 287 ZN ZN B 601 1555 1555 2.03
LINK O4 CRB B 501 ZN ZN B 601 1555 1555 2.30
LINK O5 CRB B 501 ZN ZN B 601 1555 1555 2.32
LINK OE2 GLU C 194 ZN ZN C 602 1555 1555 2.03
LINK NE2 HIS C 271 ZN ZN C 602 1555 1555 2.40
LINK NE2 HIS C 287 ZN ZN C 602 1555 1555 2.11
LINK O5 CRB C 502 ZN ZN C 602 1555 1555 2.38
LINK O4 CRB C 502 ZN ZN C 602 1555 1555 2.26
CISPEP 1 THR A 67 PRO A 68 0 -0.10
CISPEP 2 ASN A 100 PRO A 101 0 -1.08
CISPEP 3 THR A 282 PRO A 283 0 -0.47
CISPEP 4 THR B 67 PRO B 68 0 -0.21
CISPEP 5 ASN B 100 PRO B 101 0 0.02
CISPEP 6 THR B 282 PRO B 283 0 0.24
CISPEP 7 THR C 67 PRO C 68 0 0.72
CISPEP 8 ASN C 100 PRO C 101 0 -0.82
CISPEP 9 THR C 282 PRO C 283 0 0.02
SITE 1 AC1 4 GLU A 194 HIS A 271 HIS A 287 CRB A 500
SITE 1 AC2 4 GLU B 194 HIS B 271 HIS B 287 CRB B 501
SITE 1 AC3 5 ASP C 146 GLU C 194 HIS C 271 HIS C 287
SITE 2 AC3 5 CRB C 502
SITE 1 AC4 2 LYS C 89 HOH C2610
SITE 1 AC5 3 LYS A 89 LYS B 89 HOH B 629
SITE 1 AC6 3 ARG C 231 HOH C2698 HOH C2781
SITE 1 AC7 16 ASP A 44 ASN A 46 ILE A 47 GLY A 114
SITE 2 AC7 16 GLY A 115 VAL A 116 THR A 139 THR A 140
SITE 3 AC7 16 PHE A 179 THR A 182 LEU A 183 GLU A 187
SITE 4 AC7 16 ASN A 190 HOH A 619 HOH A 670 HOH A 676
SITE 1 AC8 15 ASP B 44 ASN B 46 ILE B 47 PRO B 79
SITE 2 AC8 15 GLY B 114 GLY B 115 VAL B 116 THR B 139
SITE 3 AC8 15 THR B 140 LEU B 142 PHE B 179 THR B 182
SITE 4 AC8 15 LEU B 183 GLU B 187 ASN B 190
SITE 1 AC9 15 ASP C 44 ASN C 46 ILE C 47 GLY C 114
SITE 2 AC9 15 GLY C 115 VAL C 116 THR C 139 THR C 140
SITE 3 AC9 15 LEU C 142 PHE C 179 THR C 182 LEU C 183
SITE 4 AC9 15 GLU C 187 ASN C 190 HOH C2741
SITE 1 BC1 15 ASP A 146 LYS A 152 ASN A 162 GLU A 194
SITE 2 BC1 15 LYS A 197 LYS A 250 ARG A 264 LEU A 267
SITE 3 BC1 15 ASN A 268 HIS A 271 HIS A 275 HIS A 287
SITE 4 BC1 15 LYS A 356 ZN A 600 ARG B 130
SITE 1 BC2 15 ARG A 130 ASP B 146 LYS B 152 ASN B 162
SITE 2 BC2 15 GLU B 194 LYS B 197 LYS B 250 ARG B 264
SITE 3 BC2 15 LEU B 267 ASN B 268 HIS B 271 HIS B 275
SITE 4 BC2 15 HIS B 287 LYS B 356 ZN B 601
SITE 1 BC3 15 ARG C 130 ASP C 146 LYS C 152 ASN C 162
SITE 2 BC3 15 GLU C 194 LYS C 197 LYS C 250 ARG C 264
SITE 3 BC3 15 LEU C 267 ASN C 268 HIS C 271 HIS C 275
SITE 4 BC3 15 HIS C 287 LYS C 356 ZN C 602
CRYST1 206.500 136.400 40.400 90.00 90.00 90.00 P 21 21 2 12
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 0.004843 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007331 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024752 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
