HEADER OXIDOREDUCTASE 01-SEP-99 1CZ3
TITLE DIHYDROFOLATE REDUCTASE FROM THERMOTOGA MARITIMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PTD(TRC)
KEYWDS DIMER, HYPERTHERMOPHILE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.DAMS,G.AUERBACH,G.BADER,T.PLOOM,R.HUBER,R.JAENICKE
REVDAT 3 07-FEB-24 1CZ3 1 REMARK
REVDAT 2 24-FEB-09 1CZ3 1 VERSN
REVDAT 1 31-MAR-00 1CZ3 0
JRNL AUTH T.DAMS,G.AUERBACH,G.BADER,U.JACOB,T.PLOOM,R.HUBER,R.JAENICKE
JRNL TITL THE CRYSTAL STRUCTURE OF DIHYDROFOLATE REDUCTASE FROM
JRNL TITL 2 THERMOTOGA MARITIMA: MOLECULAR FEATURES OF THERMOSTABILITY.
JRNL REF J.MOL.BIOL. V. 297 659 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10731419
JRNL DOI 10.1006/JMBI.2000.3570
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1611838.040
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 18905
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) : 0.203
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 913
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2904
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 132
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2685
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.14000
REMARK 3 B22 (A**2) : 11.94000
REMARK 3 B33 (A**2) : -5.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.77000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.30
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 61.21
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.PA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARA
REMARK 3 PARAMETER FILE 3 : NDP.PAR
REMARK 3 PARAMETER FILE 4 : MTX.PAR
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NDP.TOP
REMARK 3 TOPOLOGY FILE 4 : MTX.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009633.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-97
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 7.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19395
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 9.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9100
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) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.51700
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M (NH4)2SO4 25 MM TRIS/HCL 0.5 MM
REMARK 280 EDTA, PH 7.0, VAPOR DIFFUSION, HANGING DROP, 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 65.80250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.02550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.80250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.02550
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: 3440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 LYS A 165
REMARK 465 SER A 166
REMARK 465 HIS A 167
REMARK 465 ARG A 168
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 20 CB CG CD OE1 OE2
REMARK 480 LYS A 33 CD CE NZ
REMARK 480 GLU A 37 CD OE1 OE2
REMARK 480 ARG A 45 NE CZ NH1 NH2
REMARK 480 ARG A 53 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 65 CB CG CD NE CZ NH1 NH2
REMARK 480 ARG A 66 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS A 68 CB CG CD CE NZ
REMARK 480 THR A 69 CB OG1 CG2
REMARK 480 ASN A 71 CB CG OD1 ND2
REMARK 480 ASN A 79 CG OD1 ND2
REMARK 480 LYS A 87 CD CE NZ
REMARK 480 GLU A 108 CD OE1 OE2
REMARK 480 GLU A 112 CD OE1 OE2
REMARK 480 LYS A 129 CD CE NZ
REMARK 480 LYS A 144 NZ
REMARK 480 GLU A 153 CD OE1 OE2
REMARK 480 GLU B 20 CB CG CD OE1 OE2
REMARK 480 ARG B 65 CG CD NE CZ NH1 NH2
REMARK 480 ARG B 66 CB CG CD NE CZ NH1 NH2
REMARK 480 ASN B 79 CB CG OD1 ND2
REMARK 480 GLU B 95 CG CD OE1 OE2
REMARK 480 LYS B 129 CG CD CE NZ
REMARK 480 GLU B 136 CB CG CD OE1 OE2
REMARK 480 LYS B 165 CB CG CD CE NZ
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 GLY A 101 N - CA - C ANGL. DEV. = 16.5 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 PRO A 124 66.12 -68.34
REMARK 500 GLU A 147 147.54 -170.27
REMARK 500 ASN B 71 55.94 -99.60
REMARK 500 VAL B 115 125.67 -170.23
REMARK 500 PRO B 124 69.30 -69.43
REMARK 500 ASP B 135 -82.51 -79.60
REMARK 500 GLU B 136 145.61 -173.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 300
DBREF 1CZ3 A 1 168 UNP Q60034 DYR_THEMA 2 169
DBREF 1CZ3 B 1 168 UNP Q60034 DYR_THEMA 2 169
SEQRES 1 A 168 ALA LYS VAL ILE PHE VAL LEU ALA MET ASP VAL SER GLY
SEQRES 2 A 168 LYS ILE ALA SER SER VAL GLU SER TRP SER SER PHE GLU
SEQRES 3 A 168 ASP ARG LYS ASN PHE ARG LYS ILE THR THR GLU ILE GLY
SEQRES 4 A 168 ASN VAL VAL MET GLY ARG ILE THR PHE GLU GLU ILE GLY
SEQRES 5 A 168 ARG PRO LEU PRO GLU ARG LEU ASN VAL VAL LEU THR ARG
SEQRES 6 A 168 ARG PRO LYS THR SER ASN ASN PRO SER LEU VAL PHE PHE
SEQRES 7 A 168 ASN GLY SER PRO ALA ASP VAL VAL LYS PHE LEU GLU GLY
SEQRES 8 A 168 LYS GLY TYR GLU ARG VAL ALA VAL ILE GLY GLY LYS THR
SEQRES 9 A 168 VAL PHE THR GLU PHE LEU ARG GLU LYS LEU VAL ASP GLU
SEQRES 10 A 168 LEU PHE VAL THR VAL GLU PRO TYR VAL PHE GLY LYS GLY
SEQRES 11 A 168 ILE PRO PHE PHE ASP GLU PHE GLU GLY TYR PHE PRO LEU
SEQRES 12 A 168 LYS LEU LEU GLU MET ARG ARG LEU ASN GLU ARG GLY THR
SEQRES 13 A 168 LEU PHE LEU LYS TYR SER VAL GLU LYS SER HIS ARG
SEQRES 1 B 168 ALA LYS VAL ILE PHE VAL LEU ALA MET ASP VAL SER GLY
SEQRES 2 B 168 LYS ILE ALA SER SER VAL GLU SER TRP SER SER PHE GLU
SEQRES 3 B 168 ASP ARG LYS ASN PHE ARG LYS ILE THR THR GLU ILE GLY
SEQRES 4 B 168 ASN VAL VAL MET GLY ARG ILE THR PHE GLU GLU ILE GLY
SEQRES 5 B 168 ARG PRO LEU PRO GLU ARG LEU ASN VAL VAL LEU THR ARG
SEQRES 6 B 168 ARG PRO LYS THR SER ASN ASN PRO SER LEU VAL PHE PHE
SEQRES 7 B 168 ASN GLY SER PRO ALA ASP VAL VAL LYS PHE LEU GLU GLY
SEQRES 8 B 168 LYS GLY TYR GLU ARG VAL ALA VAL ILE GLY GLY LYS THR
SEQRES 9 B 168 VAL PHE THR GLU PHE LEU ARG GLU LYS LEU VAL ASP GLU
SEQRES 10 B 168 LEU PHE VAL THR VAL GLU PRO TYR VAL PHE GLY LYS GLY
SEQRES 11 B 168 ILE PRO PHE PHE ASP GLU PHE GLU GLY TYR PHE PRO LEU
SEQRES 12 B 168 LYS LEU LEU GLU MET ARG ARG LEU ASN GLU ARG GLY THR
SEQRES 13 B 168 LEU PHE LEU LYS TYR SER VAL GLU LYS SER HIS ARG
HET SO4 A 200 5
HET SO4 B 300 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *204(H2 O)
HELIX 1 1 SER A 24 GLY A 39 1 16
HELIX 2 2 ARG A 45 GLY A 52 1 8
HELIX 3 3 SER A 81 LYS A 92 1 12
HELIX 4 4 GLY A 102 GLU A 112 1 11
HELIX 5 5 SER B 24 GLY B 39 1 16
HELIX 6 6 ARG B 45 GLY B 52 1 8
HELIX 7 7 SER B 81 GLY B 91 1 11
HELIX 8 8 GLY B 102 GLU B 112 1 11
SHEET 1 A 9 LEU A 75 PHE A 78 0
SHEET 2 A 9 LEU A 59 LEU A 63 1 O ASN A 60 N VAL A 76
SHEET 3 A 9 ASN A 40 GLY A 44 1 O VAL A 41 N VAL A 61
SHEET 4 A 9 ARG A 96 GLY A 101 1 O ALA A 98 N VAL A 42
SHEET 5 A 9 LYS A 2 MET A 9 1 O LYS A 2 N VAL A 97
SHEET 6 A 9 GLU A 117 VAL A 122 1 O GLU A 117 N PHE A 5
SHEET 7 A 9 LEU A 157 VAL A 163 -1 O LEU A 157 N VAL A 122
SHEET 8 A 9 TYR A 140 ARG A 150 -1 O LYS A 144 N SER A 162
SHEET 9 A 9 TYR B 125 PHE B 127 -1 O VAL B 126 N PHE A 141
SHEET 1 B 2 LYS A 14 ALA A 16 0
SHEET 2 B 2 ILE A 131 PRO A 132 -1 O ILE A 131 N ILE A 15
SHEET 1 C 9 TYR A 125 PHE A 127 0
SHEET 2 C 9 TYR B 140 ARG B 150 -1 N PHE B 141 O VAL A 126
SHEET 3 C 9 LEU B 157 VAL B 163 -1 N PHE B 158 O ARG B 149
SHEET 4 C 9 GLU B 117 VAL B 122 -1 O LEU B 118 N TYR B 161
SHEET 5 C 9 LYS B 2 MET B 9 1 O VAL B 3 N GLU B 117
SHEET 6 C 9 ARG B 96 GLY B 101 1 O VAL B 97 N ILE B 4
SHEET 7 C 9 ASN B 40 GLY B 44 1 N VAL B 42 O ALA B 98
SHEET 8 C 9 LEU B 59 LEU B 63 1 O LEU B 59 N VAL B 41
SHEET 9 C 9 LEU B 75 PHE B 78 1 O VAL B 76 N VAL B 62
SHEET 1 D 2 LYS B 14 ALA B 16 0
SHEET 2 D 2 ILE B 131 PRO B 132 -1 O ILE B 131 N ILE B 15
SITE 1 AC1 9 GLY A 44 ILE A 46 THR A 47 GLY A 101
SITE 2 AC1 9 GLY A 102 LYS A 103 THR A 104 VAL A 105
SITE 3 AC1 9 HOH A 701
SITE 1 AC2 10 GLY B 44 ARG B 45 ILE B 46 THR B 47
SITE 2 AC2 10 GLY B 101 GLY B 102 LYS B 103 THR B 104
SITE 3 AC2 10 VAL B 105 HOH B 529
CRYST1 131.605 36.051 97.025 90.00 130.69 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007598 0.000000 0.006534 0.00000
SCALE2 0.000000 0.027738 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013593 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
