HEADER TRANSFERASE 02-JUL-08 3DNT
TITLE STRUCTURES OF MDT PROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN HIPA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: HIPA, B1507, JW1500;
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: PBAD22
KEYWDS MDT, PERSISTENCE, MULTIDRUG RESISTANCE, TOLERANCE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.SCHUMACHER
REVDAT 2 20-OCT-21 3DNT 1 REMARK SEQADV LINK
REVDAT 1 27-JAN-09 3DNT 0
JRNL AUTH M.A.SCHUMACHER,K.M.PIRO,W.XU,S.HANSEN,K.LEWIS,R.G.BRENNAN
JRNL TITL MOLECULAR MECHANISMS OF HIPA-MEDIATED MULTIDRUG TOLERANCE
JRNL TITL 2 AND ITS NEUTRALIZATION BY HIPB.
JRNL REF SCIENCE V. 323 396 2009
JRNL REFN ISSN 0036-8075
JRNL PMID 19150849
JRNL DOI 10.1126/SCIENCE.1163806
REMARK 2
REMARK 2 RESOLUTION. 1.66 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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1346396.860
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 89050
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 : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 16843
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 25546
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2688
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6596
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 827
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.45000
REMARK 3 B22 (A**2) : -2.61000
REMARK 3 B33 (A**2) : -2.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.71000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.21
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.000
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) : 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 : 0.36
REMARK 3 BSOL : 49.68
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 : ATP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ATP-TOP.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3DNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048267.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.989
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89050
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 42.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 1.0
REMARK 200 DATA REDUNDANCY IN SHELL : 425.0
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : 0.29500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 600, PH 9.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 42.04500
REMARK 290 SMTRY3 2 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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MSE A 1
REMARK 465 GLU A 106
REMARK 465 ASP A 107
REMARK 465 GLU A 108
REMARK 465 THR A 109
REMARK 465 VAL A 110
REMARK 465 THR A 111
REMARK 465 HIS A 112
REMARK 465 PRO A 113
REMARK 465 GLY A 185
REMARK 465 GLU A 186
REMARK 465 ILE A 187
REMARK 465 ARG A 188
REMARK 465 GLN A 189
REMARK 465 PRO A 190
REMARK 465 ASN A 191
REMARK 465 ALA A 192
REMARK 465 THR A 193
REMARK 465 LEU A 194
REMARK 465 ASP A 195
REMARK 465 LEU A 196
REMARK 465 SER A 197
REMARK 465 GLY A 438
REMARK 465 SER A 439
REMARK 465 LYS A 440
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 ILE B 184
REMARK 465 GLY B 185
REMARK 465 GLU B 186
REMARK 465 ILE B 187
REMARK 465 ARG B 188
REMARK 465 GLN B 189
REMARK 465 PRO B 190
REMARK 465 ASN B 191
REMARK 465 ALA B 192
REMARK 465 THR B 193
REMARK 465 LEU B 194
REMARK 465 ASP B 195
REMARK 465 LEU B 196
REMARK 465 SER B 197
REMARK 465 GLU B 436
REMARK 465 TYR B 437
REMARK 465 GLY B 438
REMARK 465 SER B 439
REMARK 465 LYS B 440
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 OE2 GLU A 243 O HOH A 965 2.16
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 39 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MSE A 388 CG - SE - CE ANGL. DEV. = 14.2 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 ASN A 9 -127.05 58.62
REMARK 500 ASN A 145 -6.87 -141.44
REMARK 500 PRO A 415 108.54 -53.81
REMARK 500 ASN B 9 -45.94 67.38
REMARK 500 ASN B 10 -5.83 -172.61
REMARK 500 ASP B 107 28.54 -79.38
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 MG A 441 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 314 OD1
REMARK 620 2 ASP A 332 OD2 80.7
REMARK 620 3 ATP A 500 O3B 173.3 92.7
REMARK 620 4 ATP A 500 O2A 87.0 89.0 91.7
REMARK 620 5 HOH A 860 O 93.2 173.3 93.5 93.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 442 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 332 OD1
REMARK 620 2 ASP A 332 OD2 52.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 442 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 314 OD1
REMARK 620 2 ASP B 332 OD2 91.3
REMARK 620 3 ATP B 501 O3B 171.2 84.3
REMARK 620 4 ATP B 501 O2A 96.9 90.5 90.8
REMARK 620 5 HOH B 835 O 88.7 179.0 95.5 90.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 441 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 332 OD1
REMARK 620 2 ASP B 332 OD2 59.2
REMARK 620 3 ATP B 501 O3G 161.9 110.2
REMARK 620 4 ATP B 501 O2B 74.0 79.3 90.0
REMARK 620 5 HOH B1058 O 101.8 159.4 85.7 88.0
REMARK 620 6 HOH B1165 O 90.1 93.6 105.9 164.0 94.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 442
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 833
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 441
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 442
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 834
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DNU RELATED DB: PDB
REMARK 900 RELATED ID: 3DNV RELATED DB: PDB
REMARK 900 RELATED ID: 3DNW RELATED DB: PDB
DBREF 3DNT A 1 440 UNP P23874 HIPA_ECOLI 1 440
DBREF 3DNT B 1 440 UNP P23874 HIPA_ECOLI 1 440
SEQADV 3DNT GLN A 309 UNP P23874 ASP 309 ENGINEERED MUTATION
SEQADV 3DNT GLN B 309 UNP P23874 ASP 309 ENGINEERED MUTATION
SEQRES 1 A 440 MSE PRO LYS LEU VAL THR TRP MSE ASN ASN GLN ARG VAL
SEQRES 2 A 440 GLY GLU LEU THR LYS LEU ALA ASN GLY ALA HIS THR PHE
SEQRES 3 A 440 LYS TYR ALA PRO GLU TRP LEU ALA SER ARG TYR ALA ARG
SEQRES 4 A 440 PRO LEU SER LEU SER LEU PRO LEU GLN ARG GLY ASN ILE
SEQRES 5 A 440 THR SER ASP ALA VAL PHE ASN PHE PHE ASP ASN LEU LEU
SEQRES 6 A 440 PRO ASP SER PRO ILE VAL ARG ASP ARG ILE VAL LYS ARG
SEQRES 7 A 440 TYR HIS ALA LYS SER ARG GLN PRO PHE ASP LEU LEU SER
SEQRES 8 A 440 GLU ILE GLY ARG ASP SER VAL GLY ALA VAL THR LEU ILE
SEQRES 9 A 440 PRO GLU ASP GLU THR VAL THR HIS PRO ILE MSE ALA TRP
SEQRES 10 A 440 GLU LYS LEU THR GLU ALA ARG LEU GLU GLU VAL LEU THR
SEQRES 11 A 440 ALA TYR LYS ALA ASP ILE PRO LEU GLY MSE ILE ARG GLU
SEQRES 12 A 440 GLU ASN ASP PHE ARG ILE SER VAL ALA GLY ALA GLN GLU
SEQRES 13 A 440 LYS THR ALA LEU LEU ARG ILE GLY ASN ASP TRP CYS ILE
SEQRES 14 A 440 PRO LYS GLY ILE THR PRO THR THR HIS ILE ILE LYS LEU
SEQRES 15 A 440 PRO ILE GLY GLU ILE ARG GLN PRO ASN ALA THR LEU ASP
SEQRES 16 A 440 LEU SER GLN SER VAL ASP ASN GLU TYR TYR CYS LEU LEU
SEQRES 17 A 440 LEU ALA LYS GLU LEU GLY LEU ASN VAL PRO ASP ALA GLU
SEQRES 18 A 440 ILE ILE LYS ALA GLY ASN VAL ARG ALA LEU ALA VAL GLU
SEQRES 19 A 440 ARG PHE ASP ARG ARG TRP ASN ALA GLU ARG THR VAL LEU
SEQRES 20 A 440 LEU ARG LEU PRO GLN GLU ASP MSE CYS GLN THR PHE GLY
SEQRES 21 A 440 LEU PRO SER SER VAL LYS TYR GLU SER ASP GLY GLY PRO
SEQRES 22 A 440 GLY ILE ALA ARG ILE MSE ALA PHE LEU MSE GLY SER SER
SEQRES 23 A 440 GLU ALA LEU LYS ASP ARG TYR ASP PHE MSE LYS PHE GLN
SEQRES 24 A 440 VAL PHE GLN TRP LEU ILE GLY ALA THR GLN GLY HIS ALA
SEQRES 25 A 440 LYS ASN PHE SER VAL PHE ILE GLN ALA GLY GLY SER TYR
SEQRES 26 A 440 ARG LEU THR PRO PHE TYR ASP ILE ILE SER ALA PHE PRO
SEQRES 27 A 440 VAL LEU GLY GLY THR GLY ILE HIS ILE SER ASP LEU LYS
SEQRES 28 A 440 LEU ALA MSE GLY LEU ASN ALA SER LYS GLY LYS LYS THR
SEQRES 29 A 440 ALA ILE ASP LYS ILE TYR PRO ARG HIS PHE LEU ALA THR
SEQRES 30 A 440 ALA LYS VAL LEU ARG PHE PRO GLU VAL GLN MSE HIS GLU
SEQRES 31 A 440 ILE LEU SER ASP PHE ALA ARG MSE ILE PRO ALA ALA LEU
SEQRES 32 A 440 ASP ASN VAL LYS THR SER LEU PRO THR ASP PHE PRO GLU
SEQRES 33 A 440 ASN VAL VAL THR ALA VAL GLU SER ASN VAL LEU ARG LEU
SEQRES 34 A 440 HIS GLY ARG LEU SER ARG GLU TYR GLY SER LYS
SEQRES 1 B 440 MSE PRO LYS LEU VAL THR TRP MSE ASN ASN GLN ARG VAL
SEQRES 2 B 440 GLY GLU LEU THR LYS LEU ALA ASN GLY ALA HIS THR PHE
SEQRES 3 B 440 LYS TYR ALA PRO GLU TRP LEU ALA SER ARG TYR ALA ARG
SEQRES 4 B 440 PRO LEU SER LEU SER LEU PRO LEU GLN ARG GLY ASN ILE
SEQRES 5 B 440 THR SER ASP ALA VAL PHE ASN PHE PHE ASP ASN LEU LEU
SEQRES 6 B 440 PRO ASP SER PRO ILE VAL ARG ASP ARG ILE VAL LYS ARG
SEQRES 7 B 440 TYR HIS ALA LYS SER ARG GLN PRO PHE ASP LEU LEU SER
SEQRES 8 B 440 GLU ILE GLY ARG ASP SER VAL GLY ALA VAL THR LEU ILE
SEQRES 9 B 440 PRO GLU ASP GLU THR VAL THR HIS PRO ILE MSE ALA TRP
SEQRES 10 B 440 GLU LYS LEU THR GLU ALA ARG LEU GLU GLU VAL LEU THR
SEQRES 11 B 440 ALA TYR LYS ALA ASP ILE PRO LEU GLY MSE ILE ARG GLU
SEQRES 12 B 440 GLU ASN ASP PHE ARG ILE SER VAL ALA GLY ALA GLN GLU
SEQRES 13 B 440 LYS THR ALA LEU LEU ARG ILE GLY ASN ASP TRP CYS ILE
SEQRES 14 B 440 PRO LYS GLY ILE THR PRO THR THR HIS ILE ILE LYS LEU
SEQRES 15 B 440 PRO ILE GLY GLU ILE ARG GLN PRO ASN ALA THR LEU ASP
SEQRES 16 B 440 LEU SER GLN SER VAL ASP ASN GLU TYR TYR CYS LEU LEU
SEQRES 17 B 440 LEU ALA LYS GLU LEU GLY LEU ASN VAL PRO ASP ALA GLU
SEQRES 18 B 440 ILE ILE LYS ALA GLY ASN VAL ARG ALA LEU ALA VAL GLU
SEQRES 19 B 440 ARG PHE ASP ARG ARG TRP ASN ALA GLU ARG THR VAL LEU
SEQRES 20 B 440 LEU ARG LEU PRO GLN GLU ASP MSE CYS GLN THR PHE GLY
SEQRES 21 B 440 LEU PRO SER SER VAL LYS TYR GLU SER ASP GLY GLY PRO
SEQRES 22 B 440 GLY ILE ALA ARG ILE MSE ALA PHE LEU MSE GLY SER SER
SEQRES 23 B 440 GLU ALA LEU LYS ASP ARG TYR ASP PHE MSE LYS PHE GLN
SEQRES 24 B 440 VAL PHE GLN TRP LEU ILE GLY ALA THR GLN GLY HIS ALA
SEQRES 25 B 440 LYS ASN PHE SER VAL PHE ILE GLN ALA GLY GLY SER TYR
SEQRES 26 B 440 ARG LEU THR PRO PHE TYR ASP ILE ILE SER ALA PHE PRO
SEQRES 27 B 440 VAL LEU GLY GLY THR GLY ILE HIS ILE SER ASP LEU LYS
SEQRES 28 B 440 LEU ALA MSE GLY LEU ASN ALA SER LYS GLY LYS LYS THR
SEQRES 29 B 440 ALA ILE ASP LYS ILE TYR PRO ARG HIS PHE LEU ALA THR
SEQRES 30 B 440 ALA LYS VAL LEU ARG PHE PRO GLU VAL GLN MSE HIS GLU
SEQRES 31 B 440 ILE LEU SER ASP PHE ALA ARG MSE ILE PRO ALA ALA LEU
SEQRES 32 B 440 ASP ASN VAL LYS THR SER LEU PRO THR ASP PHE PRO GLU
SEQRES 33 B 440 ASN VAL VAL THR ALA VAL GLU SER ASN VAL LEU ARG LEU
SEQRES 34 B 440 HIS GLY ARG LEU SER ARG GLU TYR GLY SER LYS
MODRES 3DNT MSE A 8 MET SELENOMETHIONINE
MODRES 3DNT MSE A 115 MET SELENOMETHIONINE
MODRES 3DNT MSE A 140 MET SELENOMETHIONINE
MODRES 3DNT MSE A 255 MET SELENOMETHIONINE
MODRES 3DNT MSE A 279 MET SELENOMETHIONINE
MODRES 3DNT MSE A 283 MET SELENOMETHIONINE
MODRES 3DNT MSE A 296 MET SELENOMETHIONINE
MODRES 3DNT MSE A 354 MET SELENOMETHIONINE
MODRES 3DNT MSE A 388 MET SELENOMETHIONINE
MODRES 3DNT MSE A 398 MET SELENOMETHIONINE
MODRES 3DNT MSE B 8 MET SELENOMETHIONINE
MODRES 3DNT MSE B 115 MET SELENOMETHIONINE
MODRES 3DNT MSE B 140 MET SELENOMETHIONINE
MODRES 3DNT MSE B 255 MET SELENOMETHIONINE
MODRES 3DNT MSE B 279 MET SELENOMETHIONINE
MODRES 3DNT MSE B 283 MET SELENOMETHIONINE
MODRES 3DNT MSE B 296 MET SELENOMETHIONINE
MODRES 3DNT MSE B 354 MET SELENOMETHIONINE
MODRES 3DNT MSE B 388 MET SELENOMETHIONINE
MODRES 3DNT MSE B 398 MET SELENOMETHIONINE
HET MSE A 8 8
HET MSE A 115 8
HET MSE A 140 8
HET MSE A 255 8
HET MSE A 279 8
HET MSE A 283 8
HET MSE A 296 8
HET MSE A 354 8
HET MSE A 388 8
HET MSE A 398 8
HET MSE B 8 8
HET MSE B 115 8
HET MSE B 140 8
HET MSE B 255 8
HET MSE B 279 8
HET MSE B 283 8
HET MSE B 296 8
HET MSE B 354 8
HET MSE B 388 8
HET MSE B 398 8
HET ATP A 500 31
HET MG A 441 1
HET MG A 442 1
HET SO4 A 833 5
HET ATP B 501 31
HET MG B 441 1
HET MG B 442 1
HET SO4 B 834 5
HETNAM MSE SELENOMETHIONINE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
FORMUL 4 MG 4(MG 2+)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 11 HOH *827(H2 O)
HELIX 1 1 ALA A 29 SER A 35 1 7
HELIX 2 2 SER A 54 ASN A 63 1 10
HELIX 3 3 SER A 68 HIS A 80 1 13
HELIX 4 4 GLN A 85 GLY A 94 1 10
HELIX 5 5 THR A 121 ALA A 131 1 11
HELIX 6 6 TYR A 132 ASP A 135 5 4
HELIX 7 7 ILE A 136 MSE A 140 5 5
HELIX 8 8 GLN A 198 LEU A 213 1 16
HELIX 9 9 MSE A 255 PHE A 259 1 5
HELIX 10 10 PRO A 262 LYS A 266 5 5
HELIX 11 11 TYR A 267 GLY A 271 5 5
HELIX 12 12 GLY A 274 MSE A 283 1 10
HELIX 13 13 GLU A 287 ILE A 305 1 19
HELIX 14 14 HIS A 311 ASN A 314 5 4
HELIX 15 15 ALA A 321 GLY A 323 5 3
HELIX 16 16 ALA A 336 LEU A 340 5 5
HELIX 17 17 HIS A 346 ASP A 349 5 4
HELIX 18 18 ASP A 367 ILE A 369 5 3
HELIX 19 19 TYR A 370 LEU A 381 1 12
HELIX 20 20 PRO A 384 LEU A 410 1 27
HELIX 21 21 PRO A 415 ARG A 435 1 21
HELIX 22 22 ALA B 29 ALA B 34 1 6
HELIX 23 23 SER B 54 ASN B 63 1 10
HELIX 24 24 SER B 68 HIS B 80 1 13
HELIX 25 25 GLN B 85 GLY B 94 1 10
HELIX 26 26 THR B 121 THR B 130 1 10
HELIX 27 27 ALA B 131 ASP B 135 5 5
HELIX 28 28 GLN B 198 LEU B 213 1 16
HELIX 29 29 MSE B 255 PHE B 259 1 5
HELIX 30 30 PRO B 262 LYS B 266 5 5
HELIX 31 31 TYR B 267 GLY B 271 5 5
HELIX 32 32 GLY B 274 MSE B 283 1 10
HELIX 33 33 GLU B 287 ILE B 305 1 19
HELIX 34 34 HIS B 311 ASN B 314 5 4
HELIX 35 35 ALA B 321 GLY B 323 5 3
HELIX 36 36 ALA B 336 LEU B 340 5 5
HELIX 37 37 HIS B 346 ASP B 349 5 4
HELIX 38 38 ASP B 367 ILE B 369 5 3
HELIX 39 39 TYR B 370 LEU B 381 1 12
HELIX 40 40 PRO B 384 SER B 409 1 26
HELIX 41 41 PRO B 415 GLY B 431 1 17
SHEET 1 A 5 ASN A 51 ILE A 52 0
SHEET 2 A 5 HIS A 24 TYR A 28 -1 N PHE A 26 O ILE A 52
SHEET 3 A 5 GLN A 11 LYS A 18 -1 N THR A 17 O THR A 25
SHEET 4 A 5 LYS A 3 MSE A 8 -1 N THR A 6 O VAL A 13
SHEET 5 A 5 THR A 102 ILE A 104 -1 O THR A 102 N TRP A 7
SHEET 1 B 6 TRP A 117 LYS A 119 0
SHEET 2 B 6 ASP A 166 PRO A 170 -1 O ILE A 169 N GLU A 118
SHEET 3 B 6 LYS A 157 ILE A 163 -1 N LEU A 161 O CYS A 168
SHEET 4 B 6 HIS A 178 LYS A 181 -1 O ILE A 180 N THR A 158
SHEET 5 B 6 VAL A 228 GLU A 234 -1 O VAL A 233 N ILE A 179
SHEET 6 B 6 ALA A 220 ALA A 225 -1 N GLU A 221 O ALA A 232
SHEET 1 C 2 ARG A 238 TRP A 240 0
SHEET 2 C 2 LEU A 247 ARG A 249 -1 O LEU A 248 N ARG A 239
SHEET 1 D 3 GLN A 252 ASP A 254 0
SHEET 2 D 3 SER A 316 ILE A 319 -1 O VAL A 317 N GLU A 253
SHEET 3 D 3 TYR A 325 LEU A 327 -1 O ARG A 326 N PHE A 318
SHEET 1 E 2 LYS A 351 ASN A 357 0
SHEET 2 E 2 LYS A 362 ALA A 365 -1 O LYS A 363 N LEU A 356
SHEET 1 F 5 ASN B 51 ILE B 52 0
SHEET 2 F 5 HIS B 24 TYR B 28 -1 N PHE B 26 O ILE B 52
SHEET 3 F 5 GLN B 11 LYS B 18 -1 N THR B 17 O THR B 25
SHEET 4 F 5 LEU B 4 MSE B 8 -1 N LEU B 4 O LEU B 16
SHEET 5 F 5 VAL B 101 PRO B 105 -1 O THR B 102 N TRP B 7
SHEET 1 G 6 TRP B 117 LYS B 119 0
SHEET 2 G 6 ASP B 166 PRO B 170 -1 O ILE B 169 N GLU B 118
SHEET 3 G 6 LYS B 157 ILE B 163 -1 N LEU B 161 O CYS B 168
SHEET 4 G 6 HIS B 178 LYS B 181 -1 O ILE B 180 N THR B 158
SHEET 5 G 6 VAL B 228 GLU B 234 -1 O VAL B 233 N ILE B 179
SHEET 6 G 6 ALA B 220 ALA B 225 -1 N GLU B 221 O ALA B 232
SHEET 1 H 2 ARG B 238 TRP B 240 0
SHEET 2 H 2 LEU B 247 ARG B 249 -1 O LEU B 248 N ARG B 239
SHEET 1 I 3 GLN B 252 ASP B 254 0
SHEET 2 I 3 SER B 316 ILE B 319 -1 O VAL B 317 N GLU B 253
SHEET 3 I 3 TYR B 325 LEU B 327 -1 O ARG B 326 N PHE B 318
SHEET 1 J 2 LYS B 351 ASN B 357 0
SHEET 2 J 2 LYS B 362 ALA B 365 -1 O LYS B 363 N LEU B 356
LINK C TRP A 7 N MSE A 8 1555 1555 1.33
LINK C MSE A 8 N ASN A 9 1555 1555 1.33
LINK C ILE A 114 N MSE A 115 1555 1555 1.34
LINK C MSE A 115 N ALA A 116 1555 1555 1.33
LINK C GLY A 139 N MSE A 140 1555 1555 1.33
LINK C MSE A 140 N ILE A 141 1555 1555 1.33
LINK C ASP A 254 N MSE A 255 1555 1555 1.33
LINK C MSE A 255 N CYS A 256 1555 1555 1.33
LINK C ILE A 278 N MSE A 279 1555 1555 1.34
LINK C MSE A 279 N ALA A 280 1555 1555 1.34
LINK C LEU A 282 N MSE A 283 1555 1555 1.33
LINK C MSE A 283 N GLY A 284 1555 1555 1.34
LINK C PHE A 295 N MSE A 296 1555 1555 1.34
LINK C MSE A 296 N LYS A 297 1555 1555 1.34
LINK C ALA A 353 N MSE A 354 1555 1555 1.33
LINK C MSE A 354 N GLY A 355 1555 1555 1.32
LINK C GLN A 387 N MSE A 388 1555 1555 1.33
LINK C MSE A 388 N HIS A 389 1555 1555 1.33
LINK C ARG A 397 N MSE A 398 1555 1555 1.34
LINK C MSE A 398 N ILE A 399 1555 1555 1.33
LINK C TRP B 7 N MSE B 8 1555 1555 1.33
LINK C MSE B 8 N ASN B 9 1555 1555 1.33
LINK C ILE B 114 N MSE B 115 1555 1555 1.33
LINK C MSE B 115 N ALA B 116 1555 1555 1.33
LINK C GLY B 139 N MSE B 140 1555 1555 1.33
LINK C MSE B 140 N ILE B 141 1555 1555 1.33
LINK C ASP B 254 N MSE B 255 1555 1555 1.34
LINK C MSE B 255 N CYS B 256 1555 1555 1.33
LINK C ILE B 278 N MSE B 279 1555 1555 1.34
LINK C MSE B 279 N ALA B 280 1555 1555 1.33
LINK C LEU B 282 N MSE B 283 1555 1555 1.32
LINK C MSE B 283 N GLY B 284 1555 1555 1.33
LINK C PHE B 295 N MSE B 296 1555 1555 1.34
LINK C MSE B 296 N LYS B 297 1555 1555 1.33
LINK C ALA B 353 N MSE B 354 1555 1555 1.33
LINK C MSE B 354 N GLY B 355 1555 1555 1.34
LINK C GLN B 387 N MSE B 388 1555 1555 1.33
LINK C MSE B 388 N HIS B 389 1555 1555 1.34
LINK C ARG B 397 N MSE B 398 1555 1555 1.34
LINK C MSE B 398 N ILE B 399 1555 1555 1.33
LINK OD1 ASN A 314 MG MG A 441 1555 1555 2.18
LINK OD2 ASP A 332 MG MG A 441 1555 1555 2.26
LINK OD1 ASP A 332 MG MG A 442 1555 1555 2.49
LINK OD2 ASP A 332 MG MG A 442 1555 1555 2.46
LINK MG MG A 441 O3B ATP A 500 1555 1555 2.31
LINK MG MG A 441 O2A ATP A 500 1555 1555 2.32
LINK MG MG A 441 O HOH A 860 1555 1555 2.20
LINK OD1 ASN B 314 MG MG B 442 1555 1555 2.11
LINK OD1 ASP B 332 MG MG B 441 1555 1555 2.29
LINK OD2 ASP B 332 MG MG B 441 1555 1555 2.16
LINK OD2 ASP B 332 MG MG B 442 1555 1555 2.12
LINK MG MG B 441 O3G ATP B 501 1555 1555 2.48
LINK MG MG B 441 O2B ATP B 501 1555 1555 2.39
LINK MG MG B 441 O HOH B1058 1555 1555 2.10
LINK MG MG B 441 O HOH B1165 1555 1555 2.20
LINK MG MG B 442 O3B ATP B 501 1555 1555 2.27
LINK MG MG B 442 O2A ATP B 501 1555 1555 2.16
LINK MG MG B 442 O HOH B 835 1555 1555 2.10
SITE 1 AC1 27 VAL A 98 ALA A 152 GLY A 153 ALA A 154
SITE 2 AC1 27 GLN A 155 LYS A 157 ILE A 179 LYS A 181
SITE 3 AC1 27 PRO A 218 VAL A 233 GLU A 234 ARG A 235
SITE 4 AC1 27 PHE A 236 ASP A 237 GLN A 252 HIS A 311
SITE 5 AC1 27 LYS A 313 ASN A 314 TYR A 331 ASP A 332
SITE 6 AC1 27 MG A 441 MG A 442 HOH A 860 HOH A 861
SITE 7 AC1 27 HOH A 867 HOH A 932 HOH A1063
SITE 1 AC2 4 ASN A 314 ASP A 332 ATP A 500 HOH A 860
SITE 1 AC3 3 GLN A 309 ASP A 332 ATP A 500
SITE 1 AC4 7 ALA A 358 SER A 359 LYS A 363 ARG A 372
SITE 2 AC4 7 HIS A 373 HOH A1014 HOH A1201
SITE 1 AC5 29 ASP B 67 VAL B 98 ALA B 152 GLY B 153
SITE 2 AC5 29 ALA B 154 GLN B 155 LYS B 157 ILE B 179
SITE 3 AC5 29 LYS B 181 VAL B 233 GLU B 234 ARG B 235
SITE 4 AC5 29 PHE B 236 ASP B 237 GLN B 252 HIS B 311
SITE 5 AC5 29 LYS B 313 ASN B 314 TYR B 331 ASP B 332
SITE 6 AC5 29 MG B 441 MG B 442 HOH B 835 HOH B 837
SITE 7 AC5 29 HOH B 842 HOH B 858 HOH B 861 HOH B1011
SITE 8 AC5 29 HOH B1145
SITE 1 AC6 4 ASP B 332 ATP B 501 HOH B1058 HOH B1165
SITE 1 AC7 4 ASN B 314 ASP B 332 ATP B 501 HOH B 835
SITE 1 AC8 5 ALA B 358 SER B 359 LYS B 363 ARG B 372
SITE 2 AC8 5 HIS B 373
CRYST1 68.540 84.090 69.250 90.00 91.56 90.00 P 1 21 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 0.014590 0.000000 0.000397 0.00000
SCALE2 0.000000 0.011892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014446 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
