HEADER HYDROLASE 19-JUL-05 2BWW
TITLE HIS350ALA ESCHERICHIA COLI AMINOPEPTIDASE P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE P;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMINOPEPTIDASE P, X-PRO AMINOPEPTIDASE, AMINOPEPTIDASE P II,
COMPND 5 APP-II, AMINOACYLPROLINE AMINOPEPTIDASE;
COMPND 6 EC: 3.4.11.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: AN1459;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: AN1459;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPL670/H350A
KEYWDS AMINOPEPTIDASE P, METALLOENZYME, 'PITA-BREAD' ENZYME, PROLINE-
KEYWDS 2 SPECIFIC ENZYME, MANGANESE ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.GRAHAM,J.M.GUSS
REVDAT 7 13-DEC-23 2BWW 1 REMARK LINK
REVDAT 6 15-MAY-19 2BWW 1 REMARK
REVDAT 5 08-MAY-19 2BWW 1 REMARK
REVDAT 4 20-JUN-18 2BWW 1 JRNL REMARK
REVDAT 3 13-JUL-11 2BWW 1 VERSN
REVDAT 2 24-FEB-09 2BWW 1 VERSN
REVDAT 1 25-JAN-06 2BWW 0
JRNL AUTH S.C.GRAHAM,P.E.LILLEY,M.LEE,P.M.SCHAEFFER,A.V.KRALICEK,
JRNL AUTH 2 N.E.DIXON,J.M.GUSS
JRNL TITL KINETIC AND CRYSTALLOGRAPHIC ANALYSIS OF MUTANT ESCHERICHIA
JRNL TITL 2 COLI AMINOPEPTIDASE P: INSIGHTS INTO SUBSTRATE RECOGNITION
JRNL TITL 3 AND THE MECHANISM OF CATALYSIS.
JRNL REF BIOCHEMISTRY V. 45 964 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16411772
JRNL DOI 10.1021/BI0518904
REMARK 2
REMARK 2 RESOLUTION. 2.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 32029
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 + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1630
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2219
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3484
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 58.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.33000
REMARK 3 B22 (A**2) : 1.33000
REMARK 3 B33 (A**2) : -2.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.213
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.361
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3602 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3287 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4886 ; 1.181 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7591 ; 0.754 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 439 ; 5.898 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;37.004 ;23.370
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 609 ;13.805 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;17.661 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 532 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4042 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 758 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 738 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3367 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1740 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2221 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 153 ; 0.132 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.305 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 70 ; 0.284 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.107 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2359 ; 0.756 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3526 ; 1.147 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1539 ; 1.660 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1357 ; 2.662 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 172
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0587 71.4038 69.4043
REMARK 3 T TENSOR
REMARK 3 T11: -0.0041 T22: 0.0359
REMARK 3 T33: -0.0771 T12: -0.0847
REMARK 3 T13: -0.0085 T23: -0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 1.2566 L22: 2.7165
REMARK 3 L33: 1.0101 L12: -0.7385
REMARK 3 L13: -0.3366 L23: 0.5587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0355 S12: -0.3685 S13: -0.0457
REMARK 3 S21: 0.4691 S22: 0.1234 S23: -0.0038
REMARK 3 S31: 0.0071 S32: 0.1299 S33: -0.0879
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 173 A 440
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8885 53.1221 41.0263
REMARK 3 T TENSOR
REMARK 3 T11: -0.0900 T22: -0.0489
REMARK 3 T33: -0.1212 T12: -0.0517
REMARK 3 T13: 0.0228 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.8127 L22: 1.6569
REMARK 3 L33: 1.0380 L12: -0.0205
REMARK 3 L13: -0.1286 L23: 0.5294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0431 S12: 0.0140 S13: 0.1484
REMARK 3 S21: -0.2204 S22: 0.0340 S23: -0.2024
REMARK 3 S31: -0.0814 S32: 0.2258 S33: -0.0772
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. PEPTIDE BOND BETWEEN RESIDUES 88 AND 89 IS COMPLETELY
REMARK 3 DISORDERED AND COULD NOT BE MODELLED. INSUFFICIENT DENSITY WAS
REMARK 3 PRESENT FOR COMPLETE MODELLING OF RESIDUES 439 AND 440
REMARK 4
REMARK 4 2BWW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1290024956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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 RU200H
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33663
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 74.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: PDB ENTRY 2BHC
REMARK 200
REMARK 200 REMARK: STARTING MODEL WAS STRIPPED OF HETATMS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 77.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOUR DIFFUSION AT 4C. 2
REMARK 280 UL 7 MG/ML APPRO PLUS 2 UL RESERVOIR SOLUTION: 28% MPD, 0.1 M
REMARK 280 CITRATE PH 7.5, 0.2 M MGACETATE. SOAKED IN RESERVOIR SOLUTION
REMARK 280 SUPPLEMENTED WITH 1 MM MNCL2 FOR 30 MIN AT 4C PRIOR TO
REMARK 280 CRYOCOOLING., PH 7.50, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 69.08500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 69.08500
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.64800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 69.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.82400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 69.08500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 173.47200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 69.08500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 173.47200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.08500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 57.82400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 69.08500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 69.08500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 115.64800
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 69.08500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 69.08500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 115.64800
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 69.08500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 173.47200
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 69.08500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 57.82400
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 69.08500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 57.82400
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 69.08500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 173.47200
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 69.08500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 69.08500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 115.64800
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
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 0.000000 -1.000000 0.000000 69.08500
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 69.08500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 115.64800
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -69.08500
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 69.08500
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 115.64800
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 138.17000
REMARK 350 BIOMT3 4 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 A2030 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2032 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, HIS 350 TO ALA
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 439 CG CD CE NZ
REMARK 470 GLN A 440 O CG CD OE1 NE2
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 TRP A 88 C O
REMARK 480 PHE A 89 N
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 ALA A 37 -131.67 63.53
REMARK 500 THR A 53 -32.04 -133.45
REMARK 500 ASN A 56 41.36 -102.96
REMARK 500 ASP A 82 114.21 -168.34
REMARK 500 TRP A 88 -97.47 -77.37
REMARK 500 ARG A 91 150.20 -41.83
REMARK 500 HIS A 243 59.18 -99.55
REMARK 500 LYS A 425 -21.74 -145.68
REMARK 500 LYS A 439 55.84 -95.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2003 DISTANCE = 6.58 ANGSTROMS
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 MN A1442 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 260 OD1
REMARK 620 2 ASP A 260 OD2 55.4
REMARK 620 3 ASP A 271 OD1 84.4 139.5
REMARK 620 4 GLU A 406 OE1 102.1 103.9 87.3
REMARK 620 5 HOH A2151 O 157.4 102.2 117.5 85.5
REMARK 620 6 HOH A2152 O 95.4 89.1 90.7 162.0 79.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1441 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 271 OD2
REMARK 620 2 HIS A 354 NE2 95.7
REMARK 620 3 GLU A 383 OE2 152.9 81.1
REMARK 620 4 GLU A 406 OE2 79.2 131.6 83.0
REMARK 620 5 HOH A2151 O 109.2 124.2 94.4 102.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1443 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2088 O
REMARK 620 2 HOH A2089 O 89.6
REMARK 620 3 HOH A2090 O 177.7 90.8
REMARK 620 4 HOH A2130 O 91.8 87.4 90.5
REMARK 620 5 HOH A2132 O 89.1 176.3 90.7 89.2
REMARK 620 6 HOH A2133 O 87.3 91.3 90.4 178.4 92.1
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 MN A1441
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1442
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1443
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A1444
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A1445
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A16 RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU
REMARK 900 RELATED ID: 1AZ9 RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P FROM E. COLI
REMARK 900 RELATED ID: 1JAW RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P FROM E. COLI LOW PH FORM
REMARK 900 RELATED ID: 1M35 RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1N51 RELATED DB: PDB
REMARK 900 AMINOPEPTIDASE P IN COMPLEX WITH THE INHIBITOR APSTATIN
REMARK 900 RELATED ID: 1W2M RELATED DB: PDB
REMARK 900 CA-SUBSTITUTED FORM OF E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 1W7V RELATED DB: PDB
REMARK 900 ZNMG SUBSTRITUTED AMINOPEPTIDASE P FROM E. COLI
REMARK 900 RELATED ID: 1WBQ RELATED DB: PDB
REMARK 900 ZNMG SUBSTITUTED AMINOPEPTIDASE P FROM E. COLI
REMARK 900 RELATED ID: 2BH3 RELATED DB: PDB
REMARK 900 ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT
REMARK 900 RELATED ID: 2BHA RELATED DB: PDB
REMARK 900 E. COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE
REMARK 900 RELATED ID: 2BHB RELATED DB: PDB
REMARK 900 ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BHC RELATED DB: PDB
REMARK 900 NA SUBSTITUTED E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BHD RELATED DB: PDB
REMARK 900 MG SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH A PRODUCT-
REMARK 900 LIKE INHIBITOR
REMARK 900 RELATED ID: 2BN7 RELATED DB: PDB
REMARK 900 MN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT AND
REMARK 900 ZN
REMARK 900 RELATED ID: 2BWS RELATED DB: PDB
REMARK 900 HIS243ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWT RELATED DB: PDB
REMARK 900 ASP260ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWU RELATED DB: PDB
REMARK 900 ASP271ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWV RELATED DB: PDB
REMARK 900 HIS361ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWX RELATED DB: PDB
REMARK 900 HIS354ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 2BWY RELATED DB: PDB
REMARK 900 GLU383ALA E. COLI AMINOPEPTIDASE P
REMARK 900 RELATED ID: 1WL9 RELATED DB: PDB
REMARK 900 NATIVE (DI-MANAGANESE) AMINOPEPTIDASE P
REMARK 900 RELATED ID: 1WL6 RELATED DB: PDB
REMARK 900 MG-SUBSTITUTED AMINOPEPTIDASE P
REMARK 900 RELATED ID: 1WLR RELATED DB: PDB
REMARK 900 APO AMINOPEPTIDASE P
DBREF 2BWW A 1 440 UNP P15034 AMPP_ECOLI 1 440
SEQADV 2BWW ALA A 350 UNP P15034 HIS 350 ENGINEERED MUTATION
SEQRES 1 A 440 SER GLU ILE SER ARG GLN GLU PHE GLN ARG ARG ARG GLN
SEQRES 2 A 440 ALA LEU VAL GLU GLN MET GLN PRO GLY SER ALA ALA LEU
SEQRES 3 A 440 ILE PHE ALA ALA PRO GLU VAL THR ARG SER ALA ASP SER
SEQRES 4 A 440 GLU TYR PRO TYR ARG GLN ASN SER ASP PHE TRP TYR PHE
SEQRES 5 A 440 THR GLY PHE ASN GLU PRO GLU ALA VAL LEU VAL LEU ILE
SEQRES 6 A 440 LYS SER ASP ASP THR HIS ASN HIS SER VAL LEU PHE ASN
SEQRES 7 A 440 ARG VAL ARG ASP LEU THR ALA GLU ILE TRP PHE GLY ARG
SEQRES 8 A 440 ARG LEU GLY GLN ASP ALA ALA PRO GLU LYS LEU GLY VAL
SEQRES 9 A 440 ASP ARG ALA LEU ALA PHE SER GLU ILE ASN GLN GLN LEU
SEQRES 10 A 440 TYR GLN LEU LEU ASN GLY LEU ASP VAL VAL TYR HIS ALA
SEQRES 11 A 440 GLN GLY GLU TYR ALA TYR ALA ASP VAL ILE VAL ASN SER
SEQRES 12 A 440 ALA LEU GLU LYS LEU ARG LYS GLY SER ARG GLN ASN LEU
SEQRES 13 A 440 THR ALA PRO ALA THR MET ILE ASP TRP ARG PRO VAL VAL
SEQRES 14 A 440 HIS GLU MET ARG LEU PHE LYS SER PRO GLU GLU ILE ALA
SEQRES 15 A 440 VAL LEU ARG ARG ALA GLY GLU ILE THR ALA MET ALA HIS
SEQRES 16 A 440 THR ARG ALA MET GLU LYS CYS ARG PRO GLY MET PHE GLU
SEQRES 17 A 440 TYR HIS LEU GLU GLY GLU ILE HIS HIS GLU PHE ASN ARG
SEQRES 18 A 440 HIS GLY ALA ARG TYR PRO SER TYR ASN THR ILE VAL GLY
SEQRES 19 A 440 SER GLY GLU ASN GLY CYS ILE LEU HIS TYR THR GLU ASN
SEQRES 20 A 440 GLU CYS GLU MET ARG ASP GLY ASP LEU VAL LEU ILE ASP
SEQRES 21 A 440 ALA GLY CYS GLU TYR LYS GLY TYR ALA GLY ASP ILE THR
SEQRES 22 A 440 ARG THR PHE PRO VAL ASN GLY LYS PHE THR GLN ALA GLN
SEQRES 23 A 440 ARG GLU ILE TYR ASP ILE VAL LEU GLU SER LEU GLU THR
SEQRES 24 A 440 SER LEU ARG LEU TYR ARG PRO GLY THR SER ILE LEU GLU
SEQRES 25 A 440 VAL THR GLY GLU VAL VAL ARG ILE MET VAL SER GLY LEU
SEQRES 26 A 440 VAL LYS LEU GLY ILE LEU LYS GLY ASP VAL ASP GLU LEU
SEQRES 27 A 440 ILE ALA GLN ASN ALA HIS ARG PRO PHE PHE MET ALA GLY
SEQRES 28 A 440 LEU SER HIS TRP LEU GLY LEU ASP VAL HIS ASP VAL GLY
SEQRES 29 A 440 VAL TYR GLY GLN ASP ARG SER ARG ILE LEU GLU PRO GLY
SEQRES 30 A 440 MET VAL LEU THR VAL GLU PRO GLY LEU TYR ILE ALA PRO
SEQRES 31 A 440 ASP ALA GLU VAL PRO GLU GLN TYR ARG GLY ILE GLY ILE
SEQRES 32 A 440 ARG ILE GLU ASP ASP ILE VAL ILE THR GLU THR GLY ASN
SEQRES 33 A 440 GLU ASN LEU THR ALA SER VAL VAL LYS LYS PRO GLU GLU
SEQRES 34 A 440 ILE GLU ALA LEU MET VAL ALA ALA ARG LYS GLN
HET MN A1441 1
HET MN A1442 1
HET MG A1443 1
HET FLC A1444 13
HET MRD A1445 8
HETNAM MN MANGANESE (II) ION
HETNAM MG MAGNESIUM ION
HETNAM FLC CITRATE ANION
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 2 MN 2(MN 2+)
FORMUL 4 MG MG 2+
FORMUL 5 FLC C6 H5 O7 3-
FORMUL 6 MRD C6 H14 O2
FORMUL 7 HOH *152(H2 O)
HELIX 1 1 SER A 4 MET A 19 1 16
HELIX 2 2 ASN A 46 GLY A 54 1 9
HELIX 3 3 ASP A 82 GLY A 90 1 9
HELIX 4 4 ALA A 97 GLY A 103 1 7
HELIX 5 5 GLU A 112 ASN A 122 1 11
HELIX 6 6 TYR A 134 LYS A 150 1 17
HELIX 7 7 GLY A 151 ASN A 155 5 5
HELIX 8 8 TRP A 165 PHE A 175 1 11
HELIX 9 9 SER A 177 CYS A 202 1 26
HELIX 10 10 PHE A 207 HIS A 222 1 16
HELIX 11 11 GLU A 237 ILE A 241 5 5
HELIX 12 12 THR A 283 TYR A 304 1 22
HELIX 13 13 SER A 309 LEU A 328 1 20
HELIX 14 14 ASP A 334 GLN A 341 1 8
HELIX 15 15 GLY A 367 SER A 371 5 5
HELIX 16 16 PRO A 395 ARG A 399 5 5
HELIX 17 17 LYS A 426 ARG A 438 1 13
SHEET 1 AA 6 ARG A 106 ALA A 109 0
SHEET 2 AA 6 ASN A 72 ASN A 78 1 O SER A 74 N ARG A 106
SHEET 3 AA 6 VAL A 61 LYS A 66 -1 O VAL A 61 N PHE A 77
SHEET 4 AA 6 SER A 23 PHE A 28 -1 O SER A 23 N LYS A 66
SHEET 5 AA 6 VAL A 126 HIS A 129 1 O VAL A 126 N ALA A 24
SHEET 6 AA 6 THR A 161 ILE A 163 1 O THR A 161 N VAL A 127
SHEET 1 AB 2 THR A 34 SER A 36 0
SHEET 2 AB 2 SER A 39 GLU A 40 -1 O SER A 39 N ARG A 35
SHEET 1 AC 3 ILE A 232 SER A 235 0
SHEET 2 AC 3 LEU A 256 ALA A 261 -1 O LEU A 258 N GLY A 234
SHEET 3 AC 3 ILE A 272 PRO A 277 -1 O ILE A 272 N ALA A 261
SHEET 1 AD 2 GLU A 264 TYR A 265 0
SHEET 2 AD 2 TYR A 268 ALA A 269 -1 O TYR A 268 N TYR A 265
SHEET 1 AE 3 VAL A 379 VAL A 382 0
SHEET 2 AE 3 ASP A 407 ILE A 411 -1 O ASP A 407 N VAL A 382
SHEET 3 AE 3 ASN A 416 ASN A 418 -1 O GLU A 417 N VAL A 410
SHEET 1 AF 2 GLY A 385 ILE A 388 0
SHEET 2 AF 2 ILE A 401 ARG A 404 -1 O ILE A 401 N ILE A 388
LINK OD1 ASP A 260 MN MN A1442 1555 1555 2.37
LINK OD2 ASP A 260 MN MN A1442 1555 1555 2.28
LINK OD2 ASP A 271 MN MN A1441 1555 1555 2.16
LINK OD1 ASP A 271 MN MN A1442 1555 1555 2.15
LINK NE2 HIS A 354 MN MN A1441 1555 1555 2.15
LINK OE2 GLU A 383 MN MN A1441 1555 1555 2.43
LINK OE2 GLU A 406 MN MN A1441 1555 1555 2.08
LINK OE1 GLU A 406 MN MN A1442 1555 1555 2.18
LINK MN MN A1441 O HOH A2151 1555 1555 1.99
LINK MN MN A1442 O HOH A2151 1555 1555 2.39
LINK MN MN A1442 O HOH A2152 1555 1555 2.30
LINK MG MG A1443 O HOH A2088 1555 6555 2.16
LINK MG MG A1443 O HOH A2089 1555 6555 2.16
LINK MG MG A1443 O HOH A2090 1555 6555 2.17
LINK MG MG A1443 O HOH A2130 1555 1555 2.16
LINK MG MG A1443 O HOH A2132 1555 1555 2.18
LINK MG MG A1443 O HOH A2133 1555 1555 2.16
SITE 1 AC1 7 ASP A 271 HIS A 354 GLU A 383 GLU A 406
SITE 2 AC1 7 MN A1442 HOH A2115 HOH A2151
SITE 1 AC2 7 ASP A 260 ASP A 271 THR A 273 GLU A 406
SITE 2 AC2 7 MN A1441 HOH A2151 HOH A2152
SITE 1 AC3 6 HOH A2088 HOH A2089 HOH A2090 HOH A2130
SITE 2 AC3 6 HOH A2132 HOH A2133
SITE 1 AC4 4 ARG A 186 MET A 193 ARG A 221 HIS A 222
SITE 1 AC5 5 LEU A 242 HIS A 243 ARG A 404 HOH A2115
SITE 2 AC5 5 HOH A2151
CRYST1 138.170 138.170 231.296 90.00 90.00 90.00 I 41 2 2 16
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 0.007237 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007237 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004323 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
