HEADER HYDROLASE/HYDROLASE INHIBITOR 27-AUG-12 4GSC
TITLE STRUCTURE ANALYSIS OF INSULIN DEGRADING ENZYME WITH COMPOUND BDM41559
TITLE 2 ((S)-2-[2-(CARBOXYMETHYL-PHENETHYL-AMINO)-ACETYLAMINO]-3-(1H-
TITLE 3 IMIDAZOL-4-YL)-PROPIONIC ACID METHYL ESTER)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-DEGRADING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 42-1019;
COMPND 5 SYNONYM: ABETA-DEGRADING PROTEASE, INSULIN PROTEASE, INSULINASE,
COMPND 6 INSULYSIN;
COMPND 7 EC: 3.4.24.56;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IDE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INSULIN DEGRADING ENZYME, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.GUO,R.DEPREZ-POULAIN,B.DEPREZ,W.J.TANG
REVDAT 4 13-SEP-23 4GSC 1 REMARK SEQADV LINK
REVDAT 3 28-MAY-14 4GSC 1 JRNL
REVDAT 2 16-APR-14 4GSC 1 JRNL
REVDAT 1 28-AUG-13 4GSC 0
JRNL AUTH J.CHARTON,M.GAURIOT,Q.GUO,N.HENNUYER,X.MARECHAL,J.DUMONT,
JRNL AUTH 2 M.HAMDANE,V.POTTIEZ,V.LANDRY,O.SPERANDIO,M.FLIPO,L.BUEE,
JRNL AUTH 3 B.STAELS,F.LEROUX,W.J.TANG,B.DEPREZ,R.DEPREZ-POULAIN
JRNL TITL IMIDAZOLE-DERIVED 2-[N-CARBAMOYLMETHYL-ALKYLAMINO]ACETIC
JRNL TITL 2 ACIDS, SUBSTRATE-DEPENDENT MODULATORS OF INSULIN-DEGRADING
JRNL TITL 3 ENZYME IN AMYLOID-BETA HYDROLYSIS.
JRNL REF EUR.J.MED.CHEM. V. 79 184 2014
JRNL REFN ISSN 0223-5234
JRNL PMID 24735644
JRNL DOI 10.1016/J.EJMECH.2014.04.009
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 75029
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3992
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) : 2.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3771
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15620
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : 0.09000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.05000
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): 0.677
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.345
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.242
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.381
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16068 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21735 ; 1.875 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1908 ; 7.000 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 795 ;37.626 ;24.516
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2868 ;21.849 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 82 ;22.181 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2334 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12262 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 9574 ; 0.706 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15494 ; 1.440 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6494 ; 2.341 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6241 ; 4.099 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 4GSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9597
REMARK 200 MONOCHROMATOR : MAR 345
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75029
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.810
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 2WBY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-13% PEG MME 5000, 100 MM HEPES PH
REMARK 280 7.0, 4-14% TACSIMATE, 10% DIOXANE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.84000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.42000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.63000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 15.21000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.05000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A 30
REMARK 465 HIS A 31
REMARK 465 HIS A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 GLY A 39
REMARK 465 ILE A 40
REMARK 465 PRO A 41
REMARK 465 ASN A 966
REMARK 465 PRO A 967
REMARK 465 VAL A 968
REMARK 465 VAL A 969
REMARK 465 GLY A 970
REMARK 465 GLU A 971
REMARK 465 PHE A 972
REMARK 465 PRO A 973
REMARK 465 ALA A 974
REMARK 465 GLN A 975
REMARK 465 ASN A 976
REMARK 465 ASP A 977
REMARK 465 ILE A 978
REMARK 465 ASN A 1013
REMARK 465 PHE A 1014
REMARK 465 MET A 1015
REMARK 465 ALA A 1016
REMARK 465 ALA A 1017
REMARK 465 LYS A 1018
REMARK 465 LEU A 1019
REMARK 465 MET B 30
REMARK 465 HIS B 31
REMARK 465 HIS B 32
REMARK 465 HIS B 33
REMARK 465 HIS B 34
REMARK 465 HIS B 35
REMARK 465 HIS B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 GLY B 39
REMARK 465 ILE B 40
REMARK 465 PRO B 41
REMARK 465 MET B 42
REMARK 465 ASN B 43
REMARK 465 ASN B 966
REMARK 465 PRO B 967
REMARK 465 VAL B 968
REMARK 465 VAL B 969
REMARK 465 GLY B 970
REMARK 465 GLU B 971
REMARK 465 PHE B 972
REMARK 465 PRO B 973
REMARK 465 ALA B 974
REMARK 465 GLN B 975
REMARK 465 ASN B 976
REMARK 465 ASP B 977
REMARK 465 ILE B 978
REMARK 465 ASN B 1013
REMARK 465 PHE B 1014
REMARK 465 MET B 1015
REMARK 465 ALA B 1016
REMARK 465 ALA B 1017
REMARK 465 LYS B 1018
REMARK 465 LEU B 1019
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 542 CG CD CE NZ
REMARK 470 GLU A 543 CG CD OE1 OE2
REMARK 470 ASP A 964 CG OD1 OD2
REMARK 470 SER A 965 OG
REMARK 470 ILE A1012 CA C O CB CG1 CG2 CD1
REMARK 470 LYS B 542 CG CD CE NZ
REMARK 470 GLU B 543 CG CD OE1 OE2
REMARK 470 ASP B 964 CG OD1 OD2
REMARK 470 SER B 965 OG
REMARK 470 ILE B1012 CA C O CB CG1 CG2 CD1
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 NE2 HIS A 108 OE1 GLU A 189 1.77
REMARK 500 NE2 HIS A 112 OE1 GLU A 189 1.91
REMARK 500 NE2 HIS B 112 OE1 GLU B 189 1.98
REMARK 500 CE1 HIS A 108 OE1 GLU A 189 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 577 CG GLU A 577 CD 0.123
REMARK 500 GLU B 189 CB GLU B 189 CG 0.121
REMARK 500 GLU B 189 CG GLU B 189 CD 0.149
REMARK 500 GLU B 577 CG GLU B 577 CD 0.091
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 62 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 VAL A 75 CB - CA - C ANGL. DEV. = -11.6 DEGREES
REMARK 500 ARG A 711 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASN B 52 N - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 VAL B 153 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 GLU B 189 OE1 - CD - OE2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 PRO B 406 C - N - CD ANGL. DEV. = -14.8 DEGREES
REMARK 500 THR B 489 CB - CA - C ANGL. DEV. = -20.9 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 HIS A 53 123.01 -34.96
REMARK 500 HIS A 93 44.27 -76.48
REMARK 500 HIS A 157 30.36 -145.92
REMARK 500 SER A 171 66.59 -165.04
REMARK 500 PHE A 174 67.15 31.83
REMARK 500 ASN A 210 105.65 -55.54
REMARK 500 GLU A 227 -59.80 -136.16
REMARK 500 PRO A 320 -178.27 -62.65
REMARK 500 GLU A 453 1.36 -65.23
REMARK 500 ASN A 515 49.36 -95.65
REMARK 500 LYS A 566 -49.26 -133.75
REMARK 500 ASP A 636 -39.33 -32.62
REMARK 500 THR A 651 28.78 -142.07
REMARK 500 PRO A 757 170.33 -56.98
REMARK 500 LEU A 763 78.55 -68.07
REMARK 500 THR A 797 -80.55 -115.06
REMARK 500 THR A 869 -39.27 -39.09
REMARK 500 VAL A 946 -34.14 -39.46
REMARK 500 MET A 963 -175.67 -67.58
REMARK 500 ASP A 964 -3.93 -148.01
REMARK 500 SER A 981 -175.86 -67.66
REMARK 500 PRO A1010 -167.62 -62.77
REMARK 500 HIS B 93 38.30 -79.89
REMARK 500 LEU B 97 -5.55 -57.07
REMARK 500 THR B 118 -167.87 -127.42
REMARK 500 GLN B 167 -37.49 -38.73
REMARK 500 LEU B 170 -64.39 -106.34
REMARK 500 SER B 171 72.95 -155.68
REMARK 500 ASP B 175 136.71 -38.16
REMARK 500 LYS B 223 -39.20 -34.64
REMARK 500 GLU B 227 -56.77 -132.65
REMARK 500 GLU B 277 38.24 -98.39
REMARK 500 ILE B 307 -71.04 -84.14
REMARK 500 LYS B 308 155.97 -44.77
REMARK 500 PHE B 424 41.64 -109.21
REMARK 500 ARG B 431 -72.00 -47.42
REMARK 500 GLU B 457 -52.97 -130.13
REMARK 500 SER B 482 129.99 -176.35
REMARK 500 ALA B 516 121.43 -33.52
REMARK 500 ALA B 544 129.27 -38.52
REMARK 500 THR B 651 18.58 -144.77
REMARK 500 ASN B 672 -8.18 -59.34
REMARK 500 ASN B 787 36.43 -94.31
REMARK 500 THR B 797 -73.99 -102.02
REMARK 500 ASP B 798 -169.45 -161.36
REMARK 500 ARG B 824 -73.55 -97.52
REMARK 500 ASN B 841 14.32 50.55
REMARK 500 ASP B 964 101.96 -161.62
REMARK 500 SER B 981 -175.78 -69.14
REMARK 500 PRO B1006 172.04 -59.66
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN B 52 HIS B 53 149.61
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 A1101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 108 NE2
REMARK 620 2 HIS A 112 NE2 61.8
REMARK 620 3 GLU A 189 OE1 56.7 51.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 108 NE2
REMARK 620 2 HIS B 112 NE2 78.5
REMARK 620 3 GLU B 189 OE2 74.2 128.7
REMARK 620 4 GLU B 189 OE1 74.1 62.7 68.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGW A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGW B 1102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GS8 RELATED DB: PDB
REMARK 900 RELATED ID: 4GSE RELATED DB: PDB
REMARK 900 RELATED ID: 4GSF RELATED DB: PDB
DBREF 4GSC A 42 1019 UNP P14735 IDE_HUMAN 42 1019
DBREF 4GSC B 42 1019 UNP P14735 IDE_HUMAN 42 1019
SEQADV 4GSC MET A 30 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS A 31 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS A 32 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS A 33 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS A 34 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS A 35 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS A 36 UNP P14735 EXPRESSION TAG
SEQADV 4GSC ALA A 37 UNP P14735 EXPRESSION TAG
SEQADV 4GSC ALA A 38 UNP P14735 EXPRESSION TAG
SEQADV 4GSC GLY A 39 UNP P14735 EXPRESSION TAG
SEQADV 4GSC ILE A 40 UNP P14735 EXPRESSION TAG
SEQADV 4GSC PRO A 41 UNP P14735 EXPRESSION TAG
SEQADV 4GSC LEU A 110 UNP P14735 CYS 110 ENGINEERED MUTATION
SEQADV 4GSC GLN A 111 UNP P14735 GLU 111 ENGINEERED MUTATION
SEQADV 4GSC SER A 171 UNP P14735 CYS 171 ENGINEERED MUTATION
SEQADV 4GSC ALA A 178 UNP P14735 CYS 178 ENGINEERED MUTATION
SEQADV 4GSC VAL A 257 UNP P14735 CYS 257 ENGINEERED MUTATION
SEQADV 4GSC LEU A 414 UNP P14735 CYS 414 ENGINEERED MUTATION
SEQADV 4GSC ASN A 573 UNP P14735 CYS 573 ENGINEERED MUTATION
SEQADV 4GSC SER A 590 UNP P14735 CYS 590 ENGINEERED MUTATION
SEQADV 4GSC SER A 789 UNP P14735 CYS 789 ENGINEERED MUTATION
SEQADV 4GSC ALA A 812 UNP P14735 CYS 812 ENGINEERED MUTATION
SEQADV 4GSC ALA A 819 UNP P14735 CYS 819 ENGINEERED MUTATION
SEQADV 4GSC SER A 904 UNP P14735 CYS 904 ENGINEERED MUTATION
SEQADV 4GSC ASN A 966 UNP P14735 CYS 966 ENGINEERED MUTATION
SEQADV 4GSC ALA A 974 UNP P14735 CYS 974 ENGINEERED MUTATION
SEQADV 4GSC MET B 30 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS B 31 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS B 32 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS B 33 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS B 34 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS B 35 UNP P14735 EXPRESSION TAG
SEQADV 4GSC HIS B 36 UNP P14735 EXPRESSION TAG
SEQADV 4GSC ALA B 37 UNP P14735 EXPRESSION TAG
SEQADV 4GSC ALA B 38 UNP P14735 EXPRESSION TAG
SEQADV 4GSC GLY B 39 UNP P14735 EXPRESSION TAG
SEQADV 4GSC ILE B 40 UNP P14735 EXPRESSION TAG
SEQADV 4GSC PRO B 41 UNP P14735 EXPRESSION TAG
SEQADV 4GSC LEU B 110 UNP P14735 CYS 110 ENGINEERED MUTATION
SEQADV 4GSC GLN B 111 UNP P14735 GLU 111 ENGINEERED MUTATION
SEQADV 4GSC SER B 171 UNP P14735 CYS 171 ENGINEERED MUTATION
SEQADV 4GSC ALA B 178 UNP P14735 CYS 178 ENGINEERED MUTATION
SEQADV 4GSC VAL B 257 UNP P14735 CYS 257 ENGINEERED MUTATION
SEQADV 4GSC LEU B 414 UNP P14735 CYS 414 ENGINEERED MUTATION
SEQADV 4GSC ASN B 573 UNP P14735 CYS 573 ENGINEERED MUTATION
SEQADV 4GSC SER B 590 UNP P14735 CYS 590 ENGINEERED MUTATION
SEQADV 4GSC SER B 789 UNP P14735 CYS 789 ENGINEERED MUTATION
SEQADV 4GSC ALA B 812 UNP P14735 CYS 812 ENGINEERED MUTATION
SEQADV 4GSC ALA B 819 UNP P14735 CYS 819 ENGINEERED MUTATION
SEQADV 4GSC SER B 904 UNP P14735 CYS 904 ENGINEERED MUTATION
SEQADV 4GSC ASN B 966 UNP P14735 CYS 966 ENGINEERED MUTATION
SEQADV 4GSC ALA B 974 UNP P14735 CYS 974 ENGINEERED MUTATION
SEQRES 1 A 990 MET HIS HIS HIS HIS HIS HIS ALA ALA GLY ILE PRO MET
SEQRES 2 A 990 ASN ASN PRO ALA ILE LYS ARG ILE GLY ASN HIS ILE THR
SEQRES 3 A 990 LYS SER PRO GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU
SEQRES 4 A 990 LEU ALA ASN GLY ILE LYS VAL LEU LEU ILE SER ASP PRO
SEQRES 5 A 990 THR THR ASP LYS SER SER ALA ALA LEU ASP VAL HIS ILE
SEQRES 6 A 990 GLY SER LEU SER ASP PRO PRO ASN ILE ALA GLY LEU SER
SEQRES 7 A 990 HIS PHE LEU GLN HIS MET LEU PHE LEU GLY THR LYS LYS
SEQRES 8 A 990 TYR PRO LYS GLU ASN GLU TYR SER GLN PHE LEU SER GLU
SEQRES 9 A 990 HIS ALA GLY SER SER ASN ALA PHE THR SER GLY GLU HIS
SEQRES 10 A 990 THR ASN TYR TYR PHE ASP VAL SER HIS GLU HIS LEU GLU
SEQRES 11 A 990 GLY ALA LEU ASP ARG PHE ALA GLN PHE PHE LEU SER PRO
SEQRES 12 A 990 LEU PHE ASP GLU SER ALA LYS ASP ARG GLU VAL ASN ALA
SEQRES 13 A 990 VAL ASP SER GLU HIS GLU LYS ASN VAL MET ASN ASP ALA
SEQRES 14 A 990 TRP ARG LEU PHE GLN LEU GLU LYS ALA THR GLY ASN PRO
SEQRES 15 A 990 LYS HIS PRO PHE SER LYS PHE GLY THR GLY ASN LYS TYR
SEQRES 16 A 990 THR LEU GLU THR ARG PRO ASN GLN GLU GLY ILE ASP VAL
SEQRES 17 A 990 ARG GLN GLU LEU LEU LYS PHE HIS SER ALA TYR TYR SER
SEQRES 18 A 990 SER ASN LEU MET ALA VAL VAL VAL LEU GLY ARG GLU SER
SEQRES 19 A 990 LEU ASP ASP LEU THR ASN LEU VAL VAL LYS LEU PHE SER
SEQRES 20 A 990 GLU VAL GLU ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO
SEQRES 21 A 990 GLU HIS PRO PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR
SEQRES 22 A 990 LYS ILE VAL PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL
SEQRES 23 A 990 THR PHE PRO ILE PRO ASP LEU GLN LYS TYR TYR LYS SER
SEQRES 24 A 990 ASN PRO GLY HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU
SEQRES 25 A 990 GLY PRO GLY SER LEU LEU SER GLU LEU LYS SER LYS GLY
SEQRES 26 A 990 TRP VAL ASN THR LEU VAL GLY GLY GLN LYS GLU GLY ALA
SEQRES 27 A 990 ARG GLY PHE MET PHE PHE ILE ILE ASN VAL ASP LEU THR
SEQRES 28 A 990 GLU GLU GLY LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS
SEQRES 29 A 990 MET PHE GLN TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO
SEQRES 30 A 990 GLN GLU TRP VAL PHE GLN GLU LEU LYS ASP LEU ASN ALA
SEQRES 31 A 990 VAL ALA PHE ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY
SEQRES 32 A 990 TYR THR SER LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO
SEQRES 33 A 990 LEU GLU GLU VAL LEU THR ALA GLU TYR LEU LEU GLU GLU
SEQRES 34 A 990 PHE ARG PRO ASP LEU ILE GLU MET VAL LEU ASP LYS LEU
SEQRES 35 A 990 ARG PRO GLU ASN VAL ARG VAL ALA ILE VAL SER LYS SER
SEQRES 36 A 990 PHE GLU GLY LYS THR ASP ARG THR GLU GLU TRP TYR GLY
SEQRES 37 A 990 THR GLN TYR LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE
SEQRES 38 A 990 LYS LYS TRP GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS
SEQRES 39 A 990 LEU PRO THR LYS ASN GLU PHE ILE PRO THR ASN PHE GLU
SEQRES 40 A 990 ILE LEU PRO LEU GLU LYS GLU ALA THR PRO TYR PRO ALA
SEQRES 41 A 990 LEU ILE LYS ASP THR ALA MET SER LYS LEU TRP PHE LYS
SEQRES 42 A 990 GLN ASP ASP LYS PHE PHE LEU PRO LYS ALA ASN LEU ASN
SEQRES 43 A 990 PHE GLU PHE PHE SER PRO PHE ALA TYR VAL ASP PRO LEU
SEQRES 44 A 990 HIS SER ASN MET ALA TYR LEU TYR LEU GLU LEU LEU LYS
SEQRES 45 A 990 ASP SER LEU ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA
SEQRES 46 A 990 GLY LEU SER TYR ASP LEU GLN ASN THR ILE TYR GLY MET
SEQRES 47 A 990 TYR LEU SER VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE
SEQRES 48 A 990 LEU LEU LYS LYS ILE ILE GLU LYS MET ALA THR PHE GLU
SEQRES 49 A 990 ILE ASP GLU LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR
SEQRES 50 A 990 MET ARG SER LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS
SEQRES 51 A 990 GLN HIS ALA MET TYR TYR LEU ARG LEU LEU MET THR GLU
SEQRES 52 A 990 VAL ALA TRP THR LYS ASP GLU LEU LYS GLU ALA LEU ASP
SEQRES 53 A 990 ASP VAL THR LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN
SEQRES 54 A 990 LEU LEU SER ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY
SEQRES 55 A 990 ASN ILE THR LYS GLN ALA ALA LEU GLY ILE MET GLN MET
SEQRES 56 A 990 VAL GLU ASP THR LEU ILE GLU HIS ALA HIS THR LYS PRO
SEQRES 57 A 990 LEU LEU PRO SER GLN LEU VAL ARG TYR ARG GLU VAL GLN
SEQRES 58 A 990 LEU PRO ASP ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN
SEQRES 59 A 990 GLU VAL HIS ASN ASN SER GLY ILE GLU ILE TYR TYR GLN
SEQRES 60 A 990 THR ASP MET GLN SER THR SER GLU ASN MET PHE LEU GLU
SEQRES 61 A 990 LEU PHE ALA GLN ILE ILE SER GLU PRO ALA PHE ASN THR
SEQRES 62 A 990 LEU ARG THR LYS GLU GLN LEU GLY TYR ILE VAL PHE SER
SEQRES 63 A 990 GLY PRO ARG ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE
SEQRES 64 A 990 ILE ILE GLN SER GLU LYS PRO PRO HIS TYR LEU GLU SER
SEQRES 65 A 990 ARG VAL GLU ALA PHE LEU ILE THR MET GLU LYS SER ILE
SEQRES 66 A 990 GLU ASP MET THR GLU GLU ALA PHE GLN LYS HIS ILE GLN
SEQRES 67 A 990 ALA LEU ALA ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU
SEQRES 68 A 990 SER ALA GLU SER ALA LYS TYR TRP GLY GLU ILE ILE SER
SEQRES 69 A 990 GLN GLN TYR ASN PHE ASP ARG ASP ASN THR GLU VAL ALA
SEQRES 70 A 990 TYR LEU LYS THR LEU THR LYS GLU ASP ILE ILE LYS PHE
SEQRES 71 A 990 TYR LYS GLU MET LEU ALA VAL ASP ALA PRO ARG ARG HIS
SEQRES 72 A 990 LYS VAL SER VAL HIS VAL LEU ALA ARG GLU MET ASP SER
SEQRES 73 A 990 ASN PRO VAL VAL GLY GLU PHE PRO ALA GLN ASN ASP ILE
SEQRES 74 A 990 ASN LEU SER GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL
SEQRES 75 A 990 ILE GLN ASN MET THR GLU PHE LYS ARG GLY LEU PRO LEU
SEQRES 76 A 990 PHE PRO LEU VAL LYS PRO HIS ILE ASN PHE MET ALA ALA
SEQRES 77 A 990 LYS LEU
SEQRES 1 B 990 MET HIS HIS HIS HIS HIS HIS ALA ALA GLY ILE PRO MET
SEQRES 2 B 990 ASN ASN PRO ALA ILE LYS ARG ILE GLY ASN HIS ILE THR
SEQRES 3 B 990 LYS SER PRO GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU
SEQRES 4 B 990 LEU ALA ASN GLY ILE LYS VAL LEU LEU ILE SER ASP PRO
SEQRES 5 B 990 THR THR ASP LYS SER SER ALA ALA LEU ASP VAL HIS ILE
SEQRES 6 B 990 GLY SER LEU SER ASP PRO PRO ASN ILE ALA GLY LEU SER
SEQRES 7 B 990 HIS PHE LEU GLN HIS MET LEU PHE LEU GLY THR LYS LYS
SEQRES 8 B 990 TYR PRO LYS GLU ASN GLU TYR SER GLN PHE LEU SER GLU
SEQRES 9 B 990 HIS ALA GLY SER SER ASN ALA PHE THR SER GLY GLU HIS
SEQRES 10 B 990 THR ASN TYR TYR PHE ASP VAL SER HIS GLU HIS LEU GLU
SEQRES 11 B 990 GLY ALA LEU ASP ARG PHE ALA GLN PHE PHE LEU SER PRO
SEQRES 12 B 990 LEU PHE ASP GLU SER ALA LYS ASP ARG GLU VAL ASN ALA
SEQRES 13 B 990 VAL ASP SER GLU HIS GLU LYS ASN VAL MET ASN ASP ALA
SEQRES 14 B 990 TRP ARG LEU PHE GLN LEU GLU LYS ALA THR GLY ASN PRO
SEQRES 15 B 990 LYS HIS PRO PHE SER LYS PHE GLY THR GLY ASN LYS TYR
SEQRES 16 B 990 THR LEU GLU THR ARG PRO ASN GLN GLU GLY ILE ASP VAL
SEQRES 17 B 990 ARG GLN GLU LEU LEU LYS PHE HIS SER ALA TYR TYR SER
SEQRES 18 B 990 SER ASN LEU MET ALA VAL VAL VAL LEU GLY ARG GLU SER
SEQRES 19 B 990 LEU ASP ASP LEU THR ASN LEU VAL VAL LYS LEU PHE SER
SEQRES 20 B 990 GLU VAL GLU ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO
SEQRES 21 B 990 GLU HIS PRO PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR
SEQRES 22 B 990 LYS ILE VAL PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL
SEQRES 23 B 990 THR PHE PRO ILE PRO ASP LEU GLN LYS TYR TYR LYS SER
SEQRES 24 B 990 ASN PRO GLY HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU
SEQRES 25 B 990 GLY PRO GLY SER LEU LEU SER GLU LEU LYS SER LYS GLY
SEQRES 26 B 990 TRP VAL ASN THR LEU VAL GLY GLY GLN LYS GLU GLY ALA
SEQRES 27 B 990 ARG GLY PHE MET PHE PHE ILE ILE ASN VAL ASP LEU THR
SEQRES 28 B 990 GLU GLU GLY LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS
SEQRES 29 B 990 MET PHE GLN TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO
SEQRES 30 B 990 GLN GLU TRP VAL PHE GLN GLU LEU LYS ASP LEU ASN ALA
SEQRES 31 B 990 VAL ALA PHE ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY
SEQRES 32 B 990 TYR THR SER LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO
SEQRES 33 B 990 LEU GLU GLU VAL LEU THR ALA GLU TYR LEU LEU GLU GLU
SEQRES 34 B 990 PHE ARG PRO ASP LEU ILE GLU MET VAL LEU ASP LYS LEU
SEQRES 35 B 990 ARG PRO GLU ASN VAL ARG VAL ALA ILE VAL SER LYS SER
SEQRES 36 B 990 PHE GLU GLY LYS THR ASP ARG THR GLU GLU TRP TYR GLY
SEQRES 37 B 990 THR GLN TYR LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE
SEQRES 38 B 990 LYS LYS TRP GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS
SEQRES 39 B 990 LEU PRO THR LYS ASN GLU PHE ILE PRO THR ASN PHE GLU
SEQRES 40 B 990 ILE LEU PRO LEU GLU LYS GLU ALA THR PRO TYR PRO ALA
SEQRES 41 B 990 LEU ILE LYS ASP THR ALA MET SER LYS LEU TRP PHE LYS
SEQRES 42 B 990 GLN ASP ASP LYS PHE PHE LEU PRO LYS ALA ASN LEU ASN
SEQRES 43 B 990 PHE GLU PHE PHE SER PRO PHE ALA TYR VAL ASP PRO LEU
SEQRES 44 B 990 HIS SER ASN MET ALA TYR LEU TYR LEU GLU LEU LEU LYS
SEQRES 45 B 990 ASP SER LEU ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA
SEQRES 46 B 990 GLY LEU SER TYR ASP LEU GLN ASN THR ILE TYR GLY MET
SEQRES 47 B 990 TYR LEU SER VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE
SEQRES 48 B 990 LEU LEU LYS LYS ILE ILE GLU LYS MET ALA THR PHE GLU
SEQRES 49 B 990 ILE ASP GLU LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR
SEQRES 50 B 990 MET ARG SER LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS
SEQRES 51 B 990 GLN HIS ALA MET TYR TYR LEU ARG LEU LEU MET THR GLU
SEQRES 52 B 990 VAL ALA TRP THR LYS ASP GLU LEU LYS GLU ALA LEU ASP
SEQRES 53 B 990 ASP VAL THR LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN
SEQRES 54 B 990 LEU LEU SER ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY
SEQRES 55 B 990 ASN ILE THR LYS GLN ALA ALA LEU GLY ILE MET GLN MET
SEQRES 56 B 990 VAL GLU ASP THR LEU ILE GLU HIS ALA HIS THR LYS PRO
SEQRES 57 B 990 LEU LEU PRO SER GLN LEU VAL ARG TYR ARG GLU VAL GLN
SEQRES 58 B 990 LEU PRO ASP ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN
SEQRES 59 B 990 GLU VAL HIS ASN ASN SER GLY ILE GLU ILE TYR TYR GLN
SEQRES 60 B 990 THR ASP MET GLN SER THR SER GLU ASN MET PHE LEU GLU
SEQRES 61 B 990 LEU PHE ALA GLN ILE ILE SER GLU PRO ALA PHE ASN THR
SEQRES 62 B 990 LEU ARG THR LYS GLU GLN LEU GLY TYR ILE VAL PHE SER
SEQRES 63 B 990 GLY PRO ARG ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE
SEQRES 64 B 990 ILE ILE GLN SER GLU LYS PRO PRO HIS TYR LEU GLU SER
SEQRES 65 B 990 ARG VAL GLU ALA PHE LEU ILE THR MET GLU LYS SER ILE
SEQRES 66 B 990 GLU ASP MET THR GLU GLU ALA PHE GLN LYS HIS ILE GLN
SEQRES 67 B 990 ALA LEU ALA ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU
SEQRES 68 B 990 SER ALA GLU SER ALA LYS TYR TRP GLY GLU ILE ILE SER
SEQRES 69 B 990 GLN GLN TYR ASN PHE ASP ARG ASP ASN THR GLU VAL ALA
SEQRES 70 B 990 TYR LEU LYS THR LEU THR LYS GLU ASP ILE ILE LYS PHE
SEQRES 71 B 990 TYR LYS GLU MET LEU ALA VAL ASP ALA PRO ARG ARG HIS
SEQRES 72 B 990 LYS VAL SER VAL HIS VAL LEU ALA ARG GLU MET ASP SER
SEQRES 73 B 990 ASN PRO VAL VAL GLY GLU PHE PRO ALA GLN ASN ASP ILE
SEQRES 74 B 990 ASN LEU SER GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL
SEQRES 75 B 990 ILE GLN ASN MET THR GLU PHE LYS ARG GLY LEU PRO LEU
SEQRES 76 B 990 PHE PRO LEU VAL LYS PRO HIS ILE ASN PHE MET ALA ALA
SEQRES 77 B 990 LYS LEU
HET ZN A1101 1
HET MGW A1102 28
HET ZN B1101 1
HET MGW B1102 28
HETNAM ZN ZINC ION
HETNAM MGW METHYL N-(CARBOXYMETHYL)-N-(2-PHENYLETHYL)GLYCYL-L-
HETNAM 2 MGW HISTIDINATE
HETSYN MGW ( (S)-2-[2-(CARBOXYMETHYL-PHENETHYL-AMINO)-
HETSYN 2 MGW ACETYLAMINO]-3-(1H-IMIDAZOL-4-YL)-PROPIONIC ACID
HETSYN 3 MGW METHYL ESTER
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 MGW 2(C19 H24 N4 O5)
FORMUL 7 HOH *180(H2 O)
HELIX 1 1 GLY A 95 ASP A 99 5 5
HELIX 2 2 GLY A 105 PHE A 115 1 11
HELIX 3 3 ASN A 125 GLU A 133 1 9
HELIX 4 4 HIS A 157 GLN A 167 1 11
HELIX 5 5 PHE A 168 LEU A 170 5 3
HELIX 6 6 ASP A 175 MET A 195 1 21
HELIX 7 7 ASN A 196 ALA A 207 1 12
HELIX 8 8 HIS A 213 LYS A 217 5 5
HELIX 9 9 ASN A 222 GLU A 227 1 6
HELIX 10 10 GLU A 227 GLU A 233 1 7
HELIX 11 11 ASP A 236 TYR A 249 1 14
HELIX 12 12 SER A 250 ASN A 252 5 3
HELIX 13 13 SER A 263 SER A 276 1 14
HELIX 14 14 GLN A 294 LEU A 298 5 5
HELIX 15 15 LEU A 322 TYR A 326 5 5
HELIX 16 16 ASN A 329 GLY A 339 1 11
HELIX 17 17 SER A 345 LYS A 353 1 9
HELIX 18 18 GLU A 382 LEU A 385 5 4
HELIX 19 19 HIS A 386 GLY A 405 1 20
HELIX 20 20 GLN A 407 PHE A 424 1 18
HELIX 21 21 ARG A 429 LEU A 441 1 13
HELIX 22 22 PRO A 445 VAL A 449 5 5
HELIX 23 23 ARG A 460 ASP A 469 1 10
HELIX 24 24 LYS A 470 LEU A 471 5 2
HELIX 25 25 ARG A 472 ASN A 475 5 4
HELIX 26 26 LYS A 483 GLU A 486 5 4
HELIX 27 27 PRO A 506 ASN A 515 1 10
HELIX 28 28 ASP A 586 ALA A 614 1 29
HELIX 29 29 LYS A 637 ALA A 650 1 14
HELIX 30 30 ASP A 655 PHE A 673 1 19
HELIX 31 31 ARG A 674 GLU A 676 5 3
HELIX 32 32 GLN A 677 THR A 691 1 15
HELIX 33 33 THR A 696 ASP A 705 1 10
HELIX 34 34 THR A 708 LEU A 720 1 13
HELIX 35 35 THR A 734 HIS A 754 1 21
HELIX 36 36 LEU A 759 LEU A 763 5 5
HELIX 37 37 SER A 801 ARG A 824 1 24
HELIX 38 38 PRO A 855 MET A 877 1 23
HELIX 39 39 THR A 878 ASP A 895 1 18
HELIX 40 40 LYS A 899 SER A 913 1 15
HELIX 41 41 ASP A 919 LYS A 929 1 11
HELIX 42 42 THR A 932 LEU A 944 1 13
HELIX 43 43 ASN A 994 GLY A 1001 1 8
HELIX 44 44 GLY B 95 ASP B 99 5 5
HELIX 45 45 GLY B 105 PHE B 115 1 11
HELIX 46 46 ASN B 125 HIS B 134 1 10
HELIX 47 47 HIS B 157 GLN B 167 1 11
HELIX 48 48 PHE B 168 LEU B 170 5 3
HELIX 49 49 ASP B 175 MET B 195 1 21
HELIX 50 50 ASN B 196 ALA B 207 1 12
HELIX 51 51 HIS B 213 LYS B 217 5 5
HELIX 52 52 ASN B 222 GLU B 227 1 6
HELIX 53 53 GLU B 227 GLU B 233 1 7
HELIX 54 54 ASP B 236 TYR B 249 1 14
HELIX 55 55 SER B 250 ASN B 252 5 3
HELIX 56 56 SER B 263 SER B 276 1 14
HELIX 57 57 GLN B 294 LEU B 298 5 5
HELIX 58 58 LEU B 322 TYR B 326 5 5
HELIX 59 59 ASN B 329 GLY B 339 1 11
HELIX 60 60 SER B 345 LYS B 353 1 9
HELIX 61 61 THR B 380 LEU B 385 1 6
HELIX 62 62 HIS B 386 ALA B 403 1 18
HELIX 63 63 GLN B 407 PHE B 424 1 18
HELIX 64 64 ARG B 429 LEU B 441 1 13
HELIX 65 65 PRO B 445 VAL B 449 5 5
HELIX 66 66 ARG B 460 ASP B 469 1 10
HELIX 67 67 LYS B 470 LEU B 471 5 2
HELIX 68 68 ARG B 472 ASN B 475 5 4
HELIX 69 69 LYS B 483 GLU B 486 5 4
HELIX 70 70 PRO B 506 ASN B 515 1 10
HELIX 71 71 PRO B 581 TYR B 584 5 4
HELIX 72 72 ASP B 586 ALA B 614 1 29
HELIX 73 73 LYS B 637 ALA B 650 1 14
HELIX 74 74 ASP B 655 ASN B 672 1 18
HELIX 75 75 PHE B 673 GLU B 676 5 4
HELIX 76 76 GLN B 677 THR B 691 1 15
HELIX 77 77 THR B 696 ALA B 703 1 8
HELIX 78 78 LEU B 704 VAL B 707 5 4
HELIX 79 79 THR B 708 SER B 721 1 14
HELIX 80 80 THR B 734 HIS B 754 1 21
HELIX 81 81 LEU B 759 LEU B 763 5 5
HELIX 82 82 SER B 801 ARG B 824 1 24
HELIX 83 83 PRO B 855 ASP B 876 1 22
HELIX 84 84 THR B 878 LEU B 894 1 17
HELIX 85 85 LYS B 899 SER B 913 1 15
HELIX 86 86 ASP B 919 LEU B 931 1 13
HELIX 87 87 THR B 932 LEU B 944 1 13
HELIX 88 88 ASN B 994 GLY B 1001 1 8
SHEET 1 A 7 ILE A 47 ILE A 50 0
SHEET 2 A 7 GLU A 63 LEU A 69 -1 O GLU A 68 N LYS A 48
SHEET 3 A 7 LYS A 74 SER A 79 -1 O LEU A 77 N ARG A 65
SHEET 4 A 7 MET A 254 GLY A 260 1 O VAL A 258 N ILE A 78
SHEET 5 A 7 LYS A 85 VAL A 92 -1 N ALA A 89 O VAL A 257
SHEET 6 A 7 HIS A 146 SER A 154 -1 O TYR A 149 N LEU A 90
SHEET 7 A 7 SER A 137 SER A 143 -1 N ASN A 139 O TYR A 150
SHEET 1 B 7 LEU A 359 ALA A 367 0
SHEET 2 B 7 PHE A 370 ASP A 378 -1 O ILE A 374 N GLY A 362
SHEET 3 B 7 ASN A 312 ILE A 319 -1 N VAL A 315 O ILE A 375
SHEET 4 B 7 ARG A 477 VAL A 481 -1 O ALA A 479 N TYR A 314
SHEET 5 B 7 GLN A 300 ILE A 304 1 N ILE A 304 O ILE A 480
SHEET 6 B 7 GLN A 499 ALA A 504 -1 O GLU A 503 N LEU A 301
SHEET 7 B 7 ARG A 491 THR A 492 -1 N ARG A 491 O TYR A 500
SHEET 1 C 6 ALA A 549 ASP A 553 0
SHEET 2 C 6 SER A 557 GLN A 563 -1 O PHE A 561 N ALA A 549
SHEET 3 C 6 HIS A 724 GLY A 731 1 O ALA A 727 N TRP A 560
SHEET 4 C 6 LYS A 571 PHE A 579 -1 N PHE A 579 O HIS A 724
SHEET 5 C 6 GLY A 626 TYR A 634 -1 O LEU A 629 N PHE A 576
SHEET 6 C 6 LEU A 616 THR A 623 -1 N THR A 623 O GLY A 626
SHEET 1 D 6 VAL A 833 ALA A 840 0
SHEET 2 D 6 ILE A 843 SER A 852 -1 O GLY A 845 N ARG A 838
SHEET 3 D 6 SER A 789 MET A 799 -1 N THR A 797 O GLN A 844
SHEET 4 D 6 HIS A 952 LEU A 959 -1 O VAL A 954 N TYR A 794
SHEET 5 D 6 GLY A 775 ARG A 782 1 N GLN A 781 O LEU A 959
SHEET 6 D 6 GLU A 990 VAL A 991 1 O GLU A 990 N TRP A 776
SHEET 1 E 7 ILE B 47 ILE B 50 0
SHEET 2 E 7 GLU B 63 LEU B 69 -1 O GLU B 68 N ARG B 49
SHEET 3 E 7 LYS B 74 SER B 79 -1 O SER B 79 N GLU B 63
SHEET 4 E 7 MET B 254 GLY B 260 1 O VAL B 258 N ILE B 78
SHEET 5 E 7 LYS B 85 VAL B 92 -1 N ALA B 89 O VAL B 257
SHEET 6 E 7 HIS B 146 SER B 154 -1 O THR B 147 N VAL B 92
SHEET 7 E 7 SER B 137 SER B 143 -1 N SER B 143 O HIS B 146
SHEET 1 F 7 LEU B 359 ALA B 367 0
SHEET 2 F 7 PHE B 370 ASP B 378 -1 O PHE B 372 N LYS B 364
SHEET 3 F 7 ASN B 312 PRO B 320 -1 N PHE B 317 O PHE B 373
SHEET 4 F 7 ARG B 477 VAL B 481 -1 O ALA B 479 N TYR B 314
SHEET 5 F 7 GLN B 300 ILE B 304 1 N TYR B 302 O ILE B 480
SHEET 6 F 7 GLN B 499 ALA B 504 -1 O LYS B 501 N LYS B 303
SHEET 7 F 7 ARG B 491 THR B 492 -1 N ARG B 491 O TYR B 500
SHEET 1 G 6 ALA B 549 ASP B 553 0
SHEET 2 G 6 SER B 557 GLN B 563 -1 O PHE B 561 N ALA B 549
SHEET 3 G 6 ARG B 722 GLY B 731 1 O ALA B 727 N TRP B 560
SHEET 4 G 6 LYS B 571 PHE B 579 -1 N ASN B 575 O LEU B 728
SHEET 5 G 6 GLY B 626 TYR B 634 -1 O VAL B 631 N LEU B 574
SHEET 6 G 6 LEU B 616 ASN B 622 -1 N GLN B 621 O TYR B 628
SHEET 1 H 4 ALA B 549 ASP B 553 0
SHEET 2 H 4 SER B 557 GLN B 563 -1 O PHE B 561 N ALA B 549
SHEET 3 H 4 ARG B 722 GLY B 731 1 O ALA B 727 N TRP B 560
SHEET 4 H 4 LYS B 756 PRO B 757 1 O LYS B 756 N LEU B 723
SHEET 1 I 6 ILE B 832 ALA B 840 0
SHEET 2 I 6 ILE B 843 SER B 852 -1 O ILE B 843 N ALA B 840
SHEET 3 I 6 SER B 789 MET B 799 -1 N TYR B 795 O LEU B 846
SHEET 4 I 6 HIS B 952 LEU B 959 -1 O VAL B 954 N TYR B 794
SHEET 5 I 6 TRP B 776 ARG B 782 1 N TYR B 779 O HIS B 957
SHEET 6 I 6 GLU B 990 VAL B 991 1 O GLU B 990 N TRP B 776
LINK NE2 HIS A 108 ZN ZN A1101 1555 1555 2.01
LINK NE2 HIS A 112 ZN ZN A1101 1555 1555 2.44
LINK OE1 GLU A 189 ZN ZN A1101 1555 1555 1.66
LINK NE2 HIS B 108 ZN ZN B1101 1555 1555 1.99
LINK NE2 HIS B 112 ZN ZN B1101 1555 1555 1.91
LINK OE2 GLU B 189 ZN ZN B1101 1555 1555 1.80
LINK OE1 GLU B 189 ZN ZN B1101 1555 1555 1.90
SITE 1 AC1 4 HIS A 108 GLN A 111 HIS A 112 GLU A 189
SITE 1 AC2 8 HIS A 332 GLY A 339 GLU A 341 LEU A 359
SITE 2 AC2 8 VAL A 360 GLY A 361 TYR A 609 HOH A1251
SITE 1 AC3 4 HIS B 108 HIS B 112 GLU B 189 TYR B 831
SITE 1 AC4 6 GLY B 335 HIS B 336 GLY B 339 GLU B 341
SITE 2 AC4 6 LEU B 359 GLY B 361
CRYST1 263.759 263.759 91.260 90.00 90.00 120.00 P 65 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 0.003791 0.002189 0.000000 0.00000
SCALE2 0.000000 0.004378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010958 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
