HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 12-FEB-03 1NYE
TITLE CRYSTAL STRUCTURE OF OSMC FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OSMOTICALLY INDUCIBLE PROTEIN C;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: OSMC OR B1482;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3)/PSJS1244;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSKB3
KEYWDS OSMC, STRUCTURAL GENOMICS, PEROXIREDOXIN, BSGC STRUCTURE FUNDED BY
KEYWDS 2 NIH, PROTEIN STRUCTURE INITIATIVE, PSI, BERKELEY STRUCTURAL GENOMICS
KEYWDS 3 CENTER, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.SHIN,I.-G.CHOI,D.BUSSO,J.JANCARIK,H.YOKOTA,R.KIM,S.-H.KIM,
AUTHOR 2 BERKELEY STRUCTURAL GENOMICS CENTER (BSGC)
REVDAT 6 14-FEB-24 1NYE 1 SEQADV
REVDAT 5 24-FEB-09 1NYE 1 VERSN
REVDAT 4 25-JAN-05 1NYE 1 AUTHOR KEYWDS REMARK
REVDAT 3 24-AUG-04 1NYE 1 KEYWDS
REVDAT 2 27-APR-04 1NYE 1 JRNL
REVDAT 1 02-MAR-04 1NYE 0
JRNL AUTH D.H.SHIN,I.G.CHOI,D.BUSSO,J.JANCARIK,H.YOKOTA,R.KIM,S.H.KIM
JRNL TITL STRUCTURE OF OSMC FROM ESCHERICHIA COLI: A
JRNL TITL 2 SALT-SHOCK-INDUCED PROTEIN.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 903 2004
JRNL REFN ISSN 0907-4449
JRNL PMID 15103136
JRNL DOI 10.1107/S0907444904005013
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.6
REMARK 3 NUMBER OF REFLECTIONS : 31657
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) : 0.218
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3197
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3178
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 350
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6813
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.20000
REMARK 3 B22 (A**2) : 5.31000
REMARK 3 B33 (A**2) : -18.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.70000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.29
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.010
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) : 8.840 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 14.140; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 11.830; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 17.520; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.27
REMARK 3 BSOL : 33.40
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NYE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018349.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38395
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 46.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.57700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM FORMATE, 20%PEG3350, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 45.14550
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, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 TOTAL BURIED SURFACE AREA: 6410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 -57.19276
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 112.41607
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 57.19276
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -112.41607
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 ASP A 6
REMARK 465 TYR A 7
REMARK 465 ASP A 8
REMARK 465 ILE A 9
REMARK 465 PRO A 10
REMARK 465 THR A 11
REMARK 465 THR A 12
REMARK 465 GLU A 13
REMARK 465 ASN A 14
REMARK 465 LEU A 15
REMARK 465 TYR A 16
REMARK 465 PHE A 17
REMARK 465 GLN A 18
REMARK 465 GLY A 19
REMARK 465 HIS A 20
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 ASP B 206
REMARK 465 TYR B 207
REMARK 465 ASP B 208
REMARK 465 ILE B 209
REMARK 465 PRO B 210
REMARK 465 THR B 211
REMARK 465 THR B 212
REMARK 465 GLU B 213
REMARK 465 ASN B 214
REMARK 465 LEU B 215
REMARK 465 TYR B 216
REMARK 465 PHE B 217
REMARK 465 GLN B 218
REMARK 465 GLY B 219
REMARK 465 HIS B 220
REMARK 465 HIS C 402
REMARK 465 HIS C 403
REMARK 465 HIS C 404
REMARK 465 HIS C 405
REMARK 465 ASP C 406
REMARK 465 TYR C 407
REMARK 465 ASP C 408
REMARK 465 ILE C 409
REMARK 465 PRO C 410
REMARK 465 HIS E 802
REMARK 465 HIS E 803
REMARK 465 HIS E 804
REMARK 465 HIS E 805
REMARK 465 ASP E 806
REMARK 465 TYR E 807
REMARK 465 ASP E 808
REMARK 465 ILE E 809
REMARK 465 PRO E 810
REMARK 465 THR E 811
REMARK 465 THR E 812
REMARK 465 PHE F 1060
REMARK 465 GLU F 1061
REMARK 465 GLY F 1062
REMARK 465 GLU F 1063
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 NH1 ARG C 459 O HOH C 1265 2.08
REMARK 500 NH2 ARG C 459 O HOH C 1265 2.10
REMARK 500 O HOH E 1237 O HOH E 1264 2.11
REMARK 500 O MET C 421 CE LYS D 708 2.12
REMARK 500 O LEU E 920 O HOH E 1237 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP E 958 O HOH D 1223 1455 2.17
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 MET A 21 CB - CA - C ANGL. DEV. = 23.9 DEGREES
REMARK 500 MET C 421 C - N - CA ANGL. DEV. = 20.2 DEGREES
REMARK 500 THR C 422 N - CA - CB ANGL. DEV. = 11.7 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 VAL A 48 -29.07 -30.43
REMARK 500 ASN A 50 -80.04 -87.79
REMARK 500 GLN A 51 50.64 -144.74
REMARK 500 ASP A 110 -120.83 72.22
REMARK 500 PRO A 127 -93.14 -21.79
REMARK 500 ASP B 234 156.85 -36.88
REMARK 500 ASN B 250 -79.38 -65.59
REMARK 500 GLN B 251 59.27 -145.55
REMARK 500 GLU B 261 -88.72 -92.19
REMARK 500 ASP B 310 -139.59 62.70
REMARK 500 PRO B 327 -87.14 -17.52
REMARK 500 THR C 412 116.75 76.28
REMARK 500 GLU C 413 -96.98 -1.15
REMARK 500 LEU C 415 57.45 100.02
REMARK 500 HIS C 420 -141.02 30.93
REMARK 500 MET C 421 179.52 79.41
REMARK 500 THR C 422 111.41 150.06
REMARK 500 ASP C 434 169.84 -35.09
REMARK 500 GLN C 451 36.92 -156.46
REMARK 500 GLU C 461 53.59 -141.09
REMARK 500 SER C 497 141.58 -170.37
REMARK 500 ASP C 510 -134.31 61.01
REMARK 500 PRO C 527 -81.26 -33.21
REMARK 500 ALA C 531 -18.66 -48.12
REMARK 500 ILE C 537 -75.05 -79.31
REMARK 500 HIS D 603 79.28 66.81
REMARK 500 GLU D 613 -140.39 -179.97
REMARK 500 ASN D 614 165.39 163.65
REMARK 500 GLN D 618 -163.99 -63.06
REMARK 500 ILE D 635 -71.22 -58.25
REMARK 500 VAL D 648 -32.00 -36.67
REMARK 500 GLN D 651 37.47 -159.91
REMARK 500 LEU D 686 -73.38 -59.99
REMARK 500 ASP D 710 -137.07 59.68
REMARK 500 ALA D 711 48.00 -89.37
REMARK 500 PRO D 727 -89.20 -15.40
REMARK 500 LEU E 815 38.43 76.62
REMARK 500 TYR E 816 77.77 -102.23
REMARK 500 ASP E 834 158.22 -34.86
REMARK 500 ASN E 850 -71.77 -65.42
REMARK 500 GLN E 851 56.47 -142.17
REMARK 500 ARG E 859 -75.54 -106.60
REMARK 500 ASP E 910 -135.78 64.82
REMARK 500 LYS E 917 143.76 -171.80
REMARK 500 PRO E 927 -74.37 -28.36
REMARK 500 TYR F1007 -166.84 -71.40
REMARK 500 ILE F1009 -7.26 162.24
REMARK 500 PRO F1010 176.70 -54.12
REMARK 500 THR F1012 179.82 -42.93
REMARK 500 GLU F1013 -49.09 170.47
REMARK 500
REMARK 500 THIS ENTRY HAS 55 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 MET C 421 THR C 422 -140.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BSGCAIR30339 RELATED DB: TARGETDB
DBREF 1NYE A 21 163 UNP P0C0L2 OSMC_ECOLI 0 142
DBREF 1NYE B 221 363 UNP P0C0L2 OSMC_ECOLI 0 142
DBREF 1NYE C 421 563 UNP P0C0L2 OSMC_ECOLI 0 142
DBREF 1NYE D 621 763 UNP P0C0L2 OSMC_ECOLI 0 142
DBREF 1NYE E 821 963 UNP P0C0L2 OSMC_ECOLI 0 142
DBREF 1NYE F 1021 1163 UNP P0C0L2 OSMC_ECOLI 0 142
SEQADV 1NYE HIS A 2 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS A 3 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS A 4 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS A 5 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP A 6 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR A 7 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP A 8 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ILE A 9 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PRO A 10 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR A 11 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR A 12 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLU A 13 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASN A 14 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE LEU A 15 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR A 16 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PHE A 17 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLN A 18 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLY A 19 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS A 20 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS B 202 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS B 203 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS B 204 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS B 205 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP B 206 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR B 207 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP B 208 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ILE B 209 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PRO B 210 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR B 211 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR B 212 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLU B 213 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASN B 214 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE LEU B 215 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR B 216 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PHE B 217 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLN B 218 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLY B 219 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS B 220 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS C 402 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS C 403 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS C 404 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS C 405 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP C 406 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR C 407 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP C 408 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ILE C 409 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PRO C 410 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR C 411 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR C 412 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLU C 413 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASN C 414 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE LEU C 415 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR C 416 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PHE C 417 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLN C 418 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLY C 419 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS C 420 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS D 602 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS D 603 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS D 604 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS D 605 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP D 606 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR D 607 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP D 608 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ILE D 609 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PRO D 610 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR D 611 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR D 612 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLU D 613 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASN D 614 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE LEU D 615 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR D 616 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PHE D 617 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLN D 618 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLY D 619 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS D 620 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS E 802 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS E 803 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS E 804 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS E 805 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP E 806 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR E 807 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP E 808 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ILE E 809 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PRO E 810 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR E 811 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR E 812 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLU E 813 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASN E 814 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE LEU E 815 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR E 816 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PHE E 817 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLN E 818 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLY E 819 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS E 820 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS F 1002 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS F 1003 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS F 1004 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS F 1005 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP F 1006 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR F 1007 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASP F 1008 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ILE F 1009 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PRO F 1010 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR F 1011 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE THR F 1012 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLU F 1013 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE ASN F 1014 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE LEU F 1015 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE TYR F 1016 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE PHE F 1017 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLN F 1018 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE GLY F 1019 UNP P0C0L2 EXPRESSION TAG
SEQADV 1NYE HIS F 1020 UNP P0C0L2 EXPRESSION TAG
SEQRES 1 A 162 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 A 162 LEU TYR PHE GLN GLY HIS MET THR ILE HIS LYS LYS GLY
SEQRES 3 A 162 GLN ALA HIS TRP GLU GLY ASP ILE LYS ARG GLY LYS GLY
SEQRES 4 A 162 THR VAL SER THR GLU SER GLY VAL LEU ASN GLN GLN PRO
SEQRES 5 A 162 TYR GLY PHE ASN THR ARG PHE GLU GLY GLU LYS GLY THR
SEQRES 6 A 162 ASN PRO GLU GLU LEU ILE GLY ALA ALA HIS ALA ALA CYS
SEQRES 7 A 162 PHE SER MET ALA LEU SER LEU MET LEU GLY GLU ALA GLY
SEQRES 8 A 162 PHE THR PRO THR SER ILE ASP THR THR ALA ASP VAL SER
SEQRES 9 A 162 LEU ASP LYS VAL ASP ALA GLY PHE ALA ILE THR LYS ILE
SEQRES 10 A 162 ALA LEU LYS SER GLU VAL ALA VAL PRO GLY ILE ASP ALA
SEQRES 11 A 162 SER THR PHE ASP GLY ILE ILE GLN LYS ALA LYS ALA GLY
SEQRES 12 A 162 CYS PRO VAL SER GLN VAL LEU LYS ALA GLU ILE THR LEU
SEQRES 13 A 162 ASP TYR GLN LEU LYS SER
SEQRES 1 B 162 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 B 162 LEU TYR PHE GLN GLY HIS MET THR ILE HIS LYS LYS GLY
SEQRES 3 B 162 GLN ALA HIS TRP GLU GLY ASP ILE LYS ARG GLY LYS GLY
SEQRES 4 B 162 THR VAL SER THR GLU SER GLY VAL LEU ASN GLN GLN PRO
SEQRES 5 B 162 TYR GLY PHE ASN THR ARG PHE GLU GLY GLU LYS GLY THR
SEQRES 6 B 162 ASN PRO GLU GLU LEU ILE GLY ALA ALA HIS ALA ALA CYS
SEQRES 7 B 162 PHE SER MET ALA LEU SER LEU MET LEU GLY GLU ALA GLY
SEQRES 8 B 162 PHE THR PRO THR SER ILE ASP THR THR ALA ASP VAL SER
SEQRES 9 B 162 LEU ASP LYS VAL ASP ALA GLY PHE ALA ILE THR LYS ILE
SEQRES 10 B 162 ALA LEU LYS SER GLU VAL ALA VAL PRO GLY ILE ASP ALA
SEQRES 11 B 162 SER THR PHE ASP GLY ILE ILE GLN LYS ALA LYS ALA GLY
SEQRES 12 B 162 CYS PRO VAL SER GLN VAL LEU LYS ALA GLU ILE THR LEU
SEQRES 13 B 162 ASP TYR GLN LEU LYS SER
SEQRES 1 C 162 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 C 162 LEU TYR PHE GLN GLY HIS MET THR ILE HIS LYS LYS GLY
SEQRES 3 C 162 GLN ALA HIS TRP GLU GLY ASP ILE LYS ARG GLY LYS GLY
SEQRES 4 C 162 THR VAL SER THR GLU SER GLY VAL LEU ASN GLN GLN PRO
SEQRES 5 C 162 TYR GLY PHE ASN THR ARG PHE GLU GLY GLU LYS GLY THR
SEQRES 6 C 162 ASN PRO GLU GLU LEU ILE GLY ALA ALA HIS ALA ALA CYS
SEQRES 7 C 162 PHE SER MET ALA LEU SER LEU MET LEU GLY GLU ALA GLY
SEQRES 8 C 162 PHE THR PRO THR SER ILE ASP THR THR ALA ASP VAL SER
SEQRES 9 C 162 LEU ASP LYS VAL ASP ALA GLY PHE ALA ILE THR LYS ILE
SEQRES 10 C 162 ALA LEU LYS SER GLU VAL ALA VAL PRO GLY ILE ASP ALA
SEQRES 11 C 162 SER THR PHE ASP GLY ILE ILE GLN LYS ALA LYS ALA GLY
SEQRES 12 C 162 CYS PRO VAL SER GLN VAL LEU LYS ALA GLU ILE THR LEU
SEQRES 13 C 162 ASP TYR GLN LEU LYS SER
SEQRES 1 D 162 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 D 162 LEU TYR PHE GLN GLY HIS MET THR ILE HIS LYS LYS GLY
SEQRES 3 D 162 GLN ALA HIS TRP GLU GLY ASP ILE LYS ARG GLY LYS GLY
SEQRES 4 D 162 THR VAL SER THR GLU SER GLY VAL LEU ASN GLN GLN PRO
SEQRES 5 D 162 TYR GLY PHE ASN THR ARG PHE GLU GLY GLU LYS GLY THR
SEQRES 6 D 162 ASN PRO GLU GLU LEU ILE GLY ALA ALA HIS ALA ALA CYS
SEQRES 7 D 162 PHE SER MET ALA LEU SER LEU MET LEU GLY GLU ALA GLY
SEQRES 8 D 162 PHE THR PRO THR SER ILE ASP THR THR ALA ASP VAL SER
SEQRES 9 D 162 LEU ASP LYS VAL ASP ALA GLY PHE ALA ILE THR LYS ILE
SEQRES 10 D 162 ALA LEU LYS SER GLU VAL ALA VAL PRO GLY ILE ASP ALA
SEQRES 11 D 162 SER THR PHE ASP GLY ILE ILE GLN LYS ALA LYS ALA GLY
SEQRES 12 D 162 CYS PRO VAL SER GLN VAL LEU LYS ALA GLU ILE THR LEU
SEQRES 13 D 162 ASP TYR GLN LEU LYS SER
SEQRES 1 E 162 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 E 162 LEU TYR PHE GLN GLY HIS MET THR ILE HIS LYS LYS GLY
SEQRES 3 E 162 GLN ALA HIS TRP GLU GLY ASP ILE LYS ARG GLY LYS GLY
SEQRES 4 E 162 THR VAL SER THR GLU SER GLY VAL LEU ASN GLN GLN PRO
SEQRES 5 E 162 TYR GLY PHE ASN THR ARG PHE GLU GLY GLU LYS GLY THR
SEQRES 6 E 162 ASN PRO GLU GLU LEU ILE GLY ALA ALA HIS ALA ALA CYS
SEQRES 7 E 162 PHE SER MET ALA LEU SER LEU MET LEU GLY GLU ALA GLY
SEQRES 8 E 162 PHE THR PRO THR SER ILE ASP THR THR ALA ASP VAL SER
SEQRES 9 E 162 LEU ASP LYS VAL ASP ALA GLY PHE ALA ILE THR LYS ILE
SEQRES 10 E 162 ALA LEU LYS SER GLU VAL ALA VAL PRO GLY ILE ASP ALA
SEQRES 11 E 162 SER THR PHE ASP GLY ILE ILE GLN LYS ALA LYS ALA GLY
SEQRES 12 E 162 CYS PRO VAL SER GLN VAL LEU LYS ALA GLU ILE THR LEU
SEQRES 13 E 162 ASP TYR GLN LEU LYS SER
SEQRES 1 F 162 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 F 162 LEU TYR PHE GLN GLY HIS MET THR ILE HIS LYS LYS GLY
SEQRES 3 F 162 GLN ALA HIS TRP GLU GLY ASP ILE LYS ARG GLY LYS GLY
SEQRES 4 F 162 THR VAL SER THR GLU SER GLY VAL LEU ASN GLN GLN PRO
SEQRES 5 F 162 TYR GLY PHE ASN THR ARG PHE GLU GLY GLU LYS GLY THR
SEQRES 6 F 162 ASN PRO GLU GLU LEU ILE GLY ALA ALA HIS ALA ALA CYS
SEQRES 7 F 162 PHE SER MET ALA LEU SER LEU MET LEU GLY GLU ALA GLY
SEQRES 8 F 162 PHE THR PRO THR SER ILE ASP THR THR ALA ASP VAL SER
SEQRES 9 F 162 LEU ASP LYS VAL ASP ALA GLY PHE ALA ILE THR LYS ILE
SEQRES 10 F 162 ALA LEU LYS SER GLU VAL ALA VAL PRO GLY ILE ASP ALA
SEQRES 11 F 162 SER THR PHE ASP GLY ILE ILE GLN LYS ALA LYS ALA GLY
SEQRES 12 F 162 CYS PRO VAL SER GLN VAL LEU LYS ALA GLU ILE THR LEU
SEQRES 13 F 162 ASP TYR GLN LEU LYS SER
FORMUL 7 HOH *87(H2 O)
HELIX 1 1 GLY A 55 GLU A 61 1 7
HELIX 2 2 ASN A 67 GLU A 90 1 24
HELIX 3 3 ASP A 130 CYS A 145 1 16
HELIX 4 4 CYS A 145 LEU A 151 1 7
HELIX 5 5 GLY B 255 PHE B 260 1 6
HELIX 6 6 ASN B 267 ALA B 291 1 25
HELIX 7 7 ASP B 330 CYS B 345 1 16
HELIX 8 8 CYS B 345 LEU B 351 1 7
HELIX 9 9 GLY C 455 GLU C 461 1 7
HELIX 10 10 ASN C 467 GLU C 490 1 24
HELIX 11 11 ASP C 530 CYS C 545 1 16
HELIX 12 12 CYS C 545 LEU C 551 1 7
HELIX 13 13 GLY D 655 PHE D 660 1 6
HELIX 14 14 ASN D 667 GLU D 690 1 24
HELIX 15 15 ASP D 730 CYS D 745 1 16
HELIX 16 16 CYS D 745 LEU D 751 1 7
HELIX 17 17 PHE E 817 MET E 821 5 5
HELIX 18 18 ASN E 867 ALA E 891 1 25
HELIX 19 19 ASP E 930 CYS E 945 1 16
HELIX 20 20 CYS E 945 LEU E 951 1 7
HELIX 21 21 PHE F 1017 HIS F 1020 5 4
HELIX 22 22 ASN F 1067 ALA F 1091 1 25
HELIX 23 23 ASP F 1130 CYS F 1145 1 16
HELIX 24 24 CYS F 1145 LEU F 1151 1 7
SHEET 1 A 7 GLN A 52 TYR A 54 0
SHEET 2 A 7 LYS A 39 THR A 44 -1 N VAL A 42 O GLN A 52
SHEET 3 A 7 ILE A 23 GLU A 32 -1 N GLN A 28 O SER A 43
SHEET 4 A 7 SER B 297 VAL B 309 -1 O VAL B 304 N LYS A 25
SHEET 5 A 7 GLY B 312 ALA B 325 -1 O GLY B 312 N VAL B 309
SHEET 6 A 7 GLU B 354 LYS B 362 1 O ASP B 358 N SER B 322
SHEET 7 A 7 HIS F1004 ASP F1006 -1 O ASP F1006 N LEU B 357
SHEET 1 B 7 GLN B 252 TYR B 254 0
SHEET 2 B 7 LYS B 239 THR B 244 -1 N GLY B 240 O TYR B 254
SHEET 3 B 7 ILE B 223 GLU B 232 -1 N GLN B 228 O SER B 243
SHEET 4 B 7 SER A 97 VAL A 109 -1 N VAL A 104 O LYS B 225
SHEET 5 B 7 GLY A 112 ALA A 125 -1 O LYS A 117 N SER A 105
SHEET 6 B 7 GLU A 154 LYS A 162 1 O LYS A 162 N VAL A 124
SHEET 7 B 7 HIS D 604 ASP D 606 -1 O HIS D 604 N TYR A 159
SHEET 1 C 6 GLN C 452 TYR C 454 0
SHEET 2 C 6 LYS C 439 THR C 444 -1 N VAL C 442 O GLN C 452
SHEET 3 C 6 ILE C 423 GLU C 432 -1 N HIS C 430 O THR C 441
SHEET 4 C 6 SER D 697 ASP D 707 -1 O LEU D 706 N ILE C 423
SHEET 5 C 6 ALA D 714 ALA D 725 -1 O GLU D 723 N ASP D 699
SHEET 6 C 6 GLU D 754 LYS D 762 1 O ASP D 758 N LEU D 720
SHEET 1 D 6 GLU C 554 LYS C 562 0
SHEET 2 D 6 GLY C 512 ALA C 525 1 N LEU C 520 O THR C 556
SHEET 3 D 6 SER C 497 VAL C 509 -1 N SER C 505 O LYS C 517
SHEET 4 D 6 ILE D 623 GLU D 632 -1 O LYS D 625 N VAL C 504
SHEET 5 D 6 LYS D 639 THR D 644 -1 O SER D 643 N GLN D 628
SHEET 6 D 6 GLN D 652 TYR D 654 -1 O TYR D 654 N GLY D 640
SHEET 1 E 6 GLN E 852 PRO E 853 0
SHEET 2 E 6 LYS E 839 THR E 844 -1 N VAL E 842 O GLN E 852
SHEET 3 E 6 ILE E 823 GLU E 832 -1 N GLN E 828 O SER E 843
SHEET 4 E 6 SER F1097 VAL F1109 -1 O VAL F1104 N LYS E 825
SHEET 5 E 6 GLY F1112 ALA F1125 -1 O LYS F1121 N THR F1101
SHEET 6 E 6 GLU F1154 LYS F1162 1 O LYS F1162 N VAL F1124
SHEET 1 F 6 GLU E 954 LYS E 962 0
SHEET 2 F 6 GLY E 912 ALA E 925 1 N VAL E 924 O LYS E 962
SHEET 3 F 6 SER E 897 VAL E 909 -1 N ASP E 907 O ALA E 914
SHEET 4 F 6 THR F1022 GLU F1032 -1 O ILE F1023 N LEU E 906
SHEET 5 F 6 LYS F1039 THR F1044 -1 O SER F1043 N GLN F1028
SHEET 6 F 6 GLN F1052 TYR F1054 -1 O GLN F1052 N VAL F1042
CRYST1 49.529 90.291 112.677 90.00 93.90 90.00 P 1 21 1 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 0.020190 0.000000 0.001378 0.00000
SCALE2 0.000000 0.011075 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008896 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
