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HEADER HYDROLASE 14-MAR-02 1L7A
TITLE STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF CEPHALOSPORIN C
TITLE 2 DEACETYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEPHALOSPORIN C DEACETYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.41;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 GENE: CAH;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET VARIANT;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, ALPHA-BETA-ALPHA SANDWICH
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,O.KOROLEVA,F.COLLERT,A.JOACHIMIAK
REVDAT 1 21-JAN-03 1L7A 0
JRNL AUTH R.ZHANG,O.KOROLEVA,F.COLLERT,A.JOACHIMIAK
JRNL TITL 1.5A CRYSTAL STRUCTURE OF THE CEPHALOSPORIN C
JRNL TITL 2 DEACETYLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 185125
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) : 0.185
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9185
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 27835
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE : 0.2120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1429
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 503
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : -0.60000
REMARK 3 B12 (A**2) : 0.49000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.16
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.06
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 2.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.94
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) : 1.260 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.750 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.350 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.170 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 52.58
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: THE NUMBER OF REFLECTIONS USED IN
REMARK 3 REFINEMENT INCLUDE FRIEDEL PAIRS. THEREFORE, THE NUMBER OF
REMARK 3 REFLECTIONS FOR REFINEMENT IS LARGER THAN THE NUMBER COLLECTED.
REMARK 4
REMARK 4 1L7A COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-2002.
REMARK 100 THE RCSB ID CODE IS RCSB015704.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793, 0.9791, 0.9520
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DTCOLLECT
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96738
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.920
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.54
REMARK 200 R MERGE FOR SHELL (I) : 0.32500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.955
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 2/3+X,1/3+Y,1/3+Z
REMARK 290 8555 2/3-Y,1/3+X-Y,1/3+Z
REMARK 290 9555 2/3-X+Y,1/3-X,1/3+Z
REMARK 290 10555 2/3+Y,1/3+X,1/3-Z
REMARK 290 11555 2/3+X-Y,1/3-Y,1/3-Z
REMARK 290 12555 2/3-X,1/3-X+Y,1/3-Z
REMARK 290 13555 1/3+X,2/3+Y,2/3+Z
REMARK 290 14555 1/3-Y,2/3+X-Y,2/3+Z
REMARK 290 15555 1/3-X+Y,2/3-X,2/3+Z
REMARK 290 16555 1/3+Y,2/3+X,2/3-Z
REMARK 290 17555 1/3+X-Y,2/3-Y,2/3-Z
REMARK 290 18555 1/3-X,2/3-X+Y,2/3-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 -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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 78.22300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.16207
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 43.91600
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 78.22300
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 45.16207
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 43.91600
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 78.22300
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 45.16207
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 43.91600
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 78.22300
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 45.16207
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 43.91600
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 78.22300
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 45.16207
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 43.91600
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 78.22300
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 45.16207
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 43.91600
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 90.32414
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 87.83200
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 90.32414
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 87.83200
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 90.32414
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 87.83200
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 90.32414
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 87.83200
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 90.32414
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 87.83200
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 90.32414
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 87.83200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMT1 2 -0.500000 -0.866025 0.000000 156.44600
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 78.22300
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 135.48621
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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
REMARK 500 O HOH 551 O HOH 906 1.88
REMARK 500 O HOH 440 O HOH 604 2.08
REMARK 500 O HOH 454 O HOH 732 2.11
REMARK 500 O HOH 678 O HOH 823 2.12
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 OE2 GLU B 17 OE2 GLU B 17 16544 1.51
REMARK 500 CD GLU B 17 OE2 GLU B 17 16544 1.58
REMARK 500 OE1 GLU B 17 OE2 GLU B 17 16544 1.68
REMARK 500 CD GLU B 17 CD GLU B 17 16544 1.80
REMARK 500 OE1 GLU B 17 CD GLU B 17 16544 1.88
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 81 CD PRO A 81 CG 0.101
REMARK 500 MET A 138 SD MET A 138 CG 0.051
REMARK 500 PRO A 221 CD PRO A 221 CG 0.103
REMARK 500 MET A 263 SD MET A 263 CG 0.049
REMARK 500 PRO B 81 CD PRO B 81 CG 0.099
REMARK 500 SER B 123 N ARG B 122 C -0.050
REMARK 500 GLN B 220 C GLN B 220 CA 0.071
REMARK 500 GLN B 220 O GLN B 220 C -0.062
REMARK 500 PRO B 221 CD PRO B 221 CG 0.095
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLN A 220 C - N - CA ANGL. DEV. =-15.0 DEGREES
REMARK 500 GLN B 220 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 GLN B 220 CA - C - O ANGL. DEV. =-33.2 DEGREES
REMARK 500 PRO B 221 O - C - N ANGL. DEV. =-16.1 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ARG A 122 -56.26 68.38
REMARK 500 SER A 181 -116.41 46.49
REMARK 500 ARG B 122 -45.34 64.00
REMARK 500 SER B 181 -114.85 45.72
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 GLN B 220 PRO B 221 60.08
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 IT IS CLEAR IN THE DENSITY MAP THAT RESIDUES
REMARK 999 122 AND 315 ARE ARG AND ILE. THE REASON
REMARK 999 FOR THE DISCREPANCY IS NOT KNOWN.
DBREF 1L7A A 1 318 SWS 2632604 CAB12112 1 318
DBREF 1L7A B 1 318 SWS 2632604 CAB12112 1 318
SEQADV 1L7A ARG A 122 SWS 2632604 SER 122 SEE REMARK 999
SEQADV 1L7A ILE A 315 SWS 2632604 HIS 315 SEE REMARK 999
SEQADV 1L7A ARG B 122 SWS 2632604 SER 122 SEE REMARK 999
SEQADV 1L7A ILE B 315 SWS 2632604 HIS 315 SEE REMARK 999
SEQRES 1 A 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 A 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 A 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 A 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 A 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 A 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 A 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 A 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 A 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 A 318 ARG GLY GLN GLN ARG SER GLU ASP THR SER ILE SER PRO
SEQRES 11 A 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 A 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 A 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 A 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 A 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 A 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 A 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 A 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 A 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 A 318 PHE ASP ILE MET ASN LEU ALA ASP ARG VAL LYS VAL PRO
SEQRES 21 A 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 A 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 A 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 A 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 A 318 LYS GLN ILE LEU LYS GLY
SEQRES 1 B 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 B 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 B 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 B 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 B 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 B 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 B 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 B 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 B 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 B 318 ARG GLY GLN GLN ARG SER GLU ASP THR SER ILE SER PRO
SEQRES 11 B 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 B 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 B 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 B 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 B 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 B 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 B 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 B 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 B 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 B 318 PHE ASP ILE MET ASN LEU ALA ASP ARG VAL LYS VAL PRO
SEQRES 21 B 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 B 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 B 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 B 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 B 318 LYS GLN ILE LEU LYS GLY
FORMUL 3 HOH *503(H2 O1)
HELIX 1 1 PRO A 7 THR A 13 1 7
HELIX 2 2 ASP A 23 LYS A 37 1 15
HELIX 3 3 PHE A 64 ASN A 66 5 3
HELIX 4 4 TYR A 95 GLY A 97 5 3
HELIX 5 5 GLU A 98 HIS A 108 1 11
HELIX 6 6 TYR A 148 PHE A 167 1 20
HELIX 7 7 SER A 181 SER A 194 1 14
HELIX 8 8 ASN A 209 ALA A 217 1 9
HELIX 9 9 LEU A 223 ASN A 232 1 10
HELIX 10 10 SER A 234 TYR A 247 1 14
HELIX 11 11 ASP A 249 ALA A 254 1 6
HELIX 12 12 ASP A 255 VAL A 257 5 3
HELIX 13 13 PRO A 273 LEU A 284 1 12
HELIX 14 14 ILE A 301 LYS A 317 1 17
HELIX 15 15 PRO B 7 GLN B 12 1 6
HELIX 16 16 ASP B 23 LYS B 37 1 15
HELIX 17 17 PHE B 64 ASN B 66 5 3
HELIX 18 18 TYR B 95 GLY B 97 5 3
HELIX 19 19 GLU B 98 HIS B 108 1 11
HELIX 20 20 TYR B 148 SER B 166 1 19
HELIX 21 21 SER B 181 SER B 194 1 14
HELIX 22 22 ASN B 209 ALA B 217 1 9
HELIX 23 23 TYR B 222 ASN B 232 1 11
HELIX 24 24 SER B 234 TYR B 247 1 14
HELIX 25 25 ASP B 249 ALA B 254 1 6
HELIX 26 26 ASP B 255 VAL B 257 5 3
HELIX 27 27 PRO B 273 LEU B 284 1 12
HELIX 28 28 ILE B 301 LYS B 317 1 17
SHEET 1 A 9 ASP A 43 VAL A 47 0
SHEET 2 A 9 VAL A 54 SER A 63 -1 O VAL A 56 N VAL A 47
SHEET 3 A 9 ALA A 67 PRO A 76 -1 O ILE A 69 N TYR A 61
SHEET 4 A 9 ALA A 111 MET A 115 -1 O THR A 112 N ALA A 74
SHEET 5 A 9 HIS A 82 TYR A 88 1 N LYS A 87 O PHE A 113
SHEET 6 A 9 VAL A 170 GLY A 180 1 O ASP A 171 N HIS A 82
SHEET 7 A 9 ALA A 199 ASP A 203 1 O VAL A 201 N VAL A 177
SHEET 8 A 9 VAL A 261 GLY A 266 1 O LEU A 262 N ALA A 202
SHEET 9 A 9 LYS A 288 TYR A 293 1 O LYS A 291 N MET A 263
SHEET 1 B 9 ASP B 43 PRO B 46 0
SHEET 2 B 9 VAL B 54 LYS B 62 -1 O THR B 60 N ASP B 43
SHEET 3 B 9 ARG B 68 PRO B 76 -1 O GLY B 71 N LEU B 59
SHEET 4 B 9 ALA B 111 MET B 115 -1 O THR B 112 N ALA B 74
SHEET 5 B 9 HIS B 82 TYR B 88 1 N LYS B 87 O PHE B 113
SHEET 6 B 9 VAL B 170 GLY B 179 1 O ASP B 171 N HIS B 82
SHEET 7 B 9 ALA B 199 ALA B 202 1 O VAL B 201 N VAL B 177
SHEET 8 B 9 VAL B 261 GLY B 266 1 O LEU B 262 N ALA B 202
SHEET 9 B 9 LYS B 288 TYR B 293 1 O LYS B 291 N MET B 263
CISPEP 1 GLY A 80 PRO A 81 0 -1.68
CISPEP 2 GLN A 220 PRO A 221 0 -4.47
CISPEP 3 GLY B 80 PRO B 81 0 -1.48
CRYST1 156.446 156.446 131.748 90.00 90.00 120.00 H 3 2 36
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 0.006392 0.003690 0.000000 0.00000
SCALE2 0.000000 0.007381 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007590 0.00000
TER 2538 GLY A 318
TER 5076 GLY B 318
MASTER 380 0 0 28 18 0 0 6 5577 2 0 50
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