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HEADER HYDROLASE 20-FEB-03 1ODS
TITLE CEPHALOSPORIN C DEACETYLASE FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEPHALOSPORIN C DEACETYLASE;
COMPND 3 SYNONYM: MULTI-FUNCTIONAL ESTERASE, CAH;
COMPND 4 CHAIN: A, B, C, D, E, F, G, H;
COMPND 5 EC: 3.1.1.41;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS ALPHA/BETA HYDROLASE, ACETYLXYLAN, CARBOHYDRATE ESTERASE,
KEYWDS 2 CEPHALOSPORIN, X-RAY STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.VINCENT,S.J.CHARNOCK,K.H.G.VERSCHUEREN,J.P.TURKENBURG,
AUTHOR 2 D.J.SCOTT,W.A.OFFEN,S.ROBERTS,G.PELL,H.J.GILBERT,
AUTHOR 3 J.A.BRANNIGAN,G.J.DAVIES
REVDAT 1 10-JUL-03 1ODS 0
JRNL AUTH F.VINCENT,S.CHARNOCK,K.VERSCHUEREN,J.TURKENBURG,
JRNL AUTH 2 D.SCOTT,W.OFFEN,S.ROBERTS,G.PELL,H.GILBERT,G.DAVIES,
JRNL AUTH 3 J.BRANNIGAN
JRNL TITL MULTIFUNCTIONAL XYLOOLIGOSACCHARIDE/CEPHALOSPORIN C
JRNL TITL 2 DEACETYLASE REVEALED BY THE HEXAMERIC STRUCTURE OF
JRNL TITL 3 THE BACILLUS SUBTILIS ENZYME AT 1.9A RESOLUTION
JRNL REF J.MOL.BIOL. V. 330 593 2003
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.9 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.67
REMARK 3 NUMBER OF REFLECTIONS : 189201
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) : 0.15387
REMARK 3 R VALUE (WORKING SET) : 0.15215
REMARK 3 FREE R VALUE : 0.18611
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 10036
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW : 1.949
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13777
REMARK 3 BIN R VALUE (WORKING SET) : 0.201
REMARK 3 BIN FREE R VALUE SET COUNT : 758
REMARK 3 BIN FREE R VALUE : 0.25
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20301
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 2055
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.819
REMARK 3 B11 (A**2) : 0.02
REMARK 3 B22 (A**2) : 0.02
REMARK 3 B33 (A**2) : -0.02
REMARK 3 B12 (A**2) : 0.01
REMARK 3 B13 (A**2) : 0.0
REMARK 3 B23 (A**2) : 0.0
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.139
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.025
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 20862 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 18477 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 28329 ; 1.327 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 43147 ; 1.520 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2520 ; 5.252 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3428 ;14.602 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3019 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 23176 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4336 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 4377 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 21455 ; 0.262 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 10311 ; 0.098 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 1439 ; 0.136 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 19 ; 0.273 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 117 ; 0.345 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 37 ; 0.201 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 12593 ; 0.449 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 20338 ; 0.804 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 8269 ; 1.534 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 7991 ; 2.464 ; 4.500
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 (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NONE
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NONE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 1ODS COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 21-FEB-2003.
REMARK 100 THE EBI ID CODE IS EBI-12215.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE BM14
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786, 0.9786, 0.9184,
REMARK 200 0.908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 199895
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.3
REMARK 200 R MERGE (I) : 0.045
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.9
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.0
REMARK 200 R MERGE FOR SHELL (I) : 0.221
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.4
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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 Y-X,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 Y-X+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 Y-X+1/3,-X+2/3,Z+2/3
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 1.000000 0.000000 0.000000 157.60750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 90.99473
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.82767
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 157.60750
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 90.99473
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 22.82767
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 157.60750
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 90.99473
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.82767
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 181.98947
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 45.65533
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 181.98947
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 45.65533
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 181.98947
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 45.65533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 2 .. 317 B 2 .. 317 0.104
REMARK 295 M 2 A 2 .. 317 C 2 .. 317 0.112
REMARK 295 M 3 A 2 .. 317 D 2 .. 317 0.098
REMARK 295 M 4 A 2 .. 317 E 2 .. 317 0.093
REMARK 295 M 5 A 2 .. 317 F 2 .. 317 0.092
REMARK 295 M 6 A 2 .. 317 G 2 .. 317 0.089
REMARK 295 M 7 A 2 .. 317 H 2 .. 317 0.081
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: THE NCS APPLIED TO OBTAINED MOLECULES
REMARK 295 B, C, D, E, F, G, H RECONSTITUTE THE HEXAMER
REMARK 295 WHICH IS THE ACTIVE OLIGOMERIC STATE OF THE ENZYME
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 10 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: HEXAMERIC
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 315.21500
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 157.60750
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 272.98420
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, G, H, E
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 1
REMARK 465 GLY A 318
REMARK 465 MET B 1
REMARK 465 GLY B 318
REMARK 465 MET C 1
REMARK 465 GLY C 318
REMARK 465 MET D 1
REMARK 465 GLY D 318
REMARK 465 MET E 1
REMARK 465 GLY E 318
REMARK 465 MET F 1
REMARK 465 GLY F 318
REMARK 465 MET G 1
REMARK 465 GLY G 318
REMARK 465 MET H 1
REMARK 465 GLY H 318
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 LEU C 290 CA - CB - CG ANGL. DEV. = 10.5 DEGREES
REMARK 500 GLU D 79 C - N - CA ANGL. DEV. = -9.4 DEGREES
REMARK 500 GLU D 79 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 LEU H 3 CA - CB - CG ANGL. DEV. = 9.2 DEGREES
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ILE A 69 CG1 ILE A 69 CD1 -0.212
REMARK 500 MET B 102 SD MET B 102 CE -0.310
REMARK 500 MET D 102 SD MET D 102 CE -0.213
REMARK 500 MET F 102 SD MET F 102 CE -0.252
REMARK 500 MET H 102 SD MET H 102 CE -0.170
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 OE2 GLU A 289 NZ LYS A 291 2.09
REMARK 500 OD2 ASP G 203 O HOH T 121 2.08
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
REMARK 500 O HOH Y 141 O HOH Z 177 3665 2.01
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 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
REMARK 500 SER A 122 -46.38 68.54
REMARK 500 SER A 181 -112.19 57.39
REMARK 500 SER B 122 -47.89 62.90
REMARK 500 SER B 181 -115.68 58.61
REMARK 500 SER C 122 -48.55 67.21
REMARK 500 SER C 181 -116.72 62.35
REMARK 500 SER D 122 -47.76 63.23
REMARK 500 SER D 181 -117.65 57.78
REMARK 500 SER E 122 -48.04 68.04
REMARK 500 SER E 181 -117.27 58.39
REMARK 500 SER F 122 -48.26 65.76
REMARK 500 SER F 181 -115.22 57.65
REMARK 500 SER G 122 -51.11 66.27
REMARK 500 SER G 181 -115.37 60.78
REMARK 500 SER H 122 -49.57 66.93
REMARK 500 SER H 181 -115.31 60.65
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 525 C X
REMARK 525 D W
REMARK 525 E V
REMARK 525 F U
REMARK 525 G T
REMARK 525 H S
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM MG MG A1319 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 105Z O
REMARK 600 2 HOH 197Z O 174.2
REMARK 600 3 HOH 200Z O 102.2 83.1
REMARK 600 4 HOH 201Z O 88.0 94.0 93.5
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM MG MG A1320 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 83W O
REMARK 600 2 HOH 79W O 94.1
REMARK 600 3 HOH 36Z O 86.7 86.6
REMARK 600 4 HOH 35Z O 96.1 167.5 86.7
REMARK 600 5 HOH 84Z O 87.2 98.2 172.5 89.6
REMARK 600 6 HOH 88Z O 179.3 85.6 93.8 84.3 92.3
REMARK 600 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN F
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN H
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN E
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN G
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE FOR CHAIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L7A RELATED DB: PDB
REMARK 900 STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF
REMARK 900 CEPHALOSPORIN CDEACETYLASE
DBREF 1ODS A 1 318 SWS P94388 P94388 1 318
DBREF 1ODS B 1 318 SWS P94388 P94388 1 318
DBREF 1ODS C 1 318 SWS P94388 P94388 1 318
DBREF 1ODS D 1 318 SWS P94388 P94388 1 318
DBREF 1ODS E 1 318 SWS P94388 P94388 1 318
DBREF 1ODS F 1 318 SWS P94388 P94388 1 318
DBREF 1ODS G 1 318 SWS P94388 P94388 1 318
DBREF 1ODS H 1 318 SWS P94388 P94388 1 318
SEQADV 1ODS GLU A 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR A 255 SWS P94388 ASP 255 CONFLICT
SEQADV 1ODS GLU B 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR B 255 SWS P94388 ASP 255 CONFLICT
SEQADV 1ODS GLU C 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR C 255 SWS P94388 ASP 255 CONFLICT
SEQADV 1ODS GLU D 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR D 255 SWS P94388 ASP 255 CONFLICT
SEQADV 1ODS GLU E 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR E 255 SWS P94388 ASP 255 CONFLICT
SEQADV 1ODS GLU F 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR F 255 SWS P94388 ASP 255 CONFLICT
SEQADV 1ODS GLU G 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR G 255 SWS P94388 ASP 255 CONFLICT
SEQADV 1ODS GLU H 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODS TYR H 255 SWS P94388 ASP 255 CONFLICT
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 SER 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 GLU 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 TYR 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 HIS 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 SER 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 GLU 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 TYR 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 HIS LEU LYS GLY
SEQRES 1 C 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 C 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 C 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 C 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 C 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 C 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 C 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 C 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 C 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 C 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 C 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 C 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 C 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 C 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 C 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 C 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 C 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 C 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 C 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 C 318 PHE ASP ILE MET ASN LEU ALA TYR ARG VAL LYS VAL PRO
SEQRES 21 C 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 C 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 C 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 C 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 C 318 LYS GLN HIS LEU LYS GLY
SEQRES 1 D 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 D 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 D 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 D 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 D 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 D 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 D 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 D 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 D 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 D 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 D 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 D 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 D 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 D 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 D 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 D 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 D 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 D 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 D 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 D 318 PHE ASP ILE MET ASN LEU ALA TYR ARG VAL LYS VAL PRO
SEQRES 21 D 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 D 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 D 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 D 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 D 318 LYS GLN HIS LEU LYS GLY
SEQRES 1 E 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 E 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 E 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 E 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 E 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 E 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 E 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 E 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 E 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 E 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 E 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 E 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 E 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 E 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 E 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 E 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 E 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 E 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 E 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 E 318 PHE ASP ILE MET ASN LEU ALA TYR ARG VAL LYS VAL PRO
SEQRES 21 E 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 E 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 E 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 E 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 E 318 LYS GLN HIS LEU LYS GLY
SEQRES 1 F 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 F 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 F 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 F 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 F 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 F 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 F 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 F 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 F 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 F 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 F 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 F 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 F 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 F 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 F 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 F 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 F 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 F 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 F 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 F 318 PHE ASP ILE MET ASN LEU ALA TYR ARG VAL LYS VAL PRO
SEQRES 21 F 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 F 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 F 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 F 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 F 318 LYS GLN HIS LEU LYS GLY
SEQRES 1 G 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 G 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 G 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 G 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 G 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 G 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 G 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 G 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 G 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 G 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 G 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 G 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 G 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 G 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 G 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 G 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 G 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 G 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 G 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 G 318 PHE ASP ILE MET ASN LEU ALA TYR ARG VAL LYS VAL PRO
SEQRES 21 G 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 G 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 G 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 G 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 G 318 LYS GLN HIS LEU LYS GLY
SEQRES 1 H 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 H 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 H 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 H 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 H 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 H 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 H 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 H 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 H 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 H 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 H 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 H 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 H 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 H 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY SER GLN
SEQRES 15 H 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 H 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 H 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 H 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 H 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 H 318 PHE ASP ILE MET ASN LEU ALA TYR ARG VAL LYS VAL PRO
SEQRES 21 H 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 H 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 H 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 H 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 H 318 LYS GLN HIS LEU LYS GLY
HET CL B1318 1
HET CL F1318 1
HET CL D1318 1
HET CL C1318 1
HET CL A1318 1
HET CL H1318 1
HET CL E1318 1
HET CL G1318 1
HET MG A1319 1
HET MG A1320 1
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 9 CL 8(CL1 1-)
FORMUL 10 MG 2(MG1 2+)
FORMUL 11 HOH *2055(H2 O1)
HELIX 1 1 PRO A 7 GLN A 12 1 6
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 SER A 166 1 19
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 TYR A 222 ASN A 232 1 11
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 TYR 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 TYR B 255 VAL B 257 5 3
HELIX 27 27 PRO B 273 HIS B 283 1 11
HELIX 28 28 ILE B 301 LYS B 317 1 17
HELIX 29 29 PRO C 7 TYR C 14 1 8
HELIX 30 30 ASP C 23 LYS C 37 1 15
HELIX 31 31 PHE C 64 ASN C 66 5 3
HELIX 32 32 TYR C 95 GLY C 97 5 3
HELIX 33 33 GLU C 98 HIS C 108 1 11
HELIX 34 34 TYR C 148 SER C 166 1 19
HELIX 35 35 SER C 181 SER C 194 1 14
HELIX 36 36 ASN C 209 ALA C 217 1 9
HELIX 37 37 TYR C 222 ASN C 232 1 11
HELIX 38 38 SER C 234 TYR C 247 1 14
HELIX 39 39 ASP C 249 ALA C 254 1 6
HELIX 40 40 TYR C 255 VAL C 257 5 3
HELIX 41 41 PRO C 273 LEU C 284 1 12
HELIX 42 42 ILE C 301 LYS C 317 1 17
HELIX 43 43 PRO D 7 GLN D 12 1 6
HELIX 44 44 ASP D 23 VAL D 38 1 16
HELIX 45 45 PHE D 64 ASN D 66 5 3
HELIX 46 46 TYR D 95 GLY D 97 5 3
HELIX 47 47 GLU D 98 HIS D 108 1 11
HELIX 48 48 TYR D 148 SER D 166 1 19
HELIX 49 49 SER D 181 SER D 194 1 14
HELIX 50 50 ASN D 209 ALA D 217 1 9
HELIX 51 51 LEU D 223 ASN D 232 1 10
HELIX 52 52 SER D 234 TYR D 247 1 14
HELIX 53 53 ASP D 249 ALA D 254 1 6
HELIX 54 54 TYR D 255 VAL D 257 5 3
HELIX 55 55 PRO D 273 HIS D 283 1 11
HELIX 56 56 ILE D 301 LYS D 317 1 17
HELIX 57 57 PRO E 7 GLN E 12 1 6
HELIX 58 58 ASP E 23 LYS E 37 1 15
HELIX 59 59 PHE E 64 ASN E 66 5 3
HELIX 60 60 TYR E 95 GLY E 97 5 3
HELIX 61 61 GLU E 98 HIS E 108 1 11
HELIX 62 62 TYR E 148 SER E 165 1 18
HELIX 63 63 SER E 181 SER E 194 1 14
HELIX 64 64 ASN E 209 ALA E 217 1 9
HELIX 65 65 TYR E 222 ASN E 232 1 11
HELIX 66 66 SER E 234 TYR E 247 1 14
HELIX 67 67 ASP E 249 ALA E 254 1 6
HELIX 68 68 TYR E 255 VAL E 257 5 3
HELIX 69 69 PRO E 273 HIS E 283 1 11
HELIX 70 70 ILE E 301 LYS E 317 1 17
HELIX 71 71 PRO F 7 GLN F 12 1 6
HELIX 72 72 ASP F 23 LYS F 37 1 15
HELIX 73 73 PHE F 64 ASN F 66 5 3
HELIX 74 74 TYR F 95 GLY F 97 5 3
HELIX 75 75 GLU F 98 HIS F 108 1 11
HELIX 76 76 TYR F 148 SER F 166 1 19
HELIX 77 77 SER F 181 SER F 194 1 14
HELIX 78 78 ASN F 209 ALA F 217 1 9
HELIX 79 79 TYR F 222 ASN F 232 1 11
HELIX 80 80 SER F 234 TYR F 247 1 14
HELIX 81 81 ASP F 249 ALA F 254 1 6
HELIX 82 82 TYR F 255 VAL F 257 5 3
HELIX 83 83 PRO F 273 LEU F 284 1 12
HELIX 84 84 ILE F 301 LYS F 317 1 17
HELIX 85 85 PRO G 7 GLN G 12 1 6
HELIX 86 86 ASP G 23 LYS G 37 1 15
HELIX 87 87 PHE G 64 ASN G 66 5 3
HELIX 88 88 TYR G 95 GLY G 97 5 3
HELIX 89 89 GLU G 98 HIS G 108 1 11
HELIX 90 90 TYR G 148 SER G 166 1 19
HELIX 91 91 SER G 181 SER G 194 1 14
HELIX 92 92 ASN G 209 ALA G 217 1 9
HELIX 93 93 TYR G 222 ASN G 232 1 11
HELIX 94 94 SER G 234 TYR G 247 1 14
HELIX 95 95 ASP G 249 ALA G 254 1 6
HELIX 96 96 TYR G 255 VAL G 257 5 3
HELIX 97 97 PRO G 273 HIS G 283 1 11
HELIX 98 98 ILE G 301 LYS G 317 1 17
HELIX 99 99 PRO H 7 GLN H 12 1 6
HELIX 100 100 ASP H 23 LYS H 37 1 15
HELIX 101 101 PHE H 64 ASN H 66 5 3
HELIX 102 102 TYR H 95 GLY H 97 5 3
HELIX 103 103 GLU H 98 HIS H 108 1 11
HELIX 104 104 TYR H 148 SER H 166 1 19
HELIX 105 105 SER H 181 SER H 194 1 14
HELIX 106 106 ASN H 209 ALA H 217 1 9
HELIX 107 107 TYR H 222 ASN H 232 1 11
HELIX 108 108 SER H 234 TYR H 247 1 14
HELIX 109 109 ASP H 249 ALA H 254 1 6
HELIX 110 110 TYR H 255 VAL H 257 5 3
HELIX 111 111 PRO H 273 LEU H 284 1 12
HELIX 112 112 ILE H 301 LYS H 317 1 17
SHEET 1 AA 9 ASP A 43 VAL A 47 0
SHEET 2 AA 9 VAL A 54 SER A 63 -1 O VAL A 56 N VAL A 47
SHEET 3 AA 9 ALA A 67 PRO A 76 -1 O ALA A 67 N SER A 63
SHEET 4 AA 9 ALA A 111 MET A 115 -1 O THR A 112 N ALA A 74
SHEET 5 AA 9 HIS A 82 TYR A 88 1 O PRO A 83 N ALA A 111
SHEET 6 AA 9 VAL A 170 GLY A 180 1 N ASP A 171 O HIS A 82
SHEET 7 AA 9 ALA A 199 ASP A 203 1 O ALA A 199 N VAL A 177
SHEET 8 AA 9 VAL A 261 GLY A 266 1 O LEU A 262 N ALA A 202
SHEET 9 AA 9 LYS A 288 TYR A 293 1 O GLU A 289 N MET A 263
SHEET 1 BA 9 ASP B 43 VAL B 47 0
SHEET 2 BA 9 VAL B 54 SER B 63 -1 O VAL B 56 N VAL B 47
SHEET 3 BA 9 ALA B 67 PRO B 76 -1 O ALA B 67 N SER B 63
SHEET 4 BA 9 ALA B 111 MET B 115 -1 O THR B 112 N ALA B 74
SHEET 5 BA 9 HIS B 82 TYR B 88 1 O PRO B 83 N ALA B 111
SHEET 6 BA 9 VAL B 170 GLY B 180 1 N ASP B 171 O HIS B 82
SHEET 7 BA 9 ALA B 199 ASP B 203 1 O ALA B 199 N VAL B 177
SHEET 8 BA 9 VAL B 261 GLY B 266 1 O LEU B 262 N ALA B 202
SHEET 9 BA 9 LYS B 288 TYR B 293 1 O GLU B 289 N MET B 263
SHEET 1 CA 9 ASP C 43 VAL C 47 0
SHEET 2 CA 9 VAL C 54 LYS C 62 -1 O VAL C 56 N VAL C 47
SHEET 3 CA 9 ARG C 68 PRO C 76 -1 O ILE C 69 N TYR C 61
SHEET 4 CA 9 ALA C 111 MET C 115 -1 O THR C 112 N ALA C 74
SHEET 5 CA 9 HIS C 82 TYR C 88 1 O PRO C 83 N ALA C 111
SHEET 6 CA 9 VAL C 170 GLY C 180 1 N ASP C 171 O HIS C 82
SHEET 7 CA 9 ALA C 199 ASP C 203 1 O ALA C 199 N VAL C 177
SHEET 8 CA 9 VAL C 261 GLY C 266 1 O LEU C 262 N ALA C 202
SHEET 9 CA 9 LYS C 288 TYR C 293 1 O GLU C 289 N MET C 263
SHEET 1 DA 9 ASP D 43 VAL D 47 0
SHEET 2 DA 9 VAL D 54 LYS D 62 -1 O VAL D 56 N VAL D 47
SHEET 3 DA 9 ARG D 68 PRO D 76 -1 O ILE D 69 N TYR D 61
SHEET 4 DA 9 ALA D 111 MET D 115 -1 O THR D 112 N ALA D 74
SHEET 5 DA 9 HIS D 82 TYR D 88 1 O PRO D 83 N ALA D 111
SHEET 6 DA 9 VAL D 170 GLY D 180 1 N ASP D 171 O HIS D 82
SHEET 7 DA 9 ALA D 199 ASP D 203 1 O ALA D 199 N VAL D 177
SHEET 8 DA 9 VAL D 261 GLY D 266 1 O LEU D 262 N ALA D 202
SHEET 9 DA 9 LYS D 288 TYR D 293 1 O GLU D 289 N MET D 263
SHEET 1 EA 9 ASP E 43 VAL E 47 0
SHEET 2 EA 9 VAL E 54 SER E 63 -1 O VAL E 56 N VAL E 47
SHEET 3 EA 9 ALA E 67 PRO E 76 -1 O ALA E 67 N SER E 63
SHEET 4 EA 9 ALA E 111 MET E 115 -1 O THR E 112 N ALA E 74
SHEET 5 EA 9 HIS E 82 TYR E 88 1 O PRO E 83 N ALA E 111
SHEET 6 EA 9 VAL E 170 GLY E 180 1 N ASP E 171 O HIS E 82
SHEET 7 EA 9 ALA E 199 ASP E 203 1 O ALA E 199 N VAL E 177
SHEET 8 EA 9 VAL E 261 GLY E 266 1 O LEU E 262 N ALA E 202
SHEET 9 EA 9 LYS E 288 TYR E 293 1 O GLU E 289 N MET E 263
SHEET 1 FA 9 ASP F 43 VAL F 47 0
SHEET 2 FA 9 VAL F 54 LYS F 62 -1 O VAL F 56 N VAL F 47
SHEET 3 FA 9 ARG F 68 PRO F 76 -1 O ILE F 69 N TYR F 61
SHEET 4 FA 9 ALA F 111 MET F 115 -1 O THR F 112 N ALA F 74
SHEET 5 FA 9 HIS F 82 TYR F 88 1 O PRO F 83 N ALA F 111
SHEET 6 FA 9 VAL F 170 GLY F 180 1 N ASP F 171 O HIS F 82
SHEET 7 FA 9 ALA F 199 ASP F 203 1 O ALA F 199 N VAL F 177
SHEET 8 FA 9 VAL F 261 GLY F 266 1 O LEU F 262 N ALA F 202
SHEET 9 FA 9 LYS F 288 TYR F 293 1 O GLU F 289 N MET F 263
SHEET 1 GA 9 ASP G 43 VAL G 47 0
SHEET 2 GA 9 VAL G 54 SER G 63 -1 O VAL G 56 N VAL G 47
SHEET 3 GA 9 ALA G 67 PRO G 76 -1 O ALA G 67 N SER G 63
SHEET 4 GA 9 ALA G 111 MET G 115 -1 O THR G 112 N ALA G 74
SHEET 5 GA 9 HIS G 82 TYR G 88 1 O PRO G 83 N ALA G 111
SHEET 6 GA 9 VAL G 170 GLY G 180 1 N ASP G 171 O HIS G 82
SHEET 7 GA 9 ALA G 199 ASP G 203 1 O ALA G 199 N VAL G 177
SHEET 8 GA 9 VAL G 261 GLY G 266 1 O LEU G 262 N ALA G 202
SHEET 9 GA 9 LYS G 288 TYR G 293 1 O GLU G 289 N MET G 263
SHEET 1 HA 9 ASP H 43 VAL H 47 0
SHEET 2 HA 9 VAL H 54 SER H 63 -1 O VAL H 56 N VAL H 47
SHEET 3 HA 9 ALA H 67 PRO H 76 -1 O ALA H 67 N SER H 63
SHEET 4 HA 9 ALA H 111 MET H 115 -1 O THR H 112 N ALA H 74
SHEET 5 HA 9 HIS H 82 TYR H 88 1 O PRO H 83 N ALA H 111
SHEET 6 HA 9 VAL H 170 GLY H 180 1 N ASP H 171 O HIS H 82
SHEET 7 HA 9 ALA H 199 ASP H 203 1 O ALA H 199 N VAL H 177
SHEET 8 HA 9 VAL H 261 GLY H 266 1 O LEU H 262 N ALA H 202
SHEET 9 HA 9 LYS H 288 TYR H 293 1 O GLU H 289 N MET H 263
LINK MG MG A1319 O HOH Z 105 1555 1555
LINK MG MG A1319 O HOH Z 197 1555 1555
LINK MG MG A1319 O HOH Z 200 1555 1555
LINK MG MG A1319 O HOH Z 201 1555 1555
LINK MG MG A1320 O HOH Z 36 1555 1555
LINK MG MG A1320 O HOH W 79 1555 1555
LINK MG MG A1320 O HOH Z 35 1555 1555
LINK MG MG A1320 O HOH Z 84 1555 1555
LINK MG MG A1320 O HOH Z 88 1555 1555
LINK MG MG A1320 O HOH W 83 1555 1555
CISPEP 1 GLY A 80 PRO A 81 0 -4.09
CISPEP 2 GLU A 220 PRO A 221 0 0.39
CISPEP 3 GLY B 80 PRO B 81 0 6.30
CISPEP 4 GLU B 220 PRO B 221 0 0.95
CISPEP 5 GLY C 80 PRO C 81 0 -4.16
CISPEP 6 GLU C 220 PRO C 221 0 -0.74
CISPEP 7 GLY D 80 PRO D 81 0 -2.25
CISPEP 8 GLU D 220 PRO D 221 0 3.33
CISPEP 9 GLY E 80 PRO E 81 0 -0.22
CISPEP 10 GLU E 220 PRO E 221 0 1.17
CISPEP 11 GLY F 80 PRO F 81 0 2.27
CISPEP 12 GLU F 220 PRO F 221 0 0.89
CISPEP 13 GLY G 80 PRO G 81 0 1.36
CISPEP 14 GLU G 220 PRO G 221 0 -1.14
CISPEP 15 GLY H 80 PRO H 81 0 -4.42
CISPEP 16 GLU H 220 PRO H 221 0 1.81
SITE 1 AC1 6 SER B 129 PRO B 130 HIS B 131 GLY B 132
SITE 2 AC1 6 HIS B 133 GLY B 141
SITE 1 AC2 6 SER F 129 PRO F 130 HIS F 131 GLY F 132
SITE 2 AC2 6 HIS F 133 GLY F 141
SITE 1 AC3 6 SER D 129 PRO D 130 HIS D 131 GLY D 132
SITE 2 AC3 6 HIS D 133 GLY D 141
SITE 1 AC4 6 SER C 129 PRO C 130 HIS C 131 GLY C 132
SITE 2 AC4 6 HIS C 133 GLY C 141
SITE 1 AC5 6 SER A 129 PRO A 130 HIS A 131 GLY A 132
SITE 2 AC5 6 HIS A 133 GLY A 141
SITE 1 AC6 6 SER H 129 PRO H 130 HIS H 131 GLY H 132
SITE 2 AC6 6 HIS H 133 GLY H 141
SITE 1 AC7 6 SER E 129 PRO E 130 HIS E 131 GLY E 132
SITE 2 AC7 6 HIS E 133 GLY E 141
SITE 1 AC8 6 SER G 129 PRO G 130 HIS G 131 GLY G 132
SITE 2 AC8 6 HIS G 133 GLY G 141
SITE 1 AC9 4 HOH Z 105 HOH Z 197 HOH Z 200 HOH Z 201
SITE 1 BC1 6 HOH W 79 HOH W 83 HOH Z 35 HOH Z 36
SITE 2 BC1 6 HOH Z 84 HOH Z 88
CRYST1 315.215 315.215 68.483 90.00 90.00 120.00 H 3 72
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 0.003172 0.001832 0.000000 0.00000
SCALE2 0.000000 0.003663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014602 0.00000
MTRIX1 1 0.992000 0.127000 0.008000 -10.29182 1
MTRIX2 1 0.127000 -0.992000 -0.003000 161.16939 1
MTRIX3 1 0.007000 0.004000 -1.000000 -1.11268 1
MTRIX1 2 -0.573000 0.816000 -0.075000 0.98422 1
MTRIX2 2 -0.816000 -0.559000 0.149000 2.34728 1
MTRIX3 2 0.080000 0.146000 0.986000 -0.01626 1
MTRIX1 3 -0.467000 -0.881000 0.074000 2.42255 1
MTRIX2 3 -0.879000 0.453000 -0.151000 1.48908 1
MTRIX3 3 0.100000 -0.135000 -0.986000 0.13497 1
MTRIX1 4 -0.529530 0.844740 0.077550 84.68312 1
MTRIX2 4 0.831680 0.534990 -0.148640 -134.53432 1
MTRIX3 4 -0.167050 -0.014210 -0.985850 51.24715 1
MTRIX1 5 -0.419620 -0.904510 -0.076050 226.47522 1
MTRIX2 5 0.891550 -0.426440 0.152590 -56.56386 1
MTRIX3 5 -0.170450 -0.003770 0.985360 50.60589 1
MTRIX1 6 0.993280 0.090950 -0.071630 -86.64191 1
MTRIX2 6 -0.079020 0.984810 0.154600 -32.08704 1
MTRIX3 6 0.084610 -0.147900 0.985380 23.30945 1
MTRIX1 7 0.995860 0.039730 0.081720 -82.40652 1
MTRIX2 7 0.051760 -0.987200 -0.150860 126.90166 1
MTRIX3 7 0.074680 0.154460 -0.985170 -2.06212 1
TER 2543 LYS A 317
TER 5083 LYS B 317
TER 7620 LYS C 317
TER 10164 LYS D 317
TER 12700 LYS E 317
TER 15232 LYS F 317
TER 17766 LYS G 317
TER 20309 LYS H 317
MASTER 465 0 10 112 72 0 19 2722366 8 12 200
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