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HEADER HYDROLASE 27-JUL-23 8K7P
TITLE STAPHYLOCOCCUS AUREUS LIPASE -PSA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: E68Q WAS GENETIC VARIANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: LIP, BN1321_80040;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KITADOKORO,S.KAMITANI,K.KITADOKORO
REVDAT 1 05-JUN-24 8K7P 0
JRNL AUTH J.KITADOKORO,S.KAMITANI,Y.OKUNO,T.HIKIMA,M.YAMAMOTO,
JRNL AUTH 2 T.HIROKAWA,K.KITADOKORO
JRNL TITL CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS LIPASE COMPLEX
JRNL TITL 2 WITH UNSATURATED PETROSELINIC ACID.
JRNL REF FEBS OPEN BIO 2024
JRNL REFN ESSN 2211-5463
JRNL PMID 38757397
JRNL DOI 10.1002/2211-5463.13808
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0419
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 108410
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5706
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7862
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3880
REMARK 3 BIN FREE R VALUE SET COUNT : 414
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6048
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 209
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.36000
REMARK 3 B22 (A**2) : 1.36000
REMARK 3 B33 (A**2) : -2.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.691
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6384 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8585 ; 1.744 ; 1.670
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 762 ; 6.272 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 32 ;10.614 ; 5.312
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 996 ;18.499 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 878 ; 0.153 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4962 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3063 ; 5.188 ; 5.949
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3818 ; 6.705 ;10.652
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3321 ; 8.371 ; 6.317
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9543 ;10.870 ;62.220
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 8K7P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1300039359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : M
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 217650
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.69
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, ACETATE, PH 4.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 124.31800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.15900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 186.47700
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 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 124.31800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 186.47700
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 62.15900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -13
REMARK 465 ASN A -12
REMARK 465 HIS A -11
REMARK 465 LYS A -10
REMARK 465 VAL A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 LYS A -1
REMARK 465 ALA A 0
REMARK 465 ASN A 1
REMARK 465 GLN A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 386
REMARK 465 LYS A 387
REMARK 465 GLY A 388
REMARK 465 THR A 389
REMARK 465 GLN A 390
REMARK 465 LEU A 391
REMARK 465 LYS A 392
REMARK 465 ALA A 393
REMARK 465 SER A 394
REMARK 465 MET B -13
REMARK 465 ASN B -12
REMARK 465 HIS B -11
REMARK 465 LYS B -10
REMARK 465 VAL B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 LYS B -1
REMARK 465 ALA B 0
REMARK 465 ASN B 1
REMARK 465 GLN B 2
REMARK 465 VAL B 3
REMARK 465 GLY B 386
REMARK 465 LYS B 387
REMARK 465 GLY B 388
REMARK 465 THR B 389
REMARK 465 GLN B 390
REMARK 465 LEU B 391
REMARK 465 LYS B 392
REMARK 465 ALA B 393
REMARK 465 SER B 394
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 OG SER A 116 C6 4I1 A 406 2.10
REMARK 500 OG SER A 116 C7 4I1 A 406 2.12
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 THR A 152 CA - CB - OG1 ANGL. DEV. = -12.8 DEGREES
REMARK 500 ARG B 225 CB - CG - CD ANGL. DEV. = -17.1 DEGREES
REMARK 500 ARG B 225 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 225 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 335 CB - CG - CD ANGL. DEV. = 21.0 DEGREES
REMARK 500 ARG B 335 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 335 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 18 -13.14 79.70
REMARK 500 TYR A 29 146.27 -171.91
REMARK 500 SER A 116 -126.96 56.89
REMARK 500 PHE A 178 -67.93 -148.03
REMARK 500 SER A 269 26.15 -144.40
REMARK 500 LEU A 275 -16.77 89.62
REMARK 500 VAL A 309 -12.40 -142.08
REMARK 500 ALA A 332 66.57 -109.76
REMARK 500 LEU B 18 -15.53 79.36
REMARK 500 TYR B 29 143.86 -171.45
REMARK 500 SER B 116 -121.28 51.36
REMARK 500 PHE B 178 -67.57 -147.69
REMARK 500 SER B 269 25.45 -146.82
REMARK 500 VAL B 309 -8.50 -141.83
REMARK 500 ALA B 332 63.01 -101.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 225 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 415 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 23 O
REMARK 620 2 HOH A 529 O 56.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 416 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD1
REMARK 620 2 ASP A 236 OD2 128.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 417 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 283 O
REMARK 620 2 ASP A 348 OD2 88.4
REMARK 620 3 ASP A 351 OD1 160.8 102.9
REMARK 620 4 ASP A 351 OD2 145.8 87.7 51.6
REMARK 620 5 ASP A 356 OD2 80.8 85.4 84.7 132.6
REMARK 620 6 ASP A 359 OD2 78.6 165.0 91.6 98.8 99.8
REMARK 620 7 HOH A 539 O 74.0 82.2 122.4 71.8 152.1 87.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 417 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 64 OD1
REMARK 620 2 ASP B 64 OD2 54.3
REMARK 620 3 ASP B 236 OD2 130.9 92.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 418 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 283 O
REMARK 620 2 ASP B 348 OD2 87.9
REMARK 620 3 ASP B 351 OD1 159.3 100.8
REMARK 620 4 ASP B 351 OD2 149.4 86.0 50.9
REMARK 620 5 ASP B 356 OD2 79.9 84.3 82.3 129.0
REMARK 620 6 ASP B 359 OD2 80.3 166.3 92.6 100.8 100.2
REMARK 620 7 HOH B 518 O 78.2 83.1 121.2 71.3 155.0 87.8
REMARK 620 N 1 2 3 4 5 6
DBREF1 8K7P A -1 394 UNP A0A0U1MWF9_STAAU
DBREF2 8K7P A A0A0U1MWF9 295 690
DBREF1 8K7P B -1 394 UNP A0A0U1MWF9_STAAU
DBREF2 8K7P B A0A0U1MWF9 295 690
SEQADV 8K7P MET A -13 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P ASN A -12 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS A -11 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P LYS A -10 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P VAL A -9 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS A -8 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS A -7 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS A -6 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS A -5 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS A -4 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS A -3 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P MET A -2 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P GLN A 68 UNP A0A0U1MWF GLU 364 CONFLICT
SEQADV 8K7P MET B -13 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P ASN B -12 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS B -11 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P LYS B -10 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P VAL B -9 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS B -8 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS B -7 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS B -6 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS B -5 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS B -4 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P HIS B -3 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P MET B -2 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 8K7P GLN B 68 UNP A0A0U1MWF GLU 364 CONFLICT
SEQRES 1 A 408 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET LYS
SEQRES 2 A 408 ALA ASN GLN VAL GLN PRO LEU ASN LYS TYR PRO VAL VAL
SEQRES 3 A 408 PHE VAL HIS GLY PHE LEU GLY LEU VAL GLY ASP ASN ALA
SEQRES 4 A 408 PRO ALA LEU TYR PRO ASN TYR TRP GLY GLY ASN LYS PHE
SEQRES 5 A 408 LYS VAL ILE GLU GLU LEU ARG LYS GLN GLY TYR ASN VAL
SEQRES 6 A 408 HIS GLN ALA SER VAL SER ALA PHE GLY SER ASN TYR ASP
SEQRES 7 A 408 ARG ALA VAL GLN LEU TYR TYR TYR ILE LYS GLY GLY ARG
SEQRES 8 A 408 VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS TYR GLY HIS
SEQRES 9 A 408 GLU ARG TYR GLY LYS THR TYR LYS GLY ILE MET PRO ASN
SEQRES 10 A 408 TRP GLU PRO GLY LYS LYS VAL HIS LEU VAL GLY HIS SER
SEQRES 11 A 408 MET GLY GLY GLN THR ILE ARG LEU MET GLU GLU PHE LEU
SEQRES 12 A 408 ARG ASN GLY ASN LYS GLU GLU ILE ALA TYR HIS GLN ALA
SEQRES 13 A 408 HIS GLY GLY GLU ILE SER PRO LEU PHE THR GLY GLY HIS
SEQRES 14 A 408 ASN ASN MET VAL ALA SER ILE THR THR LEU ALA THR PRO
SEQRES 15 A 408 HIS ASN GLY SER GLN ALA ALA ASP LYS PHE GLY ASN THR
SEQRES 16 A 408 GLU ALA VAL ARG LYS ILE MET PHE ALA LEU ASN ARG PHE
SEQRES 17 A 408 MET GLY ASN LYS TYR SER ASN ILE ASP LEU GLY LEU THR
SEQRES 18 A 408 GLN TRP GLY PHE LYS GLN LEU PRO ASN GLU SER TYR ILE
SEQRES 19 A 408 ASP TYR ILE LYS ARG VAL SER LYS SER LYS ILE TRP THR
SEQRES 20 A 408 SER ASP ASP ASN ALA ALA TYR ASP LEU THR LEU ASP GLY
SEQRES 21 A 408 SER ALA LYS LEU ASN ASN MET THR SER MET ASN PRO ASN
SEQRES 22 A 408 ILE THR TYR THR THR TYR THR GLY VAL SER SER HIS THR
SEQRES 23 A 408 GLY PRO LEU GLY TYR GLU ASN PRO ASP LEU GLY THR PHE
SEQRES 24 A 408 PHE LEU MET ASP THR THR SER ARG ILE ILE GLY HIS ASP
SEQRES 25 A 408 ALA ARG GLU GLU TRP ARG LYS ASN ASP GLY VAL VAL PRO
SEQRES 26 A 408 VAL ILE SER SER LEU HIS PRO SER ASN GLN PRO PHE VAL
SEQRES 27 A 408 ASN VAL THR ASN ASN GLU PRO ALA THR ARG ARG GLY ILE
SEQRES 28 A 408 TRP GLN VAL LYS PRO ILE LEU GLN GLY TRP ASP HIS VAL
SEQRES 29 A 408 ASP PHE ILE GLY VAL ASP PHE LEU ASP PHE LYS ARG LYS
SEQRES 30 A 408 GLY SER GLU LEU ALA ASN PHE TYR ILE GLY ILE ILE ASN
SEQRES 31 A 408 ASP LEU LEU SER VAL GLU ALA THR GLU GLY LYS GLY THR
SEQRES 32 A 408 GLN LEU LYS ALA SER
SEQRES 1 B 408 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET LYS
SEQRES 2 B 408 ALA ASN GLN VAL GLN PRO LEU ASN LYS TYR PRO VAL VAL
SEQRES 3 B 408 PHE VAL HIS GLY PHE LEU GLY LEU VAL GLY ASP ASN ALA
SEQRES 4 B 408 PRO ALA LEU TYR PRO ASN TYR TRP GLY GLY ASN LYS PHE
SEQRES 5 B 408 LYS VAL ILE GLU GLU LEU ARG LYS GLN GLY TYR ASN VAL
SEQRES 6 B 408 HIS GLN ALA SER VAL SER ALA PHE GLY SER ASN TYR ASP
SEQRES 7 B 408 ARG ALA VAL GLN LEU TYR TYR TYR ILE LYS GLY GLY ARG
SEQRES 8 B 408 VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS TYR GLY HIS
SEQRES 9 B 408 GLU ARG TYR GLY LYS THR TYR LYS GLY ILE MET PRO ASN
SEQRES 10 B 408 TRP GLU PRO GLY LYS LYS VAL HIS LEU VAL GLY HIS SER
SEQRES 11 B 408 MET GLY GLY GLN THR ILE ARG LEU MET GLU GLU PHE LEU
SEQRES 12 B 408 ARG ASN GLY ASN LYS GLU GLU ILE ALA TYR HIS GLN ALA
SEQRES 13 B 408 HIS GLY GLY GLU ILE SER PRO LEU PHE THR GLY GLY HIS
SEQRES 14 B 408 ASN ASN MET VAL ALA SER ILE THR THR LEU ALA THR PRO
SEQRES 15 B 408 HIS ASN GLY SER GLN ALA ALA ASP LYS PHE GLY ASN THR
SEQRES 16 B 408 GLU ALA VAL ARG LYS ILE MET PHE ALA LEU ASN ARG PHE
SEQRES 17 B 408 MET GLY ASN LYS TYR SER ASN ILE ASP LEU GLY LEU THR
SEQRES 18 B 408 GLN TRP GLY PHE LYS GLN LEU PRO ASN GLU SER TYR ILE
SEQRES 19 B 408 ASP TYR ILE LYS ARG VAL SER LYS SER LYS ILE TRP THR
SEQRES 20 B 408 SER ASP ASP ASN ALA ALA TYR ASP LEU THR LEU ASP GLY
SEQRES 21 B 408 SER ALA LYS LEU ASN ASN MET THR SER MET ASN PRO ASN
SEQRES 22 B 408 ILE THR TYR THR THR TYR THR GLY VAL SER SER HIS THR
SEQRES 23 B 408 GLY PRO LEU GLY TYR GLU ASN PRO ASP LEU GLY THR PHE
SEQRES 24 B 408 PHE LEU MET ASP THR THR SER ARG ILE ILE GLY HIS ASP
SEQRES 25 B 408 ALA ARG GLU GLU TRP ARG LYS ASN ASP GLY VAL VAL PRO
SEQRES 26 B 408 VAL ILE SER SER LEU HIS PRO SER ASN GLN PRO PHE VAL
SEQRES 27 B 408 ASN VAL THR ASN ASN GLU PRO ALA THR ARG ARG GLY ILE
SEQRES 28 B 408 TRP GLN VAL LYS PRO ILE LEU GLN GLY TRP ASP HIS VAL
SEQRES 29 B 408 ASP PHE ILE GLY VAL ASP PHE LEU ASP PHE LYS ARG LYS
SEQRES 30 B 408 GLY SER GLU LEU ALA ASN PHE TYR ILE GLY ILE ILE ASN
SEQRES 31 B 408 ASP LEU LEU SER VAL GLU ALA THR GLU GLY LYS GLY THR
SEQRES 32 B 408 GLN LEU LYS ALA SER
HET FMT A 401 3
HET OCA A 402 10
HET OCA A 403 10
HET PPI A 404 5
HET ACY A 405 4
HET 4I1 A 406 20
HET DAO A 407 14
HET 6NA A 408 8
HET FMT A 409 3
HET FMT A 410 3
HET FMT A 411 3
HET FMT A 412 3
HET CL A 413 1
HET CL A 414 1
HET MG A 415 1
HET ZN A 416 1
HET CA A 417 1
HET GOL A 418 6
HET 6NA B 401 8
HET FMT B 402 3
HET FMT B 403 3
HET 6NA B 404 8
HET BUA B 405 6
HET OCA B 406 10
HET OCA B 407 10
HET 4I1 B 408 20
HET FMT B 409 3
HET FMT B 410 3
HET FMT B 411 3
HET FMT B 412 3
HET DAO B 413 14
HET 6NA B 414 8
HET CL B 415 1
HET CL B 416 1
HET ZN B 417 1
HET CA B 418 1
HET GOL B 419 6
HETNAM FMT FORMIC ACID
HETNAM OCA OCTANOIC ACID (CAPRYLIC ACID)
HETNAM PPI PROPANOIC ACID
HETNAM ACY ACETIC ACID
HETNAM 4I1 PETROSELINIC ACID
HETNAM DAO LAURIC ACID
HETNAM 6NA HEXANOIC ACID
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM BUA BUTANOIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FMT 11(C H2 O2)
FORMUL 4 OCA 4(C8 H16 O2)
FORMUL 6 PPI C3 H6 O2
FORMUL 7 ACY C2 H4 O2
FORMUL 8 4I1 2(C18 H34 O2)
FORMUL 9 DAO 2(C12 H24 O2)
FORMUL 10 6NA 4(C6 H12 O2)
FORMUL 15 CL 4(CL 1-)
FORMUL 17 MG MG 2+
FORMUL 18 ZN 2(ZN 2+)
FORMUL 19 CA 2(CA 2+)
FORMUL 20 GOL 2(C3 H8 O3)
FORMUL 25 BUA C4 H8 O2
FORMUL 40 HOH *137(H2 O)
HELIX 1 AA1 VAL A 21 ALA A 25 5 5
HELIX 2 AA2 LYS A 39 GLN A 47 1 9
HELIX 3 AA3 SER A 61 GLY A 75 1 15
HELIX 4 AA4 GLY A 81 GLY A 89 1 9
HELIX 5 AA5 SER A 116 GLY A 132 1 17
HELIX 6 AA6 ASN A 133 GLY A 144 1 12
HELIX 7 AA7 SER A 148 THR A 152 5 5
HELIX 8 AA8 SER A 172 LYS A 177 1 6
HELIX 9 AA9 THR A 181 MET A 195 1 15
HELIX 10 AB1 LEU A 206 GLY A 210 5 5
HELIX 11 AB2 SER A 218 SER A 227 1 10
HELIX 12 AB3 LYS A 228 SER A 234 5 7
HELIX 13 AB4 ASN A 237 LEU A 242 1 6
HELIX 14 AB5 THR A 243 MET A 253 1 11
HELIX 15 AB6 PRO A 274 GLY A 276 5 3
HELIX 16 AB7 PHE A 285 LEU A 287 5 3
HELIX 17 AB8 MET A 288 HIS A 297 1 10
HELIX 18 AB9 ARG A 300 ARG A 304 5 5
HELIX 19 AC1 PRO A 311 LEU A 316 1 6
HELIX 20 AC2 VAL A 350 GLY A 354 5 5
HELIX 21 AC3 LYS A 363 THR A 384 1 22
HELIX 22 AC4 VAL B 21 ALA B 25 5 5
HELIX 23 AC5 LYS B 39 GLN B 47 1 9
HELIX 24 AC6 SER B 61 GLY B 75 1 15
HELIX 25 AC7 GLY B 81 GLY B 89 1 9
HELIX 26 AC8 SER B 116 GLY B 132 1 17
HELIX 27 AC9 ASN B 133 GLY B 144 1 12
HELIX 28 AD1 SER B 148 THR B 152 5 5
HELIX 29 AD2 SER B 172 LYS B 177 1 6
HELIX 30 AD3 THR B 181 MET B 195 1 15
HELIX 31 AD4 LEU B 206 GLY B 210 5 5
HELIX 32 AD5 SER B 218 SER B 227 1 10
HELIX 33 AD6 LYS B 228 SER B 234 5 7
HELIX 34 AD7 ASN B 237 LEU B 242 1 6
HELIX 35 AD8 THR B 243 MET B 253 1 11
HELIX 36 AD9 PHE B 285 LEU B 287 5 3
HELIX 37 AE1 MET B 288 HIS B 297 1 10
HELIX 38 AE2 ARG B 300 ARG B 304 5 5
HELIX 39 AE3 PRO B 311 LEU B 316 1 6
HELIX 40 AE4 VAL B 350 GLY B 354 5 5
HELIX 41 AE5 LYS B 363 THR B 384 1 22
SHEET 1 AA1 7 VAL A 51 GLN A 53 0
SHEET 2 AA1 7 VAL A 11 VAL A 14 1 N PHE A 13 O HIS A 52
SHEET 3 AA1 7 VAL A 110 HIS A 115 1 O VAL A 113 N VAL A 14
SHEET 4 AA1 7 VAL A 159 LEU A 165 1 O THR A 163 N GLY A 114
SHEET 5 AA1 7 THR A 261 TYR A 265 1 O THR A 261 N ILE A 162
SHEET 6 AA1 7 TRP A 338 VAL A 340 1 O GLN A 339 N TYR A 262
SHEET 7 AA1 7 PHE A 323 ASN A 325 1 N VAL A 324 O TRP A 338
SHEET 1 AA2 2 GLY A 76 ASP A 79 0
SHEET 2 AA2 2 TYR A 93 TYR A 97 -1 O LYS A 95 N VAL A 78
SHEET 1 AA3 2 GLY A 267 VAL A 268 0
SHEET 2 AA3 2 LEU A 344 GLN A 345 1 O LEU A 344 N VAL A 268
SHEET 1 AA4 2 SER A 270 THR A 272 0
SHEET 2 AA4 2 GLU A 278 PRO A 280 -1 O ASN A 279 N HIS A 271
SHEET 1 AA5 7 VAL B 51 GLN B 53 0
SHEET 2 AA5 7 VAL B 11 VAL B 14 1 N PHE B 13 O HIS B 52
SHEET 3 AA5 7 VAL B 110 HIS B 115 1 O VAL B 113 N VAL B 14
SHEET 4 AA5 7 VAL B 159 LEU B 165 1 O THR B 163 N GLY B 114
SHEET 5 AA5 7 THR B 261 TYR B 265 1 O TYR B 265 N THR B 164
SHEET 6 AA5 7 TRP B 338 VAL B 340 1 O GLN B 339 N TYR B 262
SHEET 7 AA5 7 PHE B 323 ASN B 325 1 N VAL B 324 O TRP B 338
SHEET 1 AA6 2 GLY B 76 ASP B 79 0
SHEET 2 AA6 2 TYR B 93 TYR B 97 -1 O LYS B 95 N VAL B 78
SHEET 1 AA7 2 GLY B 267 VAL B 268 0
SHEET 2 AA7 2 LEU B 344 GLN B 345 1 O LEU B 344 N VAL B 268
SHEET 1 AA8 2 SER B 270 THR B 272 0
SHEET 2 AA8 2 GLU B 278 PRO B 280 -1 O ASN B 279 N HIS B 271
LINK O ASP A 23 MG MG A 415 1555 1555 2.97
LINK OD1 ASP A 64 ZN ZN A 416 1555 1555 2.05
LINK OD2 ASP A 236 ZN ZN A 416 1555 1555 1.95
LINK O GLY A 283 CA CA A 417 1555 1555 2.34
LINK OD2 ASP A 348 CA CA A 417 1555 1555 2.35
LINK OD1 ASP A 351 CA CA A 417 1555 1555 2.65
LINK OD2 ASP A 351 CA CA A 417 1555 1555 2.37
LINK OD2 ASP A 356 CA CA A 417 1555 1555 2.42
LINK OD2 ASP A 359 CA CA A 417 1555 1555 2.45
LINK MG MG A 415 O HOH A 529 1555 1555 2.66
LINK CA CA A 417 O HOH A 539 1555 1555 2.60
LINK OD1 ASP B 64 ZN ZN B 417 1555 1555 2.02
LINK OD2 ASP B 64 ZN ZN B 417 1555 1555 2.69
LINK OD2 ASP B 236 ZN ZN B 417 1555 1555 1.99
LINK O GLY B 283 CA CA B 418 1555 1555 2.37
LINK OD2 ASP B 348 CA CA B 418 1555 1555 2.38
LINK OD1 ASP B 351 CA CA B 418 1555 1555 2.73
LINK OD2 ASP B 351 CA CA B 418 1555 1555 2.42
LINK OD2 ASP B 356 CA CA B 418 1555 1555 2.43
LINK OD2 ASP B 359 CA CA B 418 1555 1555 2.38
LINK CA CA B 418 O HOH B 518 1555 1555 2.56
CRYST1 132.324 132.324 248.636 90.00 90.00 90.00 P 41 2 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007557 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004022 0.00000
TER 3025 GLU A 385
TER 6050 GLU B 385
MASTER 442 0 37 41 26 0 0 6 6394 2 228 64
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