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HEADER HYDROLASE 29-JUN-06 2HIH
TITLE CRYSTAL STRUCTURE OF STAPHYLOCOCCUS HYICUS LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 46 KDA FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS HYICUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: LIP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE 3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSHT7
KEYWDS LIPASE, A1 PHOSPHOLIPASE, PHOSPHOLIPID BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.W.TIESINGA,G.VAN POUDEROYEN,M.NARDINI,B.W.DIJKSTRA
REVDAT 1 22-MAY-07 2HIH 0
JRNL AUTH J.J.W.TIESINGA,G.VAN POUDEROYEN,M.NARDINI,
JRNL AUTH 2 B.W.DIJKSTRA
JRNL TITL STRUCTURAL BASIS OF PHOSPHOLIPASE ACTIVITY OF
JRNL TITL 2 STAPHYLOCOCCUS HYICUS LIPASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 22929
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2322
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.86
REMARK 3 BIN RESOLUTION RANGE LOW : 2.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1498
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 165
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : -0.03000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.428
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.266
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.948
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.846
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6302 ; 0.005 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5348 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8526 ; 0.786 ; 1.925
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12512 ; 0.584 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 771 ; 4.783 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 320 ;35.146 ;24.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1045 ;19.114 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;18.157 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 882 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7143 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1305 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1368 ; 0.202 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5376 ; 0.192 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3027 ; 0.190 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 3573 ; 0.088 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 279 ; 0.216 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 10 ; 0.130 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 5 ; 0.172 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 24 ; 0.231 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.126 ; 0.500
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): 3912 ; 0.164 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1606 ; 0.030 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6103 ; 0.286 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2756 ; 0.355 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2423 ; 0.582 ; 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 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 29 A 35 4
REMARK 3 1 B 29 B 35 4
REMARK 3 2 A 7 A 11 4
REMARK 3 2 B 7 B 11 4
REMARK 3 3 A 40 A 84 4
REMARK 3 3 B 40 B 84 4
REMARK 3 4 A 201 A 221 4
REMARK 3 4 B 201 B 221 4
REMARK 3 5 A 283 A 326 4
REMARK 3 5 B 283 B 326 4
REMARK 3 6 A 329 A 337 4
REMARK 3 6 B 329 B 337 4
REMARK 3 7 A 368 A 392 4
REMARK 3 7 B 368 B 392 4
REMARK 3 8 A 14 A 25 4
REMARK 3 8 B 14 B 25 4
REMARK 3 9 A 86 A 198 4
REMARK 3 9 B 86 B 198 4
REMARK 3 10 A 223 A 258 4
REMARK 3 10 B 223 B 258 4
REMARK 3 11 A 339 A 366 4
REMARK 3 11 B 339 B 366 4
REMARK 3 12 A 260 A 278 4
REMARK 3 12 B 260 B 278 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 5415 ; 0.180 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 5415 ; 0.140 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2HIH COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-2006.
REMARK 100 THE RCSB ID CODE IS RCSB038382.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-1994
REMARK 200 TEMPERATURE (KELVIN) : 277.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22929
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.860
REMARK 200 RESOLUTION RANGE LOW (A) : 26.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: AMORE
REMARK 200 STARTING MODEL: 1JI3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, NA SUCCINATE, DMSO,
REMARK 280 ISOPROPANOL, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.65500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.90500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.98000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.90500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.65500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.98000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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
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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -34
REMARK 465 ALA A -33
REMARK 465 ARG A -32
REMARK 465 ILE A -31
REMARK 465 ARG A -30
REMARK 465 ALA A -29
REMARK 465 ARG A -28
REMARK 465 GLY A -27
REMARK 465 SER A -26
REMARK 465 SER A -25
REMARK 465 ARG A -24
REMARK 465 VAL A -23
REMARK 465 ASP A -22
REMARK 465 VAL A -21
REMARK 465 PRO A -20
REMARK 465 LYS A -19
REMARK 465 GLU A -18
REMARK 465 ASN A -17
REMARK 465 THR A -16
REMARK 465 THR A -15
REMARK 465 ALA A -14
REMARK 465 GLN A -13
REMARK 465 ASN A -12
REMARK 465 LYS A -11
REMARK 465 PHE A -10
REMARK 465 THR A -9
REMARK 465 SER A -8
REMARK 465 GLN A -7
REMARK 465 ALA A -6
REMARK 465 SER A -5
REMARK 465 ASP A -4
REMARK 465 LYS A -3
REMARK 465 LYS A -2
REMARK 465 PRO A -1
REMARK 465 THR A 0
REMARK 465 VAL A 1
REMARK 465 LYS A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 PRO A 5
REMARK 465 GLU A 6
REMARK 465 LYS A 394
REMARK 465 ASN A 395
REMARK 465 ALA A 396
REMARK 465 MET B -34
REMARK 465 ALA B -33
REMARK 465 ARG B -32
REMARK 465 ILE B -31
REMARK 465 ARG B -30
REMARK 465 ALA B -29
REMARK 465 ARG B -28
REMARK 465 GLY B -27
REMARK 465 SER B -26
REMARK 465 SER B -25
REMARK 465 ARG B -24
REMARK 465 VAL B -23
REMARK 465 ASP B -22
REMARK 465 VAL B -21
REMARK 465 PRO B -20
REMARK 465 LYS B -19
REMARK 465 GLU B -18
REMARK 465 ASN B -17
REMARK 465 THR B -16
REMARK 465 THR B -15
REMARK 465 ALA B -14
REMARK 465 GLN B -13
REMARK 465 ASN B -12
REMARK 465 LYS B -11
REMARK 465 PHE B -10
REMARK 465 THR B -9
REMARK 465 SER B -8
REMARK 465 GLN B -7
REMARK 465 ALA B -6
REMARK 465 SER B -5
REMARK 465 ASP B -4
REMARK 465 LYS B -3
REMARK 465 LYS B -2
REMARK 465 PRO B -1
REMARK 465 THR B 0
REMARK 465 VAL B 1
REMARK 465 LYS B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 PRO B 5
REMARK 465 GLU B 6
REMARK 465 THR B 393
REMARK 465 LYS B 394
REMARK 465 ASN B 395
REMARK 465 ALA B 396
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 VAL A 8 CA VAL A 8 CB 0.035
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 THR A 189 N - CA - C ANGL. DEV. = -4.7 DEGREES
REMARK 500 LEU A 289 N - CA - C ANGL. DEV. = -5.1 DEGREES
REMARK 500 GLY B 28 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 LEU B 52 CA - CB - CG ANGL. DEV. = 5.1 DEGREES
REMARK 500 TYR B 272 N - CA - C ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP B 307 N - CA - C ANGL. DEV. = -4.8 DEGREES
REMARK 500 PRO B 348 C - N - CA ANGL. DEV. = -5.4 DEGREES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DEPOSITORS BELIEVE THAT THE RESIDUE TYR 40 IS
REMARK 999 CORRECT AND THAT SWISSPROT IS INCORRECT AT THIS POSITION
DBREF 2HIH A -23 396 UNP P04635 LIP_STAHY 222 641
DBREF 2HIH B -23 396 UNP P04635 LIP_STAHY 222 641
SEQADV 2HIH MET A -34 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ALA A -33 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG A -32 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ILE A -31 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG A -30 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ALA A -29 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG A -28 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH GLY A -27 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH SER A -26 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH SER A -25 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG A -24 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH TYR A 40 UNP P04635 HIS 285 SEE REMARK 999
SEQADV 2HIH MET B -34 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ALA B -33 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG B -32 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ILE B -31 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG B -30 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ALA B -29 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG B -28 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH GLY B -27 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH SER B -26 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH SER B -25 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH ARG B -24 UNP P04635 CLONING ARTIFACT
SEQADV 2HIH TYR B 40 UNP P04635 HIS 285 SEE REMARK 999
SEQRES 1 A 431 MET ALA ARG ILE ARG ALA ARG GLY SER SER ARG VAL ASP
SEQRES 2 A 431 VAL PRO LYS GLU ASN THR THR ALA GLN ASN LYS PHE THR
SEQRES 3 A 431 SER GLN ALA SER ASP LYS LYS PRO THR VAL LYS ALA ALA
SEQRES 4 A 431 PRO GLU ALA VAL GLN ASN PRO GLU ASN PRO LYS ASN LYS
SEQRES 5 A 431 ASP PRO PHE VAL PHE VAL HIS GLY PHE THR GLY PHE VAL
SEQRES 6 A 431 GLY GLU VAL ALA ALA LYS GLY GLU ASN TYR TRP GLY GLY
SEQRES 7 A 431 THR LYS ALA ASN LEU ARG ASN HIS LEU ARG LYS ALA GLY
SEQRES 8 A 431 TYR GLU THR TYR GLU ALA SER VAL SER ALA LEU ALA SER
SEQRES 9 A 431 ASN HIS GLU ARG ALA VAL GLU LEU TYR TYR TYR LEU LYS
SEQRES 10 A 431 GLY GLY ARG VAL ASP TYR GLY ALA ALA HIS SER GLU LYS
SEQRES 11 A 431 TYR GLY HIS GLU ARG TYR GLY LYS THR TYR GLU GLY VAL
SEQRES 12 A 431 LEU LYS ASP TRP LYS PRO GLY HIS PRO VAL HIS PHE ILE
SEQRES 13 A 431 GLY HIS SER MET GLY GLY GLN THR ILE ARG LEU LEU GLU
SEQRES 14 A 431 HIS TYR LEU ARG PHE GLY ASP LYS ALA GLU ILE ALA TYR
SEQRES 15 A 431 GLN GLN GLN HIS GLY GLY ILE ILE SER GLU LEU PHE LYS
SEQRES 16 A 431 GLY GLY GLN ASP ASN MET VAL THR SER ILE THR THR ILE
SEQRES 17 A 431 ALA THR PRO HIS ASN GLY THR HIS ALA SER ASP ASP ILE
SEQRES 18 A 431 GLY ASN THR PRO THR ILE ARG ASN ILE LEU TYR SER PHE
SEQRES 19 A 431 ALA GLN MET SER SER HIS LEU GLY THR ILE ASP PHE GLY
SEQRES 20 A 431 MET ASP HIS TRP GLY PHE LYS ARG LYS ASP GLY GLU SER
SEQRES 21 A 431 LEU THR ASP TYR ASN LYS ARG ILE ALA GLU SER LYS ILE
SEQRES 22 A 431 TRP ASP SER GLU ASP THR GLY LEU TYR ASP LEU THR ARG
SEQRES 23 A 431 GLU GLY ALA GLU LYS ILE ASN GLN LYS THR GLU LEU ASN
SEQRES 24 A 431 PRO ASN ILE TYR TYR LYS THR TYR THR GLY VAL ALA THR
SEQRES 25 A 431 HIS GLU THR GLN LEU GLY LYS HIS ILE ALA ASP LEU GLY
SEQRES 26 A 431 MET GLU PHE THR LYS ILE LEU THR GLY ASN TYR ILE GLY
SEQRES 27 A 431 SER VAL ASP ASP ILE LEU TRP ARG PRO ASN ASP GLY LEU
SEQRES 28 A 431 VAL SER GLU ILE SER SER GLN HIS PRO SER ASP GLU LYS
SEQRES 29 A 431 ASN ILE SER VAL ASP GLU ASN SER GLU LEU HIS LYS GLY
SEQRES 30 A 431 THR TRP GLN VAL MET PRO THR MET LYS GLY TRP ASP HIS
SEQRES 31 A 431 SER ASP PHE ILE GLY ASN ASP ALA LEU ASP THR LYS HIS
SEQRES 32 A 431 SER ALA ILE GLU LEU THR ASN PHE TYR HIS SER ILE SER
SEQRES 33 A 431 ASP TYR LEU MET ARG ILE GLU LYS ALA GLU SER THR LYS
SEQRES 34 A 431 ASN ALA
SEQRES 1 B 431 MET ALA ARG ILE ARG ALA ARG GLY SER SER ARG VAL ASP
SEQRES 2 B 431 VAL PRO LYS GLU ASN THR THR ALA GLN ASN LYS PHE THR
SEQRES 3 B 431 SER GLN ALA SER ASP LYS LYS PRO THR VAL LYS ALA ALA
SEQRES 4 B 431 PRO GLU ALA VAL GLN ASN PRO GLU ASN PRO LYS ASN LYS
SEQRES 5 B 431 ASP PRO PHE VAL PHE VAL HIS GLY PHE THR GLY PHE VAL
SEQRES 6 B 431 GLY GLU VAL ALA ALA LYS GLY GLU ASN TYR TRP GLY GLY
SEQRES 7 B 431 THR LYS ALA ASN LEU ARG ASN HIS LEU ARG LYS ALA GLY
SEQRES 8 B 431 TYR GLU THR TYR GLU ALA SER VAL SER ALA LEU ALA SER
SEQRES 9 B 431 ASN HIS GLU ARG ALA VAL GLU LEU TYR TYR TYR LEU LYS
SEQRES 10 B 431 GLY GLY ARG VAL ASP TYR GLY ALA ALA HIS SER GLU LYS
SEQRES 11 B 431 TYR GLY HIS GLU ARG TYR GLY LYS THR TYR GLU GLY VAL
SEQRES 12 B 431 LEU LYS ASP TRP LYS PRO GLY HIS PRO VAL HIS PHE ILE
SEQRES 13 B 431 GLY HIS SER MET GLY GLY GLN THR ILE ARG LEU LEU GLU
SEQRES 14 B 431 HIS TYR LEU ARG PHE GLY ASP LYS ALA GLU ILE ALA TYR
SEQRES 15 B 431 GLN GLN GLN HIS GLY GLY ILE ILE SER GLU LEU PHE LYS
SEQRES 16 B 431 GLY GLY GLN ASP ASN MET VAL THR SER ILE THR THR ILE
SEQRES 17 B 431 ALA THR PRO HIS ASN GLY THR HIS ALA SER ASP ASP ILE
SEQRES 18 B 431 GLY ASN THR PRO THR ILE ARG ASN ILE LEU TYR SER PHE
SEQRES 19 B 431 ALA GLN MET SER SER HIS LEU GLY THR ILE ASP PHE GLY
SEQRES 20 B 431 MET ASP HIS TRP GLY PHE LYS ARG LYS ASP GLY GLU SER
SEQRES 21 B 431 LEU THR ASP TYR ASN LYS ARG ILE ALA GLU SER LYS ILE
SEQRES 22 B 431 TRP ASP SER GLU ASP THR GLY LEU TYR ASP LEU THR ARG
SEQRES 23 B 431 GLU GLY ALA GLU LYS ILE ASN GLN LYS THR GLU LEU ASN
SEQRES 24 B 431 PRO ASN ILE TYR TYR LYS THR TYR THR GLY VAL ALA THR
SEQRES 25 B 431 HIS GLU THR GLN LEU GLY LYS HIS ILE ALA ASP LEU GLY
SEQRES 26 B 431 MET GLU PHE THR LYS ILE LEU THR GLY ASN TYR ILE GLY
SEQRES 27 B 431 SER VAL ASP ASP ILE LEU TRP ARG PRO ASN ASP GLY LEU
SEQRES 28 B 431 VAL SER GLU ILE SER SER GLN HIS PRO SER ASP GLU LYS
SEQRES 29 B 431 ASN ILE SER VAL ASP GLU ASN SER GLU LEU HIS LYS GLY
SEQRES 30 B 431 THR TRP GLN VAL MET PRO THR MET LYS GLY TRP ASP HIS
SEQRES 31 B 431 SER ASP PHE ILE GLY ASN ASP ALA LEU ASP THR LYS HIS
SEQRES 32 B 431 SER ALA ILE GLU LEU THR ASN PHE TYR HIS SER ILE SER
SEQRES 33 B 431 ASP TYR LEU MET ARG ILE GLU LYS ALA GLU SER THR LYS
SEQRES 34 B 431 ASN ALA
HET ZN 601 1
HET CA 603 1
HET ZN 1601 1
HET CA 1603 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN1 2+)
FORMUL 4 CA 2(CA1 2+)
FORMUL 7 HOH *26(H2 O1)
HELIX 1 1 VAL A 30 ALA A 34 5 5
HELIX 2 2 ASN A 47 ALA A 55 1 9
HELIX 3 3 SER A 69 GLY A 83 1 15
HELIX 4 4 GLY A 89 GLY A 97 1 9
HELIX 5 5 MET A 125 GLY A 140 1 16
HELIX 6 6 ASP A 141 GLY A 152 1 12
HELIX 7 7 SER A 156 GLY A 161 1 6
HELIX 8 8 THR A 180 ASP A 185 1 6
HELIX 9 9 THR A 189 LEU A 206 1 18
HELIX 10 10 MET A 213 GLY A 217 5 5
HELIX 11 11 SER A 225 SER A 236 1 12
HELIX 12 12 LYS A 237 ASP A 240 5 4
HELIX 13 13 THR A 244 LEU A 249 1 6
HELIX 14 14 THR A 250 THR A 261 1 12
HELIX 15 15 GLN A 281 GLY A 283 5 3
HELIX 16 16 GLU A 292 THR A 294 5 3
HELIX 17 17 LYS A 295 GLY A 303 1 9
HELIX 18 18 ASP A 307 ARG A 311 5 5
HELIX 19 19 SER A 318 HIS A 324 1 7
HELIX 20 20 SER A 356 GLY A 360 5 5
HELIX 21 21 SER A 369 THR A 393 1 25
HELIX 22 22 ASN B 47 ALA B 55 1 9
HELIX 23 23 SER B 69 GLY B 83 1 15
HELIX 24 24 GLY B 89 GLY B 97 1 9
HELIX 25 25 MET B 125 GLY B 140 1 16
HELIX 26 26 ASP B 141 HIS B 151 1 11
HELIX 27 27 SER B 156 GLY B 161 1 6
HELIX 28 28 THR B 180 ILE B 186 1 7
HELIX 29 29 THR B 189 GLY B 207 1 19
HELIX 30 30 MET B 213 GLY B 217 5 5
HELIX 31 31 SER B 225 SER B 236 1 12
HELIX 32 32 LYS B 237 ASP B 240 5 4
HELIX 33 33 THR B 244 LEU B 249 1 6
HELIX 34 34 THR B 250 THR B 261 1 12
HELIX 35 35 GLU B 292 THR B 294 5 3
HELIX 36 36 LYS B 295 GLY B 303 1 9
HELIX 37 37 ASP B 307 ARG B 311 5 5
HELIX 38 38 SER B 318 GLN B 323 1 6
HELIX 39 39 SER B 356 GLY B 360 5 5
HELIX 40 40 SER B 369 SER B 392 1 24
SHEET 1 A 7 THR A 59 ALA A 62 0
SHEET 2 A 7 PHE A 20 VAL A 23 1 N PHE A 22 O TYR A 60
SHEET 3 A 7 VAL A 118 HIS A 123 1 O HIS A 119 N VAL A 21
SHEET 4 A 7 VAL A 167 ILE A 173 1 O THR A 168 N VAL A 118
SHEET 5 A 7 TYR A 268 TYR A 272 1 O TYR A 268 N ILE A 170
SHEET 6 A 7 TRP A 344 VAL A 346 1 O GLN A 345 N THR A 271
SHEET 7 A 7 ASN A 330 SER A 332 1 N ILE A 331 O TRP A 344
SHEET 1 B 2 GLY A 84 ASP A 87 0
SHEET 2 B 2 TYR A 101 TYR A 105 -1 O LYS A 103 N VAL A 86
SHEET 1 C 2 GLY A 274 VAL A 275 0
SHEET 2 C 2 MET A 350 LYS A 351 1 O MET A 350 N VAL A 275
SHEET 1 D 2 THR A 277 GLU A 279 0
SHEET 2 D 2 HIS A 285 ALA A 287 -1 O ILE A 286 N HIS A 278
SHEET 1 E 7 THR B 59 ALA B 62 0
SHEET 2 E 7 PHE B 20 VAL B 23 1 N PHE B 22 O TYR B 60
SHEET 3 E 7 VAL B 118 HIS B 123 1 O ILE B 121 N VAL B 21
SHEET 4 E 7 VAL B 167 ILE B 173 1 O SER B 169 N PHE B 120
SHEET 5 E 7 TYR B 268 TYR B 272 1 O LYS B 270 N THR B 172
SHEET 6 E 7 TRP B 344 VAL B 346 1 O GLN B 345 N THR B 271
SHEET 7 E 7 ASN B 330 SER B 332 1 N ILE B 331 O VAL B 346
SHEET 1 F 2 GLY B 84 ASP B 87 0
SHEET 2 F 2 TYR B 101 TYR B 105 -1 O LYS B 103 N VAL B 86
SHEET 1 G 2 GLY B 274 VAL B 275 0
SHEET 2 G 2 MET B 350 LYS B 351 1 O MET B 350 N VAL B 275
SHEET 1 H 2 THR B 277 GLU B 279 0
SHEET 2 H 2 HIS B 285 ALA B 287 -1 O ILE B 286 N HIS B 278
CRYST1 73.310 77.960 169.810 90.00 90.00 90.00 P 21 21 21 8
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 0.013641 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012827 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005889 0.00000
TER 3076 THR A 393
TER 6145 SER B 392
MASTER 400 0 4 40 26 0 0 6 6173 2 0 68
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