HEADER HYDROLASE 29-MAY-06 2DQK
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SPECIFIC
TITLE 2 LACTOFERRIN PEPTIDE VAL-LEU-LEU-HIS AT 1.93 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE K;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRITIRACHIUM ALKALINE PROTEINASE, ENDOPEPTIDASE K;
COMPND 5 EC: 3.4.21.64;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: VLLH;
COMPND 8 CHAIN: P;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENGYODONTIUM ALBUM;
SOURCE 3 ORGANISM_TAXID: 37998;
SOURCE 4 STRAIN: LIMBER;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 OTHER_DETAILS: LACTOFERRIN PEPTIDE, CHEMICALLY SYNTHESIZED
KEYWDS PROTEINSASE K, SYNTHETIC PEPTIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.SINGH,N.SINGH,S.SHARMA,S.DEY,A.BHUSHAN,T.P.SINGH
REVDAT 4 25-OCT-23 2DQK 1 REMARK SEQADV LINK
REVDAT 3 11-OCT-17 2DQK 1 REMARK
REVDAT 2 24-FEB-09 2DQK 1 VERSN
REVDAT 1 20-JUN-06 2DQK 0
JRNL AUTH A.K.SINGH,N.SINGH,R.K.SOMVANSHI,M.SINHA,S.SHARMA,A.BHUSHAN,
JRNL AUTH 2 S.DEY,T.P.SINGH
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A
JRNL TITL 2 SPECIFIC LACTOFERRIN PEPTIDE VAL-LEU-LEU-HIS AT 1.93
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 18805
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1012
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1334
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1830
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.2240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2064
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 291
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : -0.16000
REMARK 3 B33 (A**2) : 0.32000
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): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.131
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2108 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2864 ; 1.318 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 281 ; 3.848 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 324 ;15.529 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 319 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1624 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 985 ; 0.213 ; 0.300
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): 268 ; 0.140 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.029 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 23 ; 0.232 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.161 ; 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): 1392 ; 0.496 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2206 ; 0.996 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 716 ; 1.931 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 658 ; 3.315 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 2DQK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000025725.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19884
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 57.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
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 <I/SIGMA(I)> 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: 3PRK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM NITRATE, CACL2, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 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+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 54.20350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.15650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.15650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.30525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.15650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.15650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.10175
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.15650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.15650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.30525
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.15650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.15650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.10175
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 0.00000
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 54.20350
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2014 LIES ON A SPECIAL POSITION.
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 ASP A 39 -142.12 -164.89
REMARK 500 SER A 216 -166.29 -114.39
REMARK 500 ASN A 270 78.78 -107.60
REMARK 500 LEU P 2 -121.16 -110.77
REMARK 500 LEU P 3 69.22 92.71
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 CA A1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 175 O
REMARK 620 2 VAL A 177 O 86.0
REMARK 620 3 ASP A 200 OD2 156.8 79.2
REMARK 620 4 ASP A 200 OD1 152.9 113.5 50.2
REMARK 620 5 HOH A2003 O 83.5 73.3 75.1 119.1
REMARK 620 6 HOH A2013 O 97.9 145.2 84.6 76.9 72.9
REMARK 620 7 HOH A2016 O 78.8 141.3 123.6 74.2 138.5 72.8
REMARK 620 8 HOH A2023 O 87.8 73.2 104.8 80.8 145.8 141.2 70.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BJR RELATED DB: PDB
REMARK 900 COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN
REMARK 900 FRAGMENT AND PROTEINASE K
DBREF 2DQK A 1 279 UNP P06873 PRTK_TRIAL 106 384
DBREF 2DQK P 1 4 PDB 2DQK 2DQK 1 4
SEQADV 2DQK ASP A 207 UNP P06873 SER 312 CONFLICT
SEQRES 1 A 279 ALA ALA GLN THR ASN ALA PRO TRP GLY LEU ALA ARG ILE
SEQRES 2 A 279 SER SER THR SER PRO GLY THR SER THR TYR TYR TYR ASP
SEQRES 3 A 279 GLU SER ALA GLY GLN GLY SER CYS VAL TYR VAL ILE ASP
SEQRES 4 A 279 THR GLY ILE GLU ALA SER HIS PRO GLU PHE GLU GLY ARG
SEQRES 5 A 279 ALA GLN MET VAL LYS THR TYR TYR TYR SER SER ARG ASP
SEQRES 6 A 279 GLY ASN GLY HIS GLY THR HIS CYS ALA GLY THR VAL GLY
SEQRES 7 A 279 SER ARG THR TYR GLY VAL ALA LYS LYS THR GLN LEU PHE
SEQRES 8 A 279 GLY VAL LYS VAL LEU ASP ASP ASN GLY SER GLY GLN TYR
SEQRES 9 A 279 SER THR ILE ILE ALA GLY MET ASP PHE VAL ALA SER ASP
SEQRES 10 A 279 LYS ASN ASN ARG ASN CYS PRO LYS GLY VAL VAL ALA SER
SEQRES 11 A 279 LEU SER LEU GLY GLY GLY TYR SER SER SER VAL ASN SER
SEQRES 12 A 279 ALA ALA ALA ARG LEU GLN SER SER GLY VAL MET VAL ALA
SEQRES 13 A 279 VAL ALA ALA GLY ASN ASN ASN ALA ASP ALA ARG ASN TYR
SEQRES 14 A 279 SER PRO ALA SER GLU PRO SER VAL CYS THR VAL GLY ALA
SEQRES 15 A 279 SER ASP ARG TYR ASP ARG ARG SER SER PHE SER ASN TYR
SEQRES 16 A 279 GLY SER VAL LEU ASP ILE PHE GLY PRO GLY THR ASP ILE
SEQRES 17 A 279 LEU SER THR TRP ILE GLY GLY SER THR ARG SER ILE SER
SEQRES 18 A 279 GLY THR SER MET ALA THR PRO HIS VAL ALA GLY LEU ALA
SEQRES 19 A 279 ALA TYR LEU MET THR LEU GLY LYS THR THR ALA ALA SER
SEQRES 20 A 279 ALA CYS ARG TYR ILE ALA ASP THR ALA ASN LYS GLY ASP
SEQRES 21 A 279 LEU SER ASN ILE PRO PHE GLY THR VAL ASN LEU LEU ALA
SEQRES 22 A 279 TYR ASN ASN TYR GLN ALA
SEQRES 1 P 4 VAL LEU LEU HIS
HET CA A1001 1
HET NO3 A2001 4
HETNAM CA CALCIUM ION
HETNAM NO3 NITRATE ION
FORMUL 3 CA CA 2+
FORMUL 4 NO3 N O3 1-
FORMUL 5 HOH *291(H2 O)
HELIX 1 1 PRO A 7 ILE A 13 1 7
HELIX 2 2 HIS A 46 GLU A 50 5 5
HELIX 3 3 GLY A 68 SER A 79 1 12
HELIX 4 4 GLN A 103 LYS A 118 1 16
HELIX 5 5 ASN A 119 ARG A 121 5 3
HELIX 6 6 SER A 138 SER A 151 1 14
HELIX 7 7 ASP A 165 ARG A 167 5 3
HELIX 8 8 GLY A 222 LEU A 240 1 19
HELIX 9 9 SER A 247 THR A 255 1 9
SHEET 1 A 2 ALA A 2 GLN A 3 0
SHEET 2 A 2 TYR A 23 TYR A 24 -1 O TYR A 23 N GLN A 3
SHEET 1 B 7 ALA A 53 THR A 58 0
SHEET 2 B 7 GLN A 89 LYS A 94 1 O LYS A 94 N LYS A 57
SHEET 3 B 7 SER A 33 ASP A 39 1 N VAL A 35 O GLN A 89
SHEET 4 B 7 GLY A 126 LEU A 131 1 O SER A 130 N TYR A 36
SHEET 5 B 7 MET A 154 ALA A 158 1 O MET A 154 N ALA A 129
SHEET 6 B 7 CYS A 178 SER A 183 1 O VAL A 180 N VAL A 157
SHEET 7 B 7 ILE A 201 PRO A 204 1 O ILE A 201 N GLY A 181
SHEET 1 C 2 GLY A 135 GLY A 136 0
SHEET 2 C 2 TYR A 169 SER A 170 -1 O SER A 170 N GLY A 135
SHEET 1 D 2 ILE A 208 TRP A 212 0
SHEET 2 D 2 SER A 216 ILE A 220 -1 O ILE A 220 N ILE A 208
SHEET 1 E 2 ASN A 257 LYS A 258 0
SHEET 2 E 2 LEU A 271 LEU A 272 -1 O LEU A 272 N ASN A 257
SSBOND 1 CYS A 34 CYS A 123 1555 1555 2.02
SSBOND 2 CYS A 178 CYS A 249 1555 1555 2.02
LINK O PRO A 175 CA CA A1001 1555 1555 2.38
LINK O VAL A 177 CA CA A1001 1555 1555 2.40
LINK OD2 ASP A 200 CA CA A1001 1555 1555 2.45
LINK OD1 ASP A 200 CA CA A1001 1555 1555 2.62
LINK CA CA A1001 O HOH A2003 1555 1555 2.39
LINK CA CA A1001 O HOH A2013 1555 1555 2.46
LINK CA CA A1001 O HOH A2016 1555 1555 2.53
LINK CA CA A1001 O HOH A2023 1555 1555 2.44
CISPEP 1 SER A 170 PRO A 171 0 1.32
SITE 1 AC1 7 PRO A 175 VAL A 177 ASP A 200 HOH A2003
SITE 2 AC1 7 HOH A2013 HOH A2016 HOH A2023
SITE 1 AC2 8 TYR A 60 TYR A 61 ARG A 80 LYS A 94
SITE 2 AC2 8 ASP A 97 ASP A 98 HOH A2133 HOH A2252
CRYST1 68.313 68.313 108.407 90.00 90.00 90.00 P 43 21 2 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 0.014639 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014639 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009224 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
