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HEADER HYDROLASE 10-MAY-07 2PVS
TITLE STRUCTURE OF HUMAN PANCREATIC LIPASE RELATED PROTEIN 2
TITLE 2 MUTANT N336Q
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC LIPASE-RELATED PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: PNLIPRP2, PLRP2;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SMD 1168;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PGAPZB
KEYWDS LIPASE, GALACTO LIPIDS HYDROLYSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SPINELLI,C.EYDOUX,F.CARRIERE,C.CAMBILLAU
REVDAT 1 18-DEC-07 2PVS 0
JRNL AUTH C.EYDOUX,S.SPINELLI,S.DHE-PAGANON,A.EDWARDS,
JRNL AUTH 2 A.DE CARO,C.CAMBILLAU,F.CARRIERE
JRNL TITL STRUCTURE OF HUMAN PANCREATIC LIPASE-RELATED
JRNL TITL 2 PROTEIN 2 WITH THE LID IN AN OPEN CONFORMATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 27791
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1477
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1993
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6977
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 88.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.43000
REMARK 3 B22 (A**2) : 2.43000
REMARK 3 B33 (A**2) : -4.86000
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): 0.383
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.279
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.566
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7078 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4827 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9586 ; 1.369 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11722 ; 0.880 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 873 ; 7.497 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 336 ;39.050 ;24.732
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1154 ;19.065 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.710 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1003 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7926 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1436 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1656 ; 0.227 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5155 ; 0.198 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3423 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3819 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 181 ; 0.174 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.156 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 27 ; 0.208 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.330 ; 0.200
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): 4503 ; 0.496 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1794 ; 0.078 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7010 ; 0.854 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2985 ; 1.071 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2576 ; 1.760 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 235 5
REMARK 3 1 B 1 B 235 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1374 ; 0.16 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1730 ; 0.53 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1374 ; 0.47 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1730 ; 1.06 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 255 A 320 5
REMARK 3 1 B 255 B 320 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 384 ; 0.19 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 A (A): 496 ; 0.40 ; 5.00
REMARK 3 MEDIUM THERMAL 2 A (A**2): 384 ; 0.36 ; 2.00
REMARK 3 LOOSE THERMAL 2 A (A**2): 496 ; 0.72 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2PVS COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB042827.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27791
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : 0.11800
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : 0.48000
REMARK 200 FOR SHELL : 1.500
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: PDB ENTRY 1GPL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6 MICROLITER OF PROTEIN (14.5 MG/ML
REMARK 280 IN 0.2 M NACL, 25 MM TRIS-HCL, PH 8.0) AND 2 MICROLITER OF
REMARK 280 2.05 M AMMONIUM SULPHATE, 0.1 M HEPES, PH 6.7, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,1/2-Y,1/2+Z
REMARK 290 3555 -Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,-X,3/4+Z
REMARK 290 5555 1/2-X,Y,3/4-Z
REMARK 290 6555 X,1/2-Y,1/4-Z
REMARK 290 7555 1/2+Y,1/2+X,1/2-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1-X,1-Y,1+Z
REMARK 290 11555 1/2-Y,1+X,3/4+Z
REMARK 290 12555 1+Y,1/2-X,5/4+Z
REMARK 290 13555 1-X,1/2+Y,5/4-Z
REMARK 290 14555 1/2+X,1-Y,3/4-Z
REMARK 290 15555 1+Y,1+X,1-Z
REMARK 290 16555 1/2-Y,1/2-X,1/2-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 108.09050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 108.09050
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.83600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 108.09050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.91800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 108.09050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 92.75400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 108.09050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 92.75400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 108.09050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.91800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 108.09050
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 108.09050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.83600
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 108.09050
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 108.09050
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 61.83600
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 216.18100
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 216.18100
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 123.67200
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 108.09050
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 216.18100
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 92.75400
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 216.18100
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 108.09050
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 154.59000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 216.18100
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 108.09050
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 154.59000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 108.09050
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 216.18100
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 92.75400
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 216.18100
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 216.18100
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 123.67200
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 108.09050
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 108.09050
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 61.83600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 22220 ANGSTROM**2
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 0.000000 1.000000 0.000000 -108.09050
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 108.09050
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 309.18000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 216.18100
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 108.09050
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 108.09050
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 309.18000
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 LYS A 239
REMARK 465 ASN A 240
REMARK 465 VAL A 241
REMARK 465 LEU A 242
REMARK 465 SER A 243
REMARK 465 THR A 244
REMARK 465 ILE A 245
REMARK 465 THR A 246
REMARK 465 ASP A 247
REMARK 465 ILE A 248
REMARK 465 ASP A 249
REMARK 465 GLY A 250
REMARK 465 ILE A 251
REMARK 465 TRP A 252
REMARK 465 ARG A 406
REMARK 465 GLY A 407
REMARK 465 ILE A 408
REMARK 465 VAL B 241
REMARK 465 LEU B 242
REMARK 465 SER B 243
REMARK 465 THR B 244
REMARK 465 ILE B 245
REMARK 465 THR B 246
REMARK 465 ASP B 247
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O HOH A 509 O HOH A 510 2.05
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 (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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 188 CG GLU A 188 CD 0.093
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 GLU A -1 148.69 -173.25
REMARK 500 ASN A 63 0.72 -69.31
REMARK 500 LEU A 78 69.03 32.17
REMARK 500 ILE A 121 -38.02 -39.03
REMARK 500 ASP A 145 -15.72 164.70
REMARK 500 SER A 152 -119.31 57.35
REMARK 500 ASP A 176 71.94 41.60
REMARK 500 CYS A 181 -11.84 91.57
REMARK 500 VAL A 221 31.31 -142.14
REMARK 500 ILE A 255 20.70 -76.27
REMARK 500 GLU A 293 5.27 -69.58
REMARK 500 CYS A 296 25.99 -149.39
REMARK 500 GLU A 302 42.80 -94.56
REMARK 500 ASN A 364 -135.05 -54.26
REMARK 500 ILE A 372 -31.59 -136.21
REMARK 500 ASP A 380 -31.13 88.10
REMARK 500 CYS A 385 124.16 -170.13
REMARK 500 ASP A 427 22.95 -151.30
REMARK 500 SER A 435 89.44 156.51
REMARK 500 GLN B 5 0.88 -67.42
REMARK 500 LYS B 24 72.66 -101.73
REMARK 500 PRO B 56 19.77 -67.97
REMARK 500 SER B 62 -169.29 -74.13
REMARK 500 LEU B 78 62.19 34.94
REMARK 500 PHE B 94 0.57 -62.43
REMARK 500 SER B 152 -112.52 68.41
REMARK 500 ASP B 176 64.27 33.75
REMARK 500 CYS B 181 -7.85 97.17
REMARK 500 ASP B 205 52.62 -142.50
REMARK 500 LEU B 213 27.16 -141.34
REMARK 500 VAL B 221 22.11 -146.27
REMARK 500 LYS B 238 -89.27 -113.88
REMARK 500 ASP B 249 24.33 96.19
REMARK 500 SER B 260 130.28 -34.19
REMARK 500 CYS B 285 141.14 174.49
REMARK 500 SER B 294 35.67 72.72
REMARK 500 PRO B 298 -163.02 -79.55
REMARK 500 PHE B 335 -0.71 63.52
REMARK 500 LYS B 349 17.32 -145.04
REMARK 500 CYS B 385 135.54 178.35
REMARK 500 ARG B 406 -5.80 -158.65
REMARK 500 SER B 411 -39.53 97.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 409 LEU A 410 -143.70
REMARK 500 LEU A 410 SER A 411 126.18
REMARK 500 GLU B 412 PRO B 413 -148.23
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 A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 187 O
REMARK 620 2 ARG A 190 O 77.4
REMARK 620 3 ASP A 192 OD2 90.7 90.0
REMARK 620 4 ASP A 195 OD1 151.8 127.6 77.9
REMARK 620 5 ASP A 195 OD2 143.4 79.9 61.0 49.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 187 O
REMARK 620 2 ARG B 190 O 78.8
REMARK 620 3 ASP B 192 OD2 93.8 88.8
REMARK 620 4 ASP B 195 OD1 144.8 135.9 83.4
REMARK 620 5 ASP B 195 OD2 162.9 86.1 77.7 49.8
REMARK 620 6 HOH B 511 O 87.3 86.5 174.9 98.6 99.9
REMARK 620 N 1 2 3 4 5
DBREF 2PVS A -2 450 UNP P54317 LIPR2_HUMAN 18 469
DBREF 2PVS B -2 450 UNP P54317 LIPR2_HUMAN 18 469
SEQADV 2PVS GLN A 334 UNP P54317 ASN 353 ENGINEERED
SEQADV 2PVS GLN B 334 UNP P54317 ASN 353 ENGINEERED
SEQRES 1 A 452 LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE SER ASP
SEQRES 2 A 452 GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO VAL LYS
SEQRES 3 A 452 LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR ARG PHE
SEQRES 4 A 452 LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN LEU
SEQRES 5 A 452 ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA SER ASN
SEQRES 6 A 452 PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE HIS GLY
SEQRES 7 A 452 PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER ASP MET
SEQRES 8 A 452 CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN CYS ILE
SEQRES 9 A 452 CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET TYR THR
SEQRES 10 A 452 GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA GLU THR
SEQRES 11 A 452 ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU GLY TYR
SEQRES 12 A 452 SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER LEU GLY
SEQRES 13 A 452 ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU GLY GLY
SEQRES 14 A 452 ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA GLY PRO
SEQRES 15 A 452 CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU ASP PRO
SEQRES 16 A 452 SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR ASP SER
SEQRES 17 A 452 SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET SER GLN
SEQRES 18 A 452 LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS
SEQRES 19 A 452 GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER THR ILE
SEQRES 20 A 452 THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY GLY PHE
SEQRES 21 A 452 VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR TYR SER
SEQRES 22 A 452 SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY TYR PRO
SEQRES 23 A 452 CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS CYS PHE
SEQRES 24 A 452 PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY HIS TYR
SEQRES 25 A 452 ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL GLU GLN
SEQRES 26 A 452 THR PHE PHE LEU ASN THR GLY GLU SER GLY GLN PHE THR
SEQRES 27 A 452 SER TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS
SEQRES 28 A 452 GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU TYR GLY
SEQRES 29 A 452 SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE LYS GLY
SEQRES 30 A 452 SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA ILE ASP
SEQRES 31 A 452 VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL LYS PHE
SEQRES 32 A 452 LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU PRO LYS
SEQRES 33 A 452 LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY GLU ASP
SEQRES 34 A 452 GLY THR GLU TYR ASN PHE CYS SER SER ASP THR VAL GLU
SEQRES 35 A 452 GLU ASN VAL LEU GLN SER LEU TYR PRO CYS
SEQRES 1 B 452 LYS GLU VAL CYS TYR GLY GLN LEU GLY CYS PHE SER ASP
SEQRES 2 B 452 GLU LYS PRO TRP ALA GLY THR LEU GLN ARG PRO VAL LYS
SEQRES 3 B 452 LEU LEU PRO TRP SER PRO GLU ASP ILE ASP THR ARG PHE
SEQRES 4 B 452 LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN LEU
SEQRES 5 B 452 ILE THR GLY THR GLU PRO ASP THR ILE GLU ALA SER ASN
SEQRES 6 B 452 PHE GLN LEU ASP ARG LYS THR ARG PHE ILE ILE HIS GLY
SEQRES 7 B 452 PHE LEU ASP LYS ALA GLU ASP SER TRP PRO SER ASP MET
SEQRES 8 B 452 CYS LYS LYS MET PHE GLU VAL GLU LYS VAL ASN CYS ILE
SEQRES 9 B 452 CYS VAL ASP TRP ARG HIS GLY SER ARG ALA MET TYR THR
SEQRES 10 B 452 GLN ALA VAL GLN ASN ILE ARG VAL VAL GLY ALA GLU THR
SEQRES 11 B 452 ALA PHE LEU ILE GLN ALA LEU SER THR GLN LEU GLY TYR
SEQRES 12 B 452 SER LEU GLU ASP VAL HIS VAL ILE GLY HIS SER LEU GLY
SEQRES 13 B 452 ALA HIS THR ALA ALA GLU ALA GLY ARG ARG LEU GLY GLY
SEQRES 14 B 452 ARG VAL GLY ARG ILE THR GLY LEU ASP PRO ALA GLY PRO
SEQRES 15 B 452 CYS PHE GLN ASP GLU PRO GLU GLU VAL ARG LEU ASP PRO
SEQRES 16 B 452 SER ASP ALA VAL PHE VAL ASP VAL ILE HIS THR ASP SER
SEQRES 17 B 452 SER PRO ILE VAL PRO SER LEU GLY PHE GLY MET SER GLN
SEQRES 18 B 452 LYS VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY LYS
SEQRES 19 B 452 GLU MET PRO GLY CYS LYS LYS ASN VAL LEU SER THR ILE
SEQRES 20 B 452 THR ASP ILE ASP GLY ILE TRP GLU GLY ILE GLY GLY PHE
SEQRES 21 B 452 VAL SER CYS ASN HIS LEU ARG SER PHE GLU TYR TYR SER
SEQRES 22 B 452 SER SER VAL LEU ASN PRO ASP GLY PHE LEU GLY TYR PRO
SEQRES 23 B 452 CYS ALA SER TYR ASP GLU PHE GLN GLU SER LYS CYS PHE
SEQRES 24 B 452 PRO CYS PRO ALA GLU GLY CYS PRO LYS MET GLY HIS TYR
SEQRES 25 B 452 ALA ASP GLN PHE LYS GLY LYS THR SER ALA VAL GLU GLN
SEQRES 26 B 452 THR PHE PHE LEU ASN THR GLY GLU SER GLY GLN PHE THR
SEQRES 27 B 452 SER TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS
SEQRES 28 B 452 GLU LYS VAL ASN GLY TYR ILE ARG ILE ALA LEU TYR GLY
SEQRES 29 B 452 SER ASN GLU ASN SER LYS GLN TYR GLU ILE PHE LYS GLY
SEQRES 30 B 452 SER LEU LYS PRO ASP ALA SER HIS THR CYS ALA ILE ASP
SEQRES 31 B 452 VAL ASP PHE ASN VAL GLY LYS ILE GLN LYS VAL LYS PHE
SEQRES 32 B 452 LEU TRP ASN LYS ARG GLY ILE ASN LEU SER GLU PRO LYS
SEQRES 33 B 452 LEU GLY ALA SER GLN ILE THR VAL GLN SER GLY GLU ASP
SEQRES 34 B 452 GLY THR GLU TYR ASN PHE CYS SER SER ASP THR VAL GLU
SEQRES 35 B 452 GLU ASN VAL LEU GLN SER LEU TYR PRO CYS
HET SO4 A 451 5
HET SO4 A 452 5
HET SO4 A 453 5
HET SO4 B 451 5
HET SO4 B 452 5
HET SO4 A 454 5
HET SO4 A 455 5
HET SO4 B 453 5
HET CA B 501 1
HET CA A 502 1
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 11 CA 2(CA 2+)
FORMUL 13 HOH *67(H2 O)
HELIX 1 1 TYR A 3 GLY A 7 5 5
HELIX 2 2 SER A 29 ASP A 34 1 6
HELIX 3 3 PRO A 56 ALA A 61 1 6
HELIX 4 4 SER A 84 GLU A 97 1 14
HELIX 5 5 TRP A 106 ARG A 111 1 6
HELIX 6 6 MET A 113 GLY A 140 1 28
HELIX 7 7 SER A 152 LEU A 165 1 14
HELIX 8 8 PRO A 186 ARG A 190 5 5
HELIX 9 9 ASP A 192 ALA A 196 5 5
HELIX 10 10 GLY A 256 VAL A 259 5 4
HELIX 11 11 SER A 260 VAL A 274 1 15
HELIX 12 12 SER A 287 GLU A 293 1 7
HELIX 13 13 GLY A 308 PHE A 314 5 7
HELIX 14 14 TYR B 3 GLY B 7 5 5
HELIX 15 15 SER B 29 ASP B 34 1 6
HELIX 16 16 GLU B 55 SER B 62 1 8
HELIX 17 17 SER B 84 PHE B 94 1 11
HELIX 18 18 TRP B 106 ARG B 111 1 6
HELIX 19 19 MET B 113 GLY B 140 1 28
HELIX 20 20 SER B 142 GLU B 144 5 3
HELIX 21 21 SER B 152 LEU B 165 1 14
HELIX 22 22 PRO B 186 ARG B 190 5 5
HELIX 23 23 ASP B 192 ALA B 196 5 5
HELIX 24 24 GLY B 256 VAL B 259 5 4
HELIX 25 25 SER B 260 ASN B 276 1 17
HELIX 26 26 TYR B 288 GLU B 293 1 6
HELIX 27 27 GLY B 308 PHE B 314 5 7
SHEET 1 A10 GLN A 49 ILE A 51 0
SHEET 2 A10 ARG A 36 TYR A 40 -1 N LEU A 39 O GLN A 49
SHEET 3 A10 VAL A 99 ASP A 105 -1 O ASP A 105 N ARG A 36
SHEET 4 A10 LYS A 69 ILE A 74 1 N ARG A 71 O ILE A 102
SHEET 5 A10 VAL A 146 HIS A 151 1 O ILE A 149 N ILE A 74
SHEET 6 A10 ARG A 171 LEU A 175 1 O LEU A 175 N GLY A 150
SHEET 7 A10 PHE A 198 ILE A 202 1 O ILE A 202 N GLY A 174
SHEET 8 A10 LEU A 224 PRO A 228 1 O PHE A 226 N VAL A 201
SHEET 9 A10 GLN A 323 LEU A 327 1 O GLN A 323 N ASP A 225
SHEET 10 A10 TYR A 283 PRO A 284 -1 N TYR A 283 O PHE A 326
SHEET 1 B 2 SER A 206 SER A 207 0
SHEET 2 B 2 GLY A 216 MET A 217 1 O GLY A 216 N SER A 207
SHEET 1 C 8 TYR A 370 LEU A 377 0
SHEET 2 C 8 VAL A 352 TYR A 361 -1 N VAL A 352 O LEU A 377
SHEET 3 C 8 LYS A 398 ASN A 404 -1 O LYS A 400 N ALA A 359
SHEET 4 C 8 GLN A 445 PRO A 449 -1 O GLN A 445 N PHE A 401
SHEET 5 C 8 GLU A 430 CYS A 434 -1 N CYS A 434 O TYR A 448
SHEET 6 C 8 LEU A 415 SER A 424 -1 N VAL A 422 O TYR A 431
SHEET 7 C 8 TRP A 338 GLY A 348 -1 N LYS A 341 O GLN A 423
SHEET 8 C 8 SER A 382 VAL A 389 -1 O ILE A 387 N TYR A 340
SHEET 1 D10 ASN B 44 ILE B 51 0
SHEET 2 D10 ARG B 36 THR B 41 -1 N LEU B 39 O GLN B 49
SHEET 3 D10 VAL B 99 ASP B 105 -1 O CYS B 101 N TYR B 40
SHEET 4 D10 LYS B 69 ILE B 74 1 N ARG B 71 O ILE B 102
SHEET 5 D10 VAL B 146 HIS B 151 1 O ILE B 149 N PHE B 72
SHEET 6 D10 ARG B 171 LEU B 175 1 O LEU B 175 N GLY B 150
SHEET 7 D10 PHE B 198 ILE B 202 1 O PHE B 198 N ILE B 172
SHEET 8 D10 LEU B 224 PRO B 228 1 O PHE B 226 N VAL B 201
SHEET 9 D10 GLN B 323 LEU B 327 1 O PHE B 325 N PHE B 227
SHEET 10 D10 TYR B 283 PRO B 284 -1 N TYR B 283 O PHE B 326
SHEET 1 E 2 SER B 206 SER B 207 0
SHEET 2 E 2 GLY B 216 MET B 217 1 O GLY B 216 N SER B 207
SHEET 1 F 3 ASN B 366 PHE B 373 0
SHEET 2 F 3 VAL B 352 TYR B 361 -1 N LEU B 360 O SER B 367
SHEET 3 F 3 SER B 376 LEU B 377 -1 O LEU B 377 N VAL B 352
SHEET 1 G 8 ASN B 366 PHE B 373 0
SHEET 2 G 8 VAL B 352 TYR B 361 -1 N LEU B 360 O SER B 367
SHEET 3 G 8 LYS B 398 LYS B 405 -1 O LEU B 402 N ARG B 357
SHEET 4 G 8 GLN B 445 PRO B 449 -1 O GLN B 445 N PHE B 401
SHEET 5 G 8 GLU B 430 CYS B 434 -1 N CYS B 434 O TYR B 448
SHEET 6 G 8 GLN B 419 SER B 424 -1 N ILE B 420 O PHE B 433
SHEET 7 G 8 TRP B 338 SER B 343 -1 N SER B 343 O THR B 421
SHEET 8 G 8 THR B 384 VAL B 389 -1 O ILE B 387 N TYR B 340
SHEET 1 H 2 LEU B 346 SER B 347 0
SHEET 2 H 2 GLY B 416 ALA B 417 -1 O GLY B 416 N SER B 347
SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.08
SSBOND 2 CYS A 90 CYS A 101 1555 1555 2.07
SSBOND 3 CYS A 237 CYS A 261 1555 1555 2.07
SSBOND 4 CYS A 285 CYS A 296 1555 1555 2.06
SSBOND 5 CYS A 299 CYS A 304 1555 1555 2.03
SSBOND 6 CYS A 434 CYS A 450 1555 1555 2.07
SSBOND 7 CYS B 2 CYS B 8 1555 1555 2.07
SSBOND 8 CYS B 90 CYS B 101 1555 1555 2.08
SSBOND 9 CYS B 237 CYS B 261 1555 1555 2.08
SSBOND 10 CYS B 285 CYS B 296 1555 1555 2.09
SSBOND 11 CYS B 299 CYS B 304 1555 1555 2.04
SSBOND 12 CYS B 434 CYS B 450 1555 1555 2.07
LINK O GLU A 187 CA CA A 502 1555 1555 2.25
LINK O ARG A 190 CA CA A 502 1555 1555 2.38
LINK OD2 ASP A 192 CA CA A 502 1555 1555 2.32
LINK OD1 ASP A 195 CA CA A 502 1555 1555 2.59
LINK OD2 ASP A 195 CA CA A 502 1555 1555 2.66
LINK O GLU B 187 CA CA B 501 1555 1555 2.40
LINK O ARG B 190 CA CA B 501 1555 1555 2.31
LINK OD2 ASP B 192 CA CA B 501 1555 1555 2.11
LINK OD1 ASP B 195 CA CA B 501 1555 1555 2.73
LINK OD2 ASP B 195 CA CA B 501 1555 1555 2.52
LINK CA CA B 501 O HOH B 511 1555 1555 2.43
CISPEP 1 LYS A 13 PRO A 14 0 12.73
CISPEP 2 VAL A 210 PRO A 211 0 4.26
CISPEP 3 PHE A 297 PRO A 298 0 -6.09
CISPEP 4 LYS B 13 PRO B 14 0 7.26
CISPEP 5 VAL B 210 PRO B 211 0 -18.36
CISPEP 6 CYS B 237 LYS B 238 0 -15.16
CISPEP 7 PHE B 297 PRO B 298 0 -0.02
CRYST1 216.181 216.181 123.672 90.00 90.00 90.00 I 41 2 2 32
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 0.004626 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008086 0.00000
TER 3394 CYS A 450
TER 6870 CYS B 450
MASTER 483 0 10 27 45 0 0 6 6977 2 79 70
END |