HEADER COMPLEX (IMMUNOGLOBULIN/LIPOPROTEIN) 23-NOV-96 1OSP
TITLE CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN A OF BORRELIA BURGDORFERI
TITLE 2 COMPLEXED WITH A MURINE MONOCLONAL ANTIBODY FAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB 184.1;
COMPND 3 CHAIN: L;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: FAB 184.1;
COMPND 6 CHAIN: H;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: OUTER SURFACE PROTEIN A;
COMPND 9 CHAIN: O;
COMPND 10 SYNONYM: OSPA;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;
SOURCE 11 ORGANISM_TAXID: 224326;
SOURCE 12 STRAIN: B31;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PET9C
KEYWDS COMPLEX (IMMUNOGLOBULIN-LIPOPROTEIN), OUTER SURFACE PROTEIN A
KEYWDS 2 COMPLEXED WITH FAB184.1, BORRELIA BURGDORFERI STRAIN B31, COMPLEX
KEYWDS 3 (IMMUNOGLOBULIN-LIPOPROTEIN) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,C.L.LAWSON
REVDAT 5 03-NOV-21 1OSP 1 SEQADV
REVDAT 4 13-JUL-11 1OSP 1 VERSN
REVDAT 3 24-FEB-09 1OSP 1 VERSN
REVDAT 2 01-APR-03 1OSP 1 JRNL
REVDAT 1 21-APR-97 1OSP 0
JRNL AUTH H.LI,J.J.DUNN,B.J.LUFT,C.L.LAWSON
JRNL TITL CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE
JRNL TITL 2 PROTEIN A COMPLEXED WITH AN FAB.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 94 3584 1997
JRNL REFN ISSN 0027-8424
JRNL PMID 9108020
JRNL DOI 10.1073/PNAS.94.8.3584
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 54404
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5209
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 328
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.614
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OSP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175507.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-95
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58870
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.04800
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+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 44.55000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, O
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 ALA O 17
REMARK 465 LYS O 18
REMARK 465 GLN O 19
REMARK 465 ASN O 20
REMARK 465 VAL O 21
REMARK 465 SER O 22
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ASN L 212
REMARK 475 GLU L 213
REMARK 475 CYS L 214
REMARK 475 GLY H 134
REMARK 475 CYS H 135
REMARK 475 GLY H 136
REMARK 475 ASP H 137
REMARK 475 THR H 138
REMARK 475 THR H 139
REMARK 475 GLY H 140
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 HG1 THR H 90 H VAL H 118 1.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HZ3 LYS O 230 H1 HOH L 275 3446 0.65
REMARK 500 HZ1 LYS O 254 H2 HOH L 258 3446 0.66
REMARK 500 HH12 ARG L 188 H1 HOH L 281 4456 1.09
REMARK 500 HH22 ARG L 61 H1 HOH H 306 4556 1.14
REMARK 500 HZ1 LYS O 254 O HOH L 258 3446 1.27
REMARK 500 HZ3 LYS O 230 O HOH L 275 3446 1.55
REMARK 500 H TRP L 163 OD1 ASN O 251 3456 1.57
REMARK 500 NZ LYS O 254 O HOH L 258 3446 2.17
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG L 211 C ASN L 212 N -0.189
REMARK 500 ASN L 212 C GLU L 213 N -0.182
REMARK 500 PRO H 133 C GLY H 134 N 0.252
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 ARG L 211 O - C - N ANGL. DEV. = -17.5 DEGREES
REMARK 500 LEU H 4 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 PRO H 133 CA - C - N ANGL. DEV. = -27.2 DEGREES
REMARK 500 PRO H 133 O - C - N ANGL. DEV. = 26.7 DEGREES
REMARK 500 GLY H 134 C - N - CA ANGL. DEV. = -12.9 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 ALA L 51 -31.20 70.59
REMARK 500 SER L 67 2.19 -59.26
REMARK 500 ASP L 70 -138.26 -126.76
REMARK 500 LYS L 169 -62.99 -108.02
REMARK 500 ASN L 190 -65.33 -107.25
REMARK 500 THR L 200 9.37 -65.60
REMARK 500 ASN L 212 68.68 -105.30
REMARK 500 SER H 15 -17.51 82.33
REMARK 500 GLU H 27 139.35 -173.80
REMARK 500 ASN H 43 31.90 76.54
REMARK 500 ARG H 52 -151.59 -137.47
REMARK 500 CYS H 135 -178.75 -176.55
REMARK 500 PHE H 153 -74.51 -108.14
REMARK 500 SER H 156 103.05 89.54
REMARK 500 SER H 193 2.46 -69.49
REMARK 500 TRP H 195 -75.58 -87.27
REMARK 500 LYS O 48 -7.30 -59.64
REMARK 500 LYS O 83 -2.38 75.04
REMARK 500 LYS O 107 -42.95 -133.12
REMARK 500 LYS O 119 -4.87 76.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG L 211 -16.20
REMARK 500 ASN L 212 16.41
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OSP H 121 218 UNP P01867 GCBM_MOUSE 1 98
DBREF 1OSP O 17 273 UNP P14013 OSPA1_BORBU 16 273
DBREF 1OSP L 1 214 PDB 1OSP 1OSP 1 214
SEQADV 1OSP ALA O 17 UNP P14013 CYS 17 CONFLICT
SEQADV 1OSP LYS O 39 UNP P14013 ASN 39 VARIANT
SEQADV 1OSP CYS O 84 UNP P14013 SER 84 ENGINEERED MUTATION
SEQADV 1OSP GLY O 149 UNP P14013 GLU 149 VARIANT
SEQADV 1OSP GLY O 164 UNP P14013 SER 164 VARIANT
SEQRES 1 L 214 ASP ILE GLN MET SER GLN SER SER SER SER PHE SER VAL
SEQRES 2 L 214 SER LEU GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER
SEQRES 3 L 214 GLU ASP ILE TYR SER ARG LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY ASN ALA PRO ARG LEU LEU ILE SER GLY ALA THR
SEQRES 5 L 214 SER LEU GLU THR TRP VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 ASP SER GLY LYS ASP TYR THR LEU SER ILE THR SER LEU
SEQRES 7 L 214 GLN THR GLU ASP VAL ALA THR TYR PHE CYS GLN GLN TYR
SEQRES 8 L 214 TRP SER PRO PRO PRO THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 H 218 GLU VAL GLN LEU GLN GLU SER GLY PRO SER LEU VAL LYS
SEQRES 2 H 218 PRO SER GLN THR LEU SER LEU THR CYS SER VAL THR GLY
SEQRES 3 H 218 GLU PRO ILE THR SER GLY PHE TRP ASP TRP ILE ARG LYS
SEQRES 4 H 218 PHE PRO GLY ASN LYS LEU GLU PHE MET GLY TYR ILE ARG
SEQRES 5 H 218 TYR GLY GLY GLY THR TYR TYR ASN PRO SER LEU LYS SER
SEQRES 6 H 218 PRO ILE SER ILE THR ARG ASP THR SER LYS ASN HIS TYR
SEQRES 7 H 218 TYR LEU GLN LEU ASN SER VAL VAL THR GLU ASP THR ALA
SEQRES 8 H 218 THR TYR TYR CYS ALA ARG SER ARG ASP TYR TYR GLY SER
SEQRES 9 H 218 SER GLY PHE ALA PHE TRP GLY GLU GLY THR LEU VAL THR
SEQRES 10 H 218 VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 H 218 LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL
SEQRES 12 H 218 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER
SEQRES 13 H 218 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER
SEQRES 14 H 218 VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR
SEQRES 15 H 218 THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP
SEQRES 16 H 218 PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA
SEQRES 17 H 218 SER SER THR THR VAL ASP LYS LYS LEU GLU
SEQRES 1 O 257 ALA LYS GLN ASN VAL SER SER LEU ASP GLU LYS ASN SER
SEQRES 2 O 257 VAL SER VAL ASP LEU PRO GLY GLU MET LYS VAL LEU VAL
SEQRES 3 O 257 SER LYS GLU LYS ASN LYS ASP GLY LYS TYR ASP LEU ILE
SEQRES 4 O 257 ALA THR VAL ASP LYS LEU GLU LEU LYS GLY THR SER ASP
SEQRES 5 O 257 LYS ASN ASN GLY SER GLY VAL LEU GLU GLY VAL LYS ALA
SEQRES 6 O 257 ASP LYS CYS LYS VAL LYS LEU THR ILE SER ASP ASP LEU
SEQRES 7 O 257 GLY GLN THR THR LEU GLU VAL PHE LYS GLU ASP GLY LYS
SEQRES 8 O 257 THR LEU VAL SER LYS LYS VAL THR SER LYS ASP LYS SER
SEQRES 9 O 257 SER THR GLU GLU LYS PHE ASN GLU LYS GLY GLU VAL SER
SEQRES 10 O 257 GLU LYS ILE ILE THR ARG ALA ASP GLY THR ARG LEU GLU
SEQRES 11 O 257 TYR THR GLY ILE LYS SER ASP GLY SER GLY LYS ALA LYS
SEQRES 12 O 257 GLU VAL LEU LYS GLY TYR VAL LEU GLU GLY THR LEU THR
SEQRES 13 O 257 ALA GLU LYS THR THR LEU VAL VAL LYS GLU GLY THR VAL
SEQRES 14 O 257 THR LEU SER LYS ASN ILE SER LYS SER GLY GLU VAL SER
SEQRES 15 O 257 VAL GLU LEU ASN ASP THR ASP SER SER ALA ALA THR LYS
SEQRES 16 O 257 LYS THR ALA ALA TRP ASN SER GLY THR SER THR LEU THR
SEQRES 17 O 257 ILE THR VAL ASN SER LYS LYS THR LYS ASP LEU VAL PHE
SEQRES 18 O 257 THR LYS GLU ASN THR ILE THR VAL GLN GLN TYR ASP SER
SEQRES 19 O 257 ASN GLY THR LYS LEU GLU GLY SER ALA VAL GLU ILE THR
SEQRES 20 O 257 LYS LEU ASP GLU ILE LYS ASN ALA LEU LYS
FORMUL 4 HOH *328(H2 O)
HELIX 1 1 THR L 80 ASP L 82 5 3
HELIX 2 2 SER L 122 THR L 126 1 5
HELIX 3 3 LYS L 183 ARG L 188 1 6
HELIX 4 4 TYR H 53 GLY H 55 5 3
HELIX 5 5 THR H 87 ASP H 89 5 3
HELIX 6 6 SER H 192 THR H 194 5 3
HELIX 7 7 PRO H 207 SER H 209 5 3
HELIX 8 8 GLU O 26 ASN O 28 5 3
HELIX 9 9 PRO O 35 GLU O 37 5 3
HELIX 10 10 SER O 218 THR O 220 5 3
HELIX 11 11 LEU O 265 ALA O 271 1 7
SHEET 1 A 2 SER L 10 VAL L 13 0
SHEET 2 A 2 LYS L 103 ILE L 106 1 N LYS L 103 O PHE L 11
SHEET 1 B 3 VAL L 19 CYS L 23 0
SHEET 2 B 3 TYR L 71 ILE L 75 -1 N ILE L 75 O VAL L 19
SHEET 3 B 3 PHE L 62 SER L 65 -1 N SER L 65 O THR L 72
SHEET 1 C 3 THR L 85 GLN L 90 0
SHEET 2 C 3 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85
SHEET 3 C 3 ARG L 45 ILE L 48 -1 N ILE L 48 O TRP L 35
SHEET 1 D 4 THR L 114 PHE L 118 0
SHEET 2 D 4 GLY L 129 ASN L 137 -1 N ASN L 137 O THR L 114
SHEET 3 D 4 MET L 175 THR L 182 -1 N LEU L 181 O ALA L 130
SHEET 4 D 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176
SHEET 1 E 4 SER L 153 ARG L 155 0
SHEET 2 E 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 E 4 SER L 191 THR L 197 -1 N THR L 197 O ASN L 145
SHEET 4 E 4 ILE L 205 ASN L 210 -1 N PHE L 209 O TYR L 192
SHEET 1 F 4 GLN H 3 SER H 7 0
SHEET 2 F 4 LEU H 18 THR H 25 -1 N THR H 25 O GLN H 3
SHEET 3 F 4 HIS H 77 LEU H 82 -1 N LEU H 82 O LEU H 18
SHEET 4 F 4 ILE H 67 ASP H 72 -1 N ASP H 72 O HIS H 77
SHEET 1 G 5 THR H 114 VAL H 116 0
SHEET 2 G 5 ALA H 91 ARG H 97 -1 N TYR H 93 O THR H 114
SHEET 3 G 5 TRP H 34 PHE H 40 -1 N LYS H 39 O THR H 92
SHEET 4 G 5 LYS H 44 ILE H 51 -1 N ILE H 51 O TRP H 34
SHEET 5 G 5 THR H 57 TYR H 59 -1 N TYR H 58 O TYR H 50
SHEET 1 H 4 SER H 127 LEU H 131 0
SHEET 2 H 4 SER H 142 TYR H 152 -1 N LYS H 150 O SER H 127
SHEET 3 H 4 TYR H 182 PRO H 191 -1 N VAL H 190 O VAL H 143
SHEET 4 H 4 SER H 169 PHE H 173 -1 N PHE H 173 O SER H 185
SHEET 1 I 3 THR H 158 ASN H 162 0
SHEET 2 I 3 THR H 201 HIS H 206 -1 N ALA H 205 O THR H 158
SHEET 3 I 3 THR H 211 LYS H 216 -1 N LYS H 215 O CYS H 202
SHEET 1 J 2 LEU H 176 GLN H 178 0
SHEET 2 J 2 LEU H 181 THR H 183 -1 N THR H 183 O LEU H 176
SHEET 1 K 2 SER O 29 ASP O 33 0
SHEET 2 K 2 LYS O 39 SER O 43 -1 N VAL O 42 O VAL O 30
SHEET 1 L 2 TYR O 52 VAL O 58 0
SHEET 2 L 2 LEU O 61 SER O 67 -1 N SER O 67 O TYR O 52
SHEET 1 M12 GLY O 74 VAL O 79 0
SHEET 2 M12 LYS O 85 ILE O 90 -1 N ILE O 90 O GLY O 74
SHEET 3 M12 GLN O 96 PHE O 102 -1 N PHE O 102 O LYS O 85
SHEET 4 M12 LEU O 109 SER O 116 -1 N THR O 115 O THR O 97
SHEET 5 M12 SER O 121 PHE O 126 -1 N GLU O 124 O LYS O 112
SHEET 6 M12 VAL O 132 THR O 138 -1 N THR O 138 O SER O 121
SHEET 7 M12 ARG O 144 THR O 148 -1 N TYR O 147 O LYS O 135
SHEET 8 M12 GLY O 156 VAL O 161 -1 N VAL O 161 O ARG O 144
SHEET 9 M12 VAL O 166 LEU O 171 -1 N LEU O 171 O GLY O 156
SHEET 10 M12 LYS O 175 GLU O 182 -1 N VAL O 179 O GLU O 168
SHEET 11 M12 VAL O 185 SER O 192 -1 N ILE O 191 O THR O 176
SHEET 12 M12 VAL O 197 ASP O 203 -1 N ASN O 202 O THR O 186
SHEET 1 N 4 LYS O 212 ASN O 217 0
SHEET 2 N 4 THR O 222 VAL O 227 -1 N THR O 226 O THR O 213
SHEET 3 N 4 LYS O 230 PHE O 237 -1 N LEU O 235 O LEU O 223
SHEET 4 N 4 ILE O 243 GLN O 247 -1 N GLN O 246 O ASP O 234
SHEET 1 O 2 ALA H 96 SER H 98 0
SHEET 2 O 2 PHE H 107 TRP H 110 -1 N PHE H 109 O ARG H 97
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.55
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.41
SSBOND 3 CYS H 22 CYS H 95 1555 1555 2.54
SSBOND 4 CYS H 147 CYS H 202 1555 1555 2.42
CISPEP 1 PRO L 94 PRO L 95 0 -0.44
CISPEP 2 TYR L 140 PRO L 141 0 -0.49
CRYST1 89.100 91.700 100.400 90.00 90.00 90.00 P 21 21 21 4
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 0.011223 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010905 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009960 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
