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HEADER GLYCOPROTEIN 14-MAR-02 1GWB TITLE STRUCTURE OF GLYCOPROTEIN 1B COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLATELET GLYCOPROTEIN IB ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 16-296; COMPND 5 SYNONYM: GP-IB ALPHA, GPIBA, CD42B-ALPHA, CD42B; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE:; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 16-296; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: TYR 292,294,295 MODIFIED TO TYROSINE-O- COMPND 12 SULPHONIC ACID SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 MOL_ID: 2 KEYWDS GLYCOPROTEIN 1B, PLATELET, TRANSMEMBRANE, GLYCOPROTEIN, KEYWDS 2 HEMOSTASIS, BLOOD COAGULATION, REPEAT, LEUCINE-RICH REPEAT, KEYWDS 3 SIGNAL, CELL ADHESION, DISEASE MUTATION, POLYMORPHISM, VON KEYWDS 4 WILLEBRAND DISEASE, BERNARD SOULIER SYNDROME EXPDTA X-RAY DIFFRACTION AUTHOR J.EMSLEY,S.UFF,K.CLEMETSON,J.CLEMETSON,T.HARRISON REVDAT 1 06-FEB-03 1GWB 0 JRNL AUTH S.UFF,J.M.CLEMETSON,T.HARRISON,K.J.CLEMETSON, JRNL AUTH 2 J.EMSLEY JRNL TITL CRYSTAL STRUCTURE OF THE PLATELET GLYCOPROTEIN JRNL TITL 2 IB(ALPHA) N-TERMINAL DOMAIN REVEALS AN UNMASKING JRNL TITL 3 MECHANISM FOR RECEPTOR ACTIVATION. JRNL REF J.BIOL.CHEM. V. 277 35657 2002 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 37462 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.245 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 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 : 4205 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 103 REMARK 3 SOLVENT ATOMS : NULL 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) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.84 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 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 1GWB COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-9557 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 10 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37462 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : 0.09900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.1000 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 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,1/3+Z REMARK 290 3555 -X+Y,-X,2/3+Z REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,1/3+Z REMARK 290 6555 X-Y,X,2/3+Z REMARK 290 7555 Y,X,1/3-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,2/3-Z REMARK 290 10555 -Y,-X,1/3-Z REMARK 290 11555 -X+Y,Y,-Z REMARK 290 12555 X,X-Y,2/3-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.66667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 85.33333 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.66667 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 85.33333 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 42.66667 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 85.33333 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 42.66667 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 85.33333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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, B, Y, Z 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 PRO A 16 REMARK 465 HIS A 17 REMARK 465 GLY A 284 REMARK 465 ASP A 285 REMARK 465 GLU A 286 REMARK 465 GLY A 287 REMARK 465 ASP A 288 REMARK 465 THR A 289 REMARK 465 ASP A 290 REMARK 465 LEU A 291 REMARK 465 STY A 292 REMARK 465 ASP A 293 REMARK 465 STY A 294 REMARK 465 STY A 295 REMARK 465 PRO A 296 REMARK 465 PRO B 16 REMARK 465 HIS B 17 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 MET A 68 CG SD CE REMARK 470 MET A 255 CG SD CE REMARK 470 LEU A 283 CA C O CB CG CD1 CD2 REMARK 470 MET B 68 CG SD CE REMARK 470 MET B 255 CG SD CE 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 O HOH Z 27 O HOH Z 27 12565 1.97 REMARK 500 O HOH Y 57 O HOH Y 57 11556 2.05 REMARK 500 CG2 THR A 39 CG2 THR A 39 9555 2.12 REMARK 500 OE1 GLU B 188 OE1 GLU B 188 11556 2.18 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 PRO A 18 CB PRO A 18 CG 0.052 REMARK 500 THR A 282 C LEU A 283 N -0.078 REMARK 500 PRO B 42 CB PRO B 42 CG 0.067 REMARK 500 PRO B 42 CG PRO B 42 CD 0.054 REMARK 500 LEU B 139 CG LEU B 139 CD2 -0.052 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 GLY A 90 N - CA - C ANGL. DEV. = 14.9 DEGREES REMARK 500 VAL A 272 N - CA - C ANGL. DEV. =-14.7 DEGREES REMARK 500 PRO B 42 C - N - CA ANGL. DEV. = 25.0 DEGREES REMARK 500 PRO B 42 C - N - CD ANGL. DEV. =-34.9 DEGREES REMARK 500 GLY B 90 N - CA - C ANGL. DEV. = 19.2 DEGREES REMARK 500 LEU B 139 CA - CB - CG ANGL. DEV. = 13.0 DEGREES REMARK 500 PRO B 296 C - N - CA ANGL. DEV. = 52.5 DEGREES REMARK 500 PRO B 296 C - N - CD ANGL. DEV. =-53.6 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ILE A 19 -65.45 50.09 REMARK 500 ALA A 26 -111.98 65.54 REMARK 500 THR A 39 -37.07 69.15 REMARK 500 TYR A 60 -36.71 60.58 REMARK 500 LEU A 152 125.11 62.93 REMARK 500 ALA B 26 -108.04 54.48 REMARK 500 TYR B 60 -52.01 64.92 REMARK 500 GLN B 248 -115.44 58.96 REMARK 500 TYR B 273 -25.38 124.70 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH Y 6 DISTANCE = 6.86 ANGSTROMS REMARK 525 HOH Y 9 DISTANCE = 5.17 ANGSTROMS REMARK 525 HOH Y 12 DISTANCE = 7.04 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN B DBREF 1GWB A 16 296 UNP P07359 GPBA_HUMAN 16 296 DBREF 1GWB B 16 296 UNP P07359 GPBA_HUMAN 16 296 SEQRES 1 A 281 PRO HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS SEQRES 2 A 281 LEU GLU VAL ASN CYS ASP LYS ARG ASN LEU THR ALA LEU SEQRES 3 A 281 PRO PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SEQRES 4 A 281 SER GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU SEQRES 5 A 281 MET PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG SEQRES 6 A 281 CYS GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO SEQRES 7 A 281 VAL LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SEQRES 8 A 281 SER LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR SEQRES 9 A 281 VAL LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO SEQRES 10 A 281 LEU GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU SEQRES 11 A 281 TYR LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY SEQRES 12 A 281 LEU LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU SEQRES 13 A 281 ALA ASN ASN ASN LEU THR GLU LEU PRO ALA GLY LEU LEU SEQRES 14 A 281 ASN GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU SEQRES 15 A 281 ASN SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER SEQRES 16 A 281 HIS LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP SEQRES 17 A 281 LEU CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU SEQRES 18 A 281 GLN ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY SEQRES 19 A 281 VAL ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL SEQRES 20 A 281 GLN CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR SEQRES 21 A 281 PRO GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP SEQRES 22 A 281 THR ASP LEU STY ASP STY STY PRO SEQRES 1 B 281 PRO HIS PRO ILE CYS GLU VAL SER LYS VAL ALA SER HIS SEQRES 2 B 281 LEU GLU VAL ASN CYS ASP LYS ARG ASN LEU THR ALA LEU SEQRES 3 B 281 PRO PRO ASP LEU PRO LYS ASP THR THR ILE LEU HIS LEU SEQRES 4 B 281 SER GLU ASN LEU LEU TYR THR PHE SER LEU ALA THR LEU SEQRES 5 B 281 MET PRO TYR THR ARG LEU THR GLN LEU ASN LEU ASP ARG SEQRES 6 B 281 CYS GLU LEU THR LYS LEU GLN VAL ASP GLY THR LEU PRO SEQRES 7 B 281 VAL LEU GLY THR LEU ASP LEU SER HIS ASN GLN LEU GLN SEQRES 8 B 281 SER LEU PRO LEU LEU GLY GLN THR LEU PRO ALA LEU THR SEQRES 9 B 281 VAL LEU ASP VAL SER PHE ASN ARG LEU THR SER LEU PRO SEQRES 10 B 281 LEU GLY ALA LEU ARG GLY LEU GLY GLU LEU GLN GLU LEU SEQRES 11 B 281 TYR LEU LYS GLY ASN GLU LEU LYS THR LEU PRO PRO GLY SEQRES 12 B 281 LEU LEU THR PRO THR PRO LYS LEU GLU LYS LEU SER LEU SEQRES 13 B 281 ALA ASN ASN ASN LEU THR GLU LEU PRO ALA GLY LEU LEU SEQRES 14 B 281 ASN GLY LEU GLU ASN LEU ASP THR LEU LEU LEU GLN GLU SEQRES 15 B 281 ASN SER LEU TYR THR ILE PRO LYS GLY PHE PHE GLY SER SEQRES 16 B 281 HIS LEU LEU PRO PHE ALA PHE LEU HIS GLY ASN PRO TRP SEQRES 17 B 281 LEU CYS ASN CYS GLU ILE LEU TYR PHE ARG ARG TRP LEU SEQRES 18 B 281 GLN ASP ASN ALA GLU ASN VAL TYR VAL TRP LYS GLN GLY SEQRES 19 B 281 VAL ASP VAL LYS ALA MET THR SER ASN VAL ALA SER VAL SEQRES 20 B 281 GLN CYS ASP ASN SER ASP LYS PHE PRO VAL TYR LYS TYR SEQRES 21 B 281 PRO GLY LYS GLY CYS PRO THR LEU GLY ASP GLU GLY ASP SEQRES 22 B 281 THR ASP LEU TYS ASP TYS TYS PRO MODRES 1GWB ASN A 175 ASN GLYCOSYLATION SITE MODRES 1GWB ASN B 175 ASN GLYCOSYLATION SITE MODRES 1GWB ASN A 37 ASN GLYCOSYLATION SITE MODRES 1GWB TYS B 292 TYR SULFONATED TYROSINE MODRES 1GWB TYS B 294 TYR SULFONATED TYROSINE MODRES 1GWB TYS B 295 TYR SULFONATED TYROSINE HET TYS B 292 16 HET TYS B 294 16 HET TYS B 295 16 HET NAG A 600 14 HET NAG A1175 14 HET NDG A1137 14 HET PT A 400 1 HET PT A 402 1 HET PT A 403 1 HET PT A 404 1 HET SO4 B 504 5 HET ACY A 510 4 HETNAM TYS SULFONATED TYROSINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE HETNAM PT PLATINUM (II) ION HETNAM SO4 SULFATE ION HETNAM ACY ACETIC ACID HETSYN NAG NAG FORMUL 2 TYS 3(C9 H11 N O6 S) FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 5 NDG C8 H15 N O6 FORMUL 6 PT 4(PT 2+) FORMUL 10 SO4 O4 S 2- FORMUL 11 ACY C2 H4 O2 FORMUL 12 HOH *143(H2 O) HELIX 1 1 ALA A 65 MET A 68 5 4 HELIX 2 2 GLU A 228 ASN A 239 1 12 HELIX 3 3 ASN A 258 SER A 261 5 4 HELIX 4 4 ALA B 65 MET B 68 5 4 HELIX 5 5 ILE B 229 ASN B 239 1 11 HELIX 6 6 ASN B 258 VAL B 262 5 5 HELIX 7 7 ASP B 265 SER B 267 5 3 SHEET 1 AA11 VAL A 22 SER A 23 0 SHEET 2 AA11 GLU A 30 ASN A 32 -1 O GLU A 30 N SER A 23 SHEET 3 AA11 ILE A 51 HIS A 53 1 O ILE A 51 N VAL A 31 SHEET 4 AA11 GLN A 75 ASN A 77 1 O GLN A 75 N LEU A 52 SHEET 5 AA11 THR A 97 ASP A 99 1 O THR A 97 N LEU A 76 SHEET 6 AA11 VAL A 120 ASP A 122 1 O VAL A 120 N LEU A 98 SHEET 7 AA11 GLU A 144 TYR A 146 1 O GLU A 144 N LEU A 121 SHEET 8 AA11 LYS A 168 SER A 170 1 O LYS A 168 N LEU A 145 SHEET 9 AA11 THR A 192 LEU A 194 1 O THR A 192 N LEU A 169 SHEET 10 AA11 PHE A 215 PHE A 217 1 O PHE A 215 N LEU A 193 SHEET 11 AA11 VAL A 243 TYR A 244 1 N TYR A 244 O ALA A 216 SHEET 1 AB 2 THR A 61 SER A 63 0 SHEET 2 AB 2 LYS A 85 GLN A 87 1 O LYS A 85 N PHE A 62 SHEET 1 AC 2 GLN A 263 CYS A 264 0 SHEET 2 AC 2 PHE A 270 PRO A 271 -1 O PHE A 270 N CYS A 264 SHEET 1 BA11 GLU B 21 SER B 23 0 SHEET 2 BA11 GLU B 30 ASN B 32 -1 O GLU B 30 N SER B 23 SHEET 3 BA11 ILE B 51 HIS B 53 1 O ILE B 51 N VAL B 31 SHEET 4 BA11 GLN B 75 ASN B 77 1 O GLN B 75 N LEU B 52 SHEET 5 BA11 THR B 97 ASP B 99 1 O THR B 97 N LEU B 76 SHEET 6 BA11 VAL B 120 ASP B 122 1 O VAL B 120 N LEU B 98 SHEET 7 BA11 GLU B 144 TYR B 146 1 O GLU B 144 N LEU B 121 SHEET 8 BA11 LYS B 168 SER B 170 1 O LYS B 168 N LEU B 145 SHEET 9 BA11 THR B 192 LEU B 194 1 O THR B 192 N LEU B 169 SHEET 10 BA11 PHE B 215 PHE B 217 1 O PHE B 215 N LEU B 193 SHEET 11 BA11 VAL B 243 TYR B 244 1 N TYR B 244 O ALA B 216 SHEET 1 BB 2 THR B 61 SER B 63 0 SHEET 2 BB 2 LYS B 85 GLN B 87 1 O LYS B 85 N PHE B 62 SSBOND 1 CYS A 20 CYS A 33 SSBOND 2 CYS A 225 CYS A 264 SSBOND 3 CYS A 227 CYS A 280 SSBOND 4 CYS B 20 CYS B 33 SSBOND 5 CYS B 225 CYS B 264 SSBOND 6 CYS B 227 CYS B 280 LINK ND2 ASN A 37 C1 NDG A1137 LINK ND2 ASN A 175 C1 NAG A1175 LINK PT PT A 400 O HOH Y 14 LINK PT PT A 404 O HOH Y 27 LINK ND2 ASN B 175 C1 NAG A 600 LINK C LEU B 291 N TYS B 292 LINK C TYS B 292 N ASP B 293 LINK C ASP B 293 N TYS B 294 LINK C TYS B 294 N TYS B 295 LINK C TYS B 295 N PRO B 296 CISPEP 1 LEU B 41 PRO B 42 0 1.11 SITE 1 AC2 2 MET A 68 THR A 91 SITE 1 AC5 4 ASN A 185 GLY A 186 SER A 210 HIS A 211 SITE 1 AC6 3 GLU B 151 ASN B 175 HOH Z 54 SITE 1 AC8 3 GLU A 151 ASN A 175 HOH Z 55 SITE 1 AC9 5 ARG B 137 GLY B 138 GLU B 141 PRO B 162 SITE 2 AC9 5 LYS B 165 CRYST1 202.000 202.000 128.000 90.00 90.00 120.00 P 64 2 2 24 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 0.004950 0.002858 0.000000 0.00000 SCALE2 0.000000 0.005716 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007812 0.00000