[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER IMMUNE SYSTEM 15-APR-99 1QFW TITLE TERNARY COMPLEX OF HUMAN CHORIONIC GONADOTROPIN WITH FV TITLE 2 ANTI ALPHA SUBUNIT AND FV ANTI BETA SUBUNIT COMPND MOL_ID: 1; COMPND 2 MOLECULE: GONADOTROPIN ALPHA SUBUNIT; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HCG; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GONADOTROPHIN BETA SUBUNIT; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: HCG; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ANTIBODY (ANTI ALPHA SUBUNIT) (LIGHT CHAIN); COMPND 11 CHAIN: L; COMPND 12 FRAGMENT: FV; COMPND 13 SYNONYM: FV; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: ANTIBODY (ANTI ALPHA SUBUNIT) (HEAVY CHAIN); COMPND 17 CHAIN: H; COMPND 18 FRAGMENT: FV; COMPND 19 SYNONYM: FV; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: ANTIBODY (ANTI BETA SUBUNIT) (LIGHT CHAIN); COMPND 23 CHAIN: M; COMPND 24 FRAGMENT: FV; COMPND 25 SYNONYM: FV; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 6; COMPND 28 MOLECULE: ANTIBODY (ANTI BETA SUBUNIT) (HEAVY CHAIN); COMPND 29 CHAIN: I; COMPND 30 FRAGMENT: FV; COMPND 31 SYNONYM: FV; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 SECRETION: HUMAN PREGNANCY URINE; SOURCE 5 OTHER_DETAILS: SUGAR RESIDUES LINKED TO ASN52 AND ASN78; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 SECRETION: HUMAN PREGNANCY URINE; SOURCE 10 MOL_ID: 3; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 MOL_ID: 4; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 MOL_ID: 5; SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 16 MOL_ID: 6; SOURCE 17 ORGANISM_SCIENTIFIC: MUS MUSCULUS KEYWDS GLYCOPROTEIN HORMONE, STIMULATION OF PRODUCTION OF KEYWDS 2 PROGESTERONE, FVS SPECIFICALLY DIRECTED AGAINST ALPHA AND KEYWDS 3 BETA SUBUNIT EXPDTA X-RAY DIFFRACTION AUTHOR M.TEGONI,S.SPINELLI,C.CAMBILLAU REVDAT 2 01-APR-03 1QFW 1 JRNL REVDAT 1 26-APR-00 1QFW 0 JRNL AUTH M.TEGONI,S.SPINELLI,M.VERHOEYEN,P.DAVIS,C.CAMBILLAU JRNL TITL CRYSTAL STRUCTURE OF A TERNARY COMPLEX BETWEEN JRNL TITL 2 HUMAN CHORIONIC GONADOTROPIN (HCG) AND TWO FV JRNL TITL 3 FRAGMENTS SPECIFIC FOR THE ALPHA AND BETA-SUBUNITS. JRNL REF J.MOL.BIOL. V. 289 1375 1999 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.C.HEIKOOP,P.VAN DEN BOOGAART,R.DE LEEUW, REMARK 1 AUTH 2 U.M.ROSEJ,W.M.MULDERS,P.D.J.GROOTENHUIS REMARK 1 TITL PARTIALLY DEGLYCOSYLATED HUMAN CHORIOGANADOTROPIN, REMARK 1 TITL 2 STABILIZED BY INTERSUBUNIT DISULFIDE BONDS, SHOWS REMARK 1 TITL 3 FULL BIOACTIVITY REMARK 1 REF EUR.J.BIOCHEM. V. 253 354 1998 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.J.LAPTHORN,N.W.ISAAC REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN REMARK 1 REF NATURE V. 369 455 1994 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REFERENCE 3 REMARK 1 AUTH H.WU,J.W.LUSTBADER,Y.LIU,R.E.CANFIELD, REMARK 1 AUTH 2 W.A.HENDRIKSON REMARK 1 TITL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 REMARK 1 TITL 2 RESOLUTION FROM MAD ANALYSIS OF THE REMARK 1 TITL 3 SELENOMETHIONYL PROTEIN REMARK 1 REF STRUCTURE (LONDON) V. 2 545 1994 REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REFERENCE 4 REMARK 1 AUTH W.A.HENDRICKSON,R.E.CANFIELD REMARK 1 TITL CRYSTALLIZATION AND CHARACTERIZATION OF HUMAN REMARK 1 TITL 2 CHORIONIC GONADOTROPIN IN CHEMICALLY REMARK 1 TITL 3 DEGLYCOSYLATED AND ENZYMATICALLY DESIALYLATED REMARK 1 TITL 4 STATES REMARK 1 REF BIOCHEMISTRY V. 28 9239 1989 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 5 REMARK 1 AUTH M.M.MATZUK,J.L.KEENE,I.BOIME REMARK 1 TITL SITE SPECIFICITY OF THE CHORIONIC GONADOTROPIN REMARK 1 TITL 2 N-LINKED OLIGOSACCHARIDES IN SIGNAL TRANSDUCTION REMARK 1 REF J.BIOL.CHEM. V. 264 2409 1989 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REFERENCE 6 REMARK 1 AUTH W.R.MOYLE,O.P.BAHL,L.MRZ REMARK 1 TITL ROLE OF THE CARBOHYDRATE OF HUMAN CHORIONIC REMARK 1 TITL 2 GONADOTROPINN IN THE MECHANISM OF HORMONE ACTION REMARK 1 REF J.BIOL.CHEM. V. 250 9163 1975 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 250.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.0 REMARK 3 NUMBER OF REFLECTIONS : 9772 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 SET) : 0.260 REMARK 3 FREE R VALUE : 0.310 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000 REMARK 3 FREE R VALUE TEST SET COUNT : 890 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 : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.65 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1261 REMARK 3 BIN R VALUE (WORKING SET) : 0.3600 REMARK 3 BIN FREE R VALUE : 0.3700 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 116 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 : 4910 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.00 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) : 0.016 REMARK 3 BOND ANGLES (DEGREES) : 2.62 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 29.14 REMARK 3 IMPROPER ANGLES (DEGREES) : 2.29 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 : PARAM19X.PRO REMARK 3 PARAMETER FILE 2 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO REMARK 3 TOPOLOGY FILE 2 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QFW 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 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB000856. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 297.0 REMARK 200 PH : 8.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 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 RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12096 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.16600 REMARK 200 FOR THE DATA SET : 9.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.60 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.46000 REMARK 200 FOR SHELL : 3.000 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: 1HRP, 1IGC, 2IMN 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): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 100 MM REMARK 280 TRIS/HCL PH 8.0, PROTEIN CONCENTRATION 3 MG/ML REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 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 Y,X,-Z REMARK 290 5555 X-Y,-Y,2/3-Z REMARK 290 6555 -X,-X+Y,1/3-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 50.03333 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 100.06667 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 100.06667 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 50.03333 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 6 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, L, H, M, I, S 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 A 1 REMARK 465 PRO A 2 REMARK 465 ASP A 3 REMARK 465 THR A 4 REMARK 465 GLN A 5 REMARK 465 SER B 1 REMARK 465 PRO B 113 REMARK 465 ARG B 114 REMARK 465 PHE B 115 REMARK 465 GLN B 116 REMARK 465 ASP B 117 REMARK 465 SER B 118 REMARK 465 SER B 119 REMARK 465 SER B 120 REMARK 465 SER B 121 REMARK 465 LYS B 122 REMARK 465 ALA B 123 REMARK 465 PRO B 124 REMARK 465 PRO B 125 REMARK 465 PRO B 126 REMARK 465 SER B 127 REMARK 465 LEU B 128 REMARK 465 PRO B 129 REMARK 465 SER B 130 REMARK 465 PRO B 131 REMARK 465 SER B 132 REMARK 465 ARG B 133 REMARK 465 LEU B 134 REMARK 465 PRO B 135 REMARK 465 GLY B 136 REMARK 465 PRO B 137 REMARK 465 SER B 138 REMARK 465 ASP B 139 REMARK 465 THR B 140 REMARK 465 PRO B 141 REMARK 465 ILE B 142 REMARK 465 LEU B 143 REMARK 465 PRO B 144 REMARK 465 GLN B 145 REMARK 465 SER L 28 REMARK 465 VAL L 29 REMARK 465 GLN H 1 REMARK 465 VAL H 2 REMARK 465 PHE H 64 REMARK 465 LYS H 65 REMARK 465 SER H 66 REMARK 465 SER I 322 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 LYS A 45 CG CD CE NZ REMARK 470 LYS B 2 CG CD CE NZ REMARK 470 ARG B 6 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 89 CG CD OE1 NE2 REMARK 470 ASP B 112 CA C O CB CG OD1 OD2 REMARK 470 ASP L 1 CG OD1 OD2 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 GLU L 27 CA C O CB CG CD OE1 REMARK 470 GLU L 27 OE2 REMARK 470 ASP L 30 CG OD1 OD2 REMARK 470 LYS L 43 CG CD CE NZ REMARK 470 ARG L 65 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 114 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 LYS H 23 CG CD CE NZ REMARK 470 GLN H 43 CG CD OE1 NE2 REMARK 470 LYS H 63 CA C O CB CG CD CE REMARK 470 LYS H 63 NZ REMARK 470 LYS H 67 CG CD CE NZ REMARK 470 GLN H 109 CG CD OE1 NE2 REMARK 470 SER H 117 OG REMARK 470 ARG M 308 CA C O CB CG CD NE REMARK 470 ARG M 308 CZ NH1 NH2 REMARK 470 SER I 321 CA C O CB OG 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 OD1 ASN H 52 OG1 THR H 53 2.01 REMARK 500 O GLY B 47 N LEU B 49 2.17 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 THR A 46 O THR A 46 6765 1.97 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 SER A 92 C SER A 92 O -0.187 REMARK 500 GLU B 3 CA GLU B 3 CB 0.137 REMARK 500 GLU B 3 CA GLU B 3 C 0.193 REMARK 500 GLU B 3 C GLU B 3 O -0.160 REMARK 500 PRO B 4 N PRO B 4 CA 0.246 REMARK 500 PRO B 4 CD PRO B 4 N -0.181 REMARK 500 PRO B 4 CA PRO B 4 C 0.144 REMARK 500 PRO B 4 C LEU B 5 N -0.292 REMARK 500 LEU B 5 C ARG B 6 N -0.233 REMARK 500 ARG B 6 C PRO B 7 N 0.380 REMARK 500 CYS B 9 CA CYS B 9 C -0.146 REMARK 500 SER L 26 C SER L 26 O -0.209 REMARK 500 ASP H 26 C TYR H 27 N -0.162 REMARK 500 TYR H 100 C GLY H 101 N -0.158 REMARK 500 ASP M 230 C SER M 231 N -0.367 REMARK 500 THR I 252 C THR I 252 O -0.318 REMARK 500 GLY I 255 CA GLY I 255 C -0.240 REMARK 500 ARG I 298 C GLN I 299 N 0.163 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 GLU B 3 N - CA - C ANGL. DEV. =-17.4 DEGREES REMARK 500 PRO B 4 N - CA - C ANGL. DEV. = 29.7 DEGREES REMARK 500 LEU B 5 CA - C - N ANGL. DEV. = 31.0 DEGREES REMARK 500 LEU B 5 O - C - N ANGL. DEV. =-59.5 DEGREES REMARK 500 CYS B 9 CA - C - N ANGL. DEV. =-18.1 DEGREES REMARK 500 ARG B 10 C - N - CA ANGL. DEV. = 18.2 DEGREES REMARK 500 LEU B 49 CA - CB - CG ANGL. DEV. = 21.0 DEGREES REMARK 500 SER L 26 O - C - N ANGL. DEV. =-78.0 DEGREES REMARK 500 ALA H 16 N - CA - C ANGL. DEV. = 19.6 DEGREES REMARK 500 ASP H 26 CB - CA - C ANGL. DEV. =-18.7 DEGREES REMARK 500 THR H 28 CB - CA - C ANGL. DEV. = 19.0 DEGREES REMARK 500 THR H 28 N - CA - CB ANGL. DEV. =-26.4 DEGREES REMARK 500 ASN H 102 CA - CB - CG ANGL. DEV. = 24.5 DEGREES REMARK 500 ASP M 230 CA - C - N ANGL. DEV. = 33.5 DEGREES REMARK 500 ASP M 230 O - C - N ANGL. DEV. =-31.6 DEGREES REMARK 500 SER M 231 C - N - CA ANGL. DEV. = 44.9 DEGREES REMARK 500 GLY I 255 N - CA - C ANGL. DEV. = 18.7 DEGREES 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 ARG B 6 PRO B 7 -140.04 REMARK 500 ASP H 26 TYR H 27 144.12 REMARK 500 ASP M 230 SER M 231 52.92 DBREF 1QFW A 1 92 UNP P01215 GLHA_HUMAN 25 116 DBREF 1QFW B 1 145 UNP P01233 CGHB_HUMAN 1 145 SEQADV 1QFW THR A 4 UNP P01215 VAL 28 CONFLICT SEQRES 1 A 92 ALA PRO ASP THR GLN ASP CYS PRO GLU CYS THR LEU GLN SEQRES 2 A 92 GLU ASN PRO PHE PHE SER GLN PRO GLY ALA PRO ILE LEU SEQRES 3 A 92 GLN CYS MET GLY CYS CYS PHE SER ARG ALA TYR PRO THR SEQRES 4 A 92 PRO LEU ARG SER LYS LYS THR MET LEU VAL GLN LYS ASN SEQRES 5 A 92 VAL THR SER GLU SER THR CYS CYS VAL ALA LYS SER TYR SEQRES 6 A 92 ASN ARG VAL THR VAL MET GLY GLY PHE LYS VAL GLU ASN SEQRES 7 A 92 HIS THR ALA CYS HIS CYS SER THR CYS TYR TYR HIS LYS SEQRES 8 A 92 SER SEQRES 1 B 145 SER LYS GLU PRO LEU ARG PRO ARG CYS ARG PRO ILE ASN SEQRES 2 B 145 ALA THR LEU ALA VAL GLU LYS GLU GLY CYS PRO VAL CYS SEQRES 3 B 145 ILE THR VAL ASN THR THR ILE CYS ALA GLY TYR CYS PRO SEQRES 4 B 145 THR MET THR ARG VAL LEU GLN GLY VAL LEU PRO ALA LEU SEQRES 5 B 145 PRO GLN VAL VAL CYS ASN TYR ARG ASP VAL ARG PHE GLU SEQRES 6 B 145 SER ILE ARG LEU PRO GLY CYS PRO ARG GLY VAL ASN PRO SEQRES 7 B 145 VAL VAL SER TYR ALA VAL ALA LEU SER CYS GLN CYS ALA SEQRES 8 B 145 LEU CYS ARG ARG SER THR THR ASP CYS GLY GLY PRO LYS SEQRES 9 B 145 ASP HIS PRO LEU THR CYS ASP ASP PRO ARG PHE GLN ASP SEQRES 10 B 145 SER SER SER SER LYS ALA PRO PRO PRO SER LEU PRO SER SEQRES 11 B 145 PRO SER ARG LEU PRO GLY PRO SER ASP THR PRO ILE LEU SEQRES 12 B 145 PRO GLN SEQRES 1 L 114 ASP ILE GLU LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 L 114 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 L 114 GLU SER VAL ASP SER TYR GLY ASN SER PHE MET GLN TRP SEQRES 4 L 114 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 L 114 TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 L 114 PHE SER GLY THR GLY SER ARG THR ASP PHE THR LEU THR SEQRES 7 L 114 ILE ASN PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR SEQRES 8 L 114 CYS GLN GLN SER ASP GLU TYR PRO TYR MET TYR THR PHE SEQRES 9 L 114 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG SEQRES 1 H 117 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 H 117 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER ASP SEQRES 3 H 117 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 H 117 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN SEQRES 5 H 117 PRO THR ASN GLY ARG THR TYR TYR ASN GLU LYS PHE LYS SEQRES 6 H 117 SER LYS ALA THR LEU THR VAL ALA ALA SER ALA SER THR SEQRES 7 H 117 ALA ALA MET GLN ALA SER SER LEU THR SER GLU ASP SER SEQRES 8 H 117 ALA VAL TYR TYR CYS ALA ARG ARG TYR GLY ASN SER PHE SEQRES 9 H 117 ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 M 108 ASP ILE GLU LEU THR GLN SER PRO LYS SER MET SER MET SEQRES 2 M 108 SER VAL GLY GLU ARG VAL THR LEU SER CYS LYS ALA SER SEQRES 3 M 108 GLU THR VAL ASP SER PHE VAL SER TRP TYR GLN GLN LYS SEQRES 4 M 108 PRO GLU GLN SER PRO LYS LEU LEU ILE PHE GLY ALA SER SEQRES 5 M 108 ASN ARG PHE SER GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 M 108 GLY SER ALA THR ASP PHE THR LEU THR ILE SER SER VAL SEQRES 7 M 108 GLN ALA GLU ASP PHE ALA ASP TYR HIS CYS GLY GLN THR SEQRES 8 M 108 TYR ASN HIS PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 M 108 GLU ILE LYS ARG SEQRES 1 I 122 GLN VAL GLN LEU GLN GLU SER GLY GLY HIS LEU VAL LYS SEQRES 2 I 122 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 I 122 PHE ALA PHE SER SER PHE ASP MET SER TRP ILE ARG GLN SEQRES 4 I 122 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA SER ILE THR SEQRES 5 I 122 ASN VAL GLY THR TYR THR TYR TYR PRO GLY SER VAL LYS SEQRES 6 I 122 GLY ARG PHE SER ILE SER ARG ASP ASN ALA ARG ASN THR SEQRES 7 I 122 LEU ASN LEU GLN MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 I 122 ALA LEU TYR PHE CYS ALA ARG GLN GLY THR ALA ALA GLN SEQRES 9 I 122 PRO TYR TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR SEQRES 10 I 122 VAL THR VAL SER SER MODRES 1QFW ASN A 52 ASN GLYCOSYLATION SITE MODRES 1QFW ASN A 78 ASN GLYCOSYLATION SITE HET NAG S 1 14 HET NAG S 11 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETSYN NAG NAG FORMUL 7 NAG 2(C8 H15 N O6) HELIX 1 1 PRO A 40 LYS A 45 1 6 HELIX 2 2 THR H 28 TYR H 32 5 5 HELIX 3 3 ALA I 228 PHE I 232 5 5 HELIX 4 4 ARG I 287 THR I 291 5 5 SHEET 1 A 4 LYS A 75 THR A 86 0 SHEET 2 A 4 VAL A 53 THR A 69 -1 N CYS A 59 O SER A 85 SHEET 3 A 4 LEU A 26 PRO A 38 -1 O PHE A 33 N THR A 58 SHEET 4 A 4 THR A 11 GLU A 14 -1 O THR A 11 N MET A 29 SHEET 1 B 5 LYS A 75 THR A 86 0 SHEET 2 B 5 VAL A 53 THR A 69 -1 N CYS A 59 O SER A 85 SHEET 3 B 5 LEU A 26 PRO A 38 -1 O PHE A 33 N THR A 58 SHEET 4 B 5 ILE B 27 MET B 41 -1 O CYS B 34 N ALA A 36 SHEET 5 B 5 ARG B 10 VAL B 18 -1 N ARG B 10 O ALA B 35 SHEET 1 C 2 LYS A 91 SER A 92 0 SHEET 2 C 2 CYS B 93 ARG B 94 1 O CYS B 93 N SER A 92 SHEET 1 D 2 VAL B 56 ARG B 68 0 SHEET 2 D 2 VAL B 79 ALA B 91 -1 N VAL B 80 O ILE B 67 SHEET 1 E 4 THR L 5 GLN L 6 0 SHEET 2 E 4 CYS L 23 ARG L 24 -1 N ARG L 24 O THR L 5 SHEET 3 E 4 ASP L 74 THR L 78 -1 N PHE L 75 O CYS L 23 SHEET 4 E 4 SER L 67 THR L 69 -1 O SER L 67 N THR L 78 SHEET 1 F 2 SER L 10 SER L 14 0 SHEET 2 F 2 LYS L 109 LYS L 113 1 O LYS L 109 N LEU L 11 SHEET 1 G 4 LEU L 50 ILE L 52 0 SHEET 2 G 4 SER L 35 GLN L 42 -1 O TRP L 39 N LEU L 51 SHEET 3 G 4 THR L 89 ASP L 96 -1 O THR L 89 N GLN L 42 SHEET 4 G 4 TYR L 102 PHE L 104 -1 O THR L 103 N GLN L 94 SHEET 1 H 4 LEU H 4 SER H 7 0 SHEET 2 H 4 SER H 21 ALA H 24 -1 O SER H 21 N SER H 7 SHEET 3 H 4 THR H 78 ALA H 79 -1 O ALA H 79 N CYS H 22 SHEET 4 H 4 VAL H 72 ALA H 73 -1 N ALA H 73 O THR H 78 SHEET 1 I 2 SER H 17 VAL H 18 0 SHEET 2 I 2 ALA H 83 SER H 84 -1 O ALA H 83 N VAL H 18 SHEET 1 J 4 THR H 57 TYR H 59 0 SHEET 2 J 4 LEU H 45 ILE H 51 -1 N GLU H 50 O TYR H 59 SHEET 3 J 4 HIS H 35 GLN H 39 -1 O TRP H 36 N ILE H 48 SHEET 4 J 4 VAL H 93 ALA H 97 -1 O VAL H 93 N GLN H 39 SHEET 1 K 4 LEU M 204 SER M 207 0 SHEET 2 K 4 VAL M 219 ALA M 225 -1 N SER M 222 O SER M 207 SHEET 3 K 4 ASP M 270 ILE M 275 -1 N PHE M 271 O CYS M 223 SHEET 4 K 4 PHE M 262 THR M 263 -1 N THR M 263 O THR M 274 SHEET 1 L 4 LYS M 245 ILE M 248 0 SHEET 2 L 4 VAL M 233 GLN M 238 -1 O TRP M 235 N LEU M 247 SHEET 3 L 4 ASP M 285 GLN M 290 -1 N ASP M 285 O GLN M 238 SHEET 4 L 4 THR M 297 PHE M 298 -1 O THR M 297 N GLN M 290 SHEET 1 M 5 LYS M 245 ILE M 248 0 SHEET 2 M 5 VAL M 233 GLN M 238 -1 O TRP M 235 N LEU M 247 SHEET 3 M 5 ASP M 285 GLN M 290 -1 N ASP M 285 O GLN M 238 SHEET 4 M 5 THR M 302 GLU M 305 -1 O THR M 302 N TYR M 286 SHEET 5 M 5 MET M 211 SER M 212 1 O MET M 211 N GLU M 305 SHEET 1 N 4 LEU I 204 SER I 207 0 SHEET 2 N 4 LEU I 218 ALA I 224 -1 N SER I 221 O SER I 207 SHEET 3 N 4 THR I 278 MET I 283 -1 O LEU I 279 N CYS I 222 SHEET 4 N 4 PHE I 268 ILE I 270 -1 O SER I 269 N GLN I 282 SHEET 1 O 4 LEU I 245 TRP I 247 0 SHEET 2 O 4 MET I 234 GLN I 239 -1 N ARG I 238 O GLU I 246 SHEET 3 O 4 ALA I 292 ARG I 298 -1 N LEU I 293 O GLN I 239 SHEET 4 O 4 THR I 317 VAL I 318 -1 N VAL I 318 O ALA I 292 SHEET 1 P 2 SER I 250 ILE I 251 0 SHEET 2 P 2 THR I 258 TYR I 259 -1 N TYR I 259 O SER I 250 SSBOND 1 CYS A 7 CYS A 31 SSBOND 2 CYS A 10 CYS A 60 SSBOND 3 CYS A 28 CYS A 82 SSBOND 4 CYS A 32 CYS A 84 SSBOND 5 CYS A 59 CYS A 87 SSBOND 6 CYS B 9 CYS B 57 SSBOND 7 CYS B 23 CYS B 72 SSBOND 8 CYS B 26 CYS B 110 SSBOND 9 CYS B 34 CYS B 88 SSBOND 10 CYS B 38 CYS B 90 SSBOND 11 CYS B 93 CYS B 100 SSBOND 12 CYS L 23 CYS L 92 SSBOND 13 CYS H 22 CYS H 96 SSBOND 14 CYS M 223 CYS M 288 SSBOND 15 CYS I 222 CYS I 296 LINK ND2 ASN A 52 C1 NAG S 1 LINK ND2 ASN A 78 C1 NAG S 11 CISPEP 1 SER M 207 PRO M 208 0 0.09 CISPEP 2 HIS M 294 PRO M 295 0 -0.53 CRYST1 104.900 104.900 150.100 90.00 90.00 120.00 P 31 2 1 6 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 0.009533 0.005504 0.000000 0.00000 SCALE2 0.000000 0.011008 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006662 0.00000