REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.KUROKI,M.HIROSE,Y.KATO,M.D.FEESE,T.TAMADA, REMARK 1 AUTH 2 H.SHIGEMATSU,H.WATARAI,Y.MAEDA,T.TAHARA,T.KATO, REMARK 1 AUTH 3 H.MIYAZAKI REMARK 1 TITL CRYSTALLIZATION OF THE FUNCTIONAL DOMAIN OF HUMAN REMARK 1 TITL 2 THROMBOPOIETIN USING AN ANTIGEN-BINDING FRAGMENT REMARK 1 TITL 3 DERIVED FROM NEUTRALIZING MONOCLONAL ANTIBODY REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 856 2002 REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 11976502 REMARK 1 DOI 10.1107/S0907444902004791 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.19 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) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.63 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 34015 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) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.305 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1801 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.38 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2479 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.1830 REMARK 3 BIN FREE R VALUE SET COUNT : 125 REMARK 3 BIN FREE R VALUE : 0.3780 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 17297 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 169 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 36.60 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.77 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.72000 REMARK 3 B22 (A**2) : 2.25000 REMARK 3 B33 (A**2) : -0.53000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.33000 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): 0.737 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.581 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.656 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.770 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17722 ; 0.028 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24136 ; 2.768 ; 1.954 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2266 ;11.133 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2752 ; 0.173 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13236 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 10891 ; 0.337 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1057 ; 0.269 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 89 ; 0.329 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.340 ; 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): 11334 ; 1.029 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18321 ; 1.934 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6388 ; 2.827 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5815 ; 4.777 ; 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 : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1V7N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-DEC-03. REMARK 100 THE RCSB ID CODE IS RCSB006308. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-98 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-6B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : SI REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : WEISSENBERG REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35598 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 60.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -0.500 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 1.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09800 REMARK 200 FOR THE DATA SET : 3.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.21400 REMARK 200 FOR SHELL : 1.100 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 1IAI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.88 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.1M POTASSIUM REMARK 280 PHOSPHATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 23.29100 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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, V 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, I, X 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, J, Y 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, K, 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 CYS M 213 REMARK 465 CYS N 213 REMARK 465 SER V 1 REMARK 465 PRO V 2 REMARK 465 ALA V 3 REMARK 465 PRO V 4 REMARK 465 PRO V 5 REMARK 465 ALA V 6 REMARK 465 VAL V 152 REMARK 465 ARG V 153 REMARK 465 ARG V 154 REMARK 465 ALA V 155 REMARK 465 PRO V 156 REMARK 465 PRO V 157 REMARK 465 THR V 158 REMARK 465 THR V 159 REMARK 465 ALA V 160 REMARK 465 VAL V 161 REMARK 465 PRO V 162 REMARK 465 SER V 163 REMARK 465 SER X 1 REMARK 465 PRO X 2 REMARK 465 ALA X 3 REMARK 465 PRO X 4 REMARK 465 PRO X 5 REMARK 465 ALA X 6 REMARK 465 CYS X 7 REMARK 465 GLY X 146 REMARK 465 GLY X 147 REMARK 465 SER X 148 REMARK 465 THR X 149 REMARK 465 LEU X 150 REMARK 465 CYS X 151 REMARK 465 VAL X 152 REMARK 465 ARG X 153 REMARK 465 ARG X 154 REMARK 465 ALA X 155 REMARK 465 PRO X 156 REMARK 465 PRO X 157 REMARK 465 THR X 158 REMARK 465 THR X 159 REMARK 465 ALA X 160 REMARK 465 VAL X 161 REMARK 465 PRO X 162 REMARK 465 SER X 163 REMARK 465 SER Y 1 REMARK 465 PRO Y 2 REMARK 465 ALA Y 3 REMARK 465 PRO Y 4 REMARK 465 PRO Y 5 REMARK 465 ALA Y 6 REMARK 465 CYS Y 7 REMARK 465 GLY Y 147 REMARK 465 SER Y 148 REMARK 465 THR Y 149 REMARK 465 LEU Y 150 REMARK 465 CYS Y 151 REMARK 465 VAL Y 152 REMARK 465 ARG Y 153 REMARK 465 ARG Y 154 REMARK 465 ALA Y 155 REMARK 465 PRO Y 156 REMARK 465 PRO Y 157 REMARK 465 THR Y 158 REMARK 465 THR Y 159 REMARK 465 ALA Y 160 REMARK 465 VAL Y 161 REMARK 465 PRO Y 162 REMARK 465 SER Y 163 REMARK 465 SER Z 1 REMARK 465 PRO Z 2 REMARK 465 ALA Z 3 REMARK 465 PRO Z 4 REMARK 465 PRO Z 5 REMARK 465 ALA Z 6 REMARK 465 CYS Z 7 REMARK 465 ASP Z 8 REMARK 465 GLY Z 147 REMARK 465 SER Z 148 REMARK 465 THR Z 149 REMARK 465 LEU Z 150 REMARK 465 CYS Z 151 REMARK 465 VAL Z 152 REMARK 465 ARG Z 153 REMARK 465 ARG Z 154 REMARK 465 ALA Z 155 REMARK 465 PRO Z 156 REMARK 465 PRO Z 157 REMARK 465 THR Z 158 REMARK 465 THR Z 159 REMARK 465 ALA Z 160 REMARK 465 VAL Z 161 REMARK 465 PRO Z 162 REMARK 465 SER Z 163 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 GLU H 1 CG CD OE1 OE2 REMARK 470 LYS H 208 CG CD CE NZ REMARK 470 LYS H 212 CG CD CE NZ REMARK 470 GLU I 1 CG CD OE1 OE2 REMARK 470 LYS I 208 CG CD CE NZ REMARK 470 LYS I 212 CG CD CE NZ REMARK 470 GLU J 1 CG CD OE1 OE2 REMARK 470 LYS J 208 CG CD CE NZ REMARK 470 LYS J 212 CG CD CE NZ REMARK 470 GLU K 1 CG CD OE1 OE2 REMARK 470 LYS K 208 CG CD CE NZ REMARK 470 LYS K 212 CG CD CE NZ REMARK 470 ARG V 10 CG CD NE CZ NH1 NH2 REMARK 470 LYS V 14 CG CD CE NZ REMARK 470 ARG X 10 CG CD NE CZ NH1 NH2 REMARK 470 LYS X 14 CG CD CE NZ REMARK 470 ARG Y 10 CG CD NE CZ NH1 NH2 REMARK 470 LYS Y 14 CG CD CE NZ REMARK 470 ARG Z 10 CG CD NE CZ NH1 NH2 REMARK 470 LYS Z 14 CG CD CE NZ 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 NH2 ARG O 90 O SER K 102 1.74 REMARK 500 O ILE N 149 O SER N 190 1.83 REMARK 500 O GLY J 130 N ALA J 133 1.89 REMARK 500 CB SER H 189 O HOH H 224 1.95 REMARK 500 O HIS O 197 N THR O 199 1.96 REMARK 500 N VAL L 131 O LEU L 178 1.98 REMARK 500 CA SER H 189 O HOH H 224 2.00 REMARK 500 NE2 GLN M 123 OG SER M 130 2.03 REMARK 500 O SER M 120 N GLU M 122 2.08 REMARK 500 OD2 ASP M 169 OG1 THR M 171 2.08 REMARK 500 OG1 THR M 192 OG SER M 207 2.08 REMARK 500 CE MET J 85 CE1 TYR J 96 2.09 REMARK 500 O PRO J 187 OG1 THR J 190 2.09 REMARK 500 OD1 ASN N 160 OG SER N 176 2.10 REMARK 500 O GLN H 174 N ASP H 176 2.11 REMARK 500 O ASN I 158 N GLY I 160 2.12 REMARK 500 O ILE L 149 O SER L 190 2.12 REMARK 500 O GLN X 61 N LEU X 64 2.12 REMARK 500 NH2 ARG M 107 OE2 GLU N 78 2.13 REMARK 500 O PRO Y 124 N ALA Y 126 2.13 REMARK 500 O THR J 156 N ASN J 199 2.14 REMARK 500 O GLY K 100 N LEU K 104 2.15 REMARK 500 O ASP I 76 N SER I 79 2.15 REMARK 500 O PHE H 169 O HOH H 233 2.17 REMARK 500 O ASP I 92 OH TYR I 96 2.17 REMARK 500 N LEU Z 35 O LYS Z 122 2.17 REMARK 500 OG SER I 206 O HOH I 243 2.17 REMARK 500 O TYR L 185 OH TYR L 191 2.18 REMARK 500 OE1 GLU M 104 O HOH M 229 2.19 REMARK 500 O SER H 189 OG SER H 193 2.19 REMARK 500 O GLN V 61 N GLY V 65 2.19 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 NH2 ARG L 62 O HOH V 165 1545 2.19 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 TYR L 48 CE2 TYR L 48 CD2 -0.114 REMARK 500 TYR L 139 CB TYR L 139 CG -0.166 REMARK 500 TYR L 139 CD1 TYR L 139 CE1 -0.092 REMARK 500 TYR L 139 CE2 TYR L 139 CD2 -0.097 REMARK 500 TYR H 97 CD1 TYR H 97 CE1 -0.091 REMARK 500 CYS H 98 CB CYS H 98 SG -0.113 REMARK 500 GLU H 151 CD GLU H 151 OE2 0.095 REMARK 500 ALA M 59 CA ALA M 59 CB -0.138 REMARK 500 CYS J 143 CB CYS J 143 SG -0.121 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 ASP L 81 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES REMARK 500 ARG L 95 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARG L 95 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG L 154 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 VAL L 205 CB - CA - C ANGL. DEV. = -14.7 DEGREES REMARK 500 ASP H 76 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 PRO H 122 N - CD - CG ANGL. DEV. = -9.7 DEGREES REMARK 500 CYS H 143 CA - CB - SG ANGL. DEV. = -15.5 DEGREES REMARK 500 LEU H 144 CA - CB - CG ANGL. DEV. = -21.6 DEGREES REMARK 500 LEU H 162 CB - CG - CD1 ANGL. DEV. = -12.5 DEGREES REMARK 500 ASP H 176 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES REMARK 500 ALA H 204 N - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 ALA H 204 C - N - CA ANGL. DEV. = 15.2 DEGREES REMARK 500 ARG H 216 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG M 60 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES REMARK 500 ASP M 81 CB - CG - OD1 ANGL. DEV. = -7.7 DEGREES REMARK 500 ASP M 81 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES REMARK 500 ASP M 142 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES REMARK 500 ASP M 150 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES REMARK 500 ASP M 169 CB - CG - OD2 ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP M 183 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 ASP I 35 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 LEU I 83 CA - CB - CG ANGL. DEV. = -21.5 DEGREES REMARK 500 ASP I 176 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 CYS I 198 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 PRO I 203 N - CD - CG ANGL. DEV. = -12.6 DEGREES REMARK 500 PRO N 8 N - CD - CG ANGL. DEV. = -13.0 DEGREES REMARK 500 ASP N 81 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES REMARK 500 ASP N 109 CB - CG - OD1 ANGL. DEV. = -6.7 DEGREES REMARK 500 ASP N 109 CB - CG - OD2 ANGL. DEV. = 8.9 DEGREES REMARK 500 ASP N 142 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES REMARK 500 ASP N 150 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES REMARK 500 ASP N 166 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES REMARK 500 ASP J 31 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 ASP J 76 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES REMARK 500 ARG J 89 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 VAL J 139 CB - CA - C ANGL. DEV. = -11.5 DEGREES REMARK 500 VAL J 145 N - CA - C ANGL. DEV. = -18.4 DEGREES REMARK 500 ASP J 176 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES REMARK 500 LEU O 53 CA - CB - CG ANGL. DEV. = -25.6 DEGREES REMARK 500 LEU O 72 CB - CG - CD1 ANGL. DEV. = -10.4 DEGREES REMARK 500 ASP O 109 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 ASP O 150 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 ASP O 164 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES REMARK 500 ASP O 183 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 ASP K 31 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 ASP K 76 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES REMARK 500 SER K 175 N - CA - CB ANGL. DEV. = -12.3 DEGREES REMARK 500 PRO K 192 N - CD - CG ANGL. DEV. = -10.3 DEGREES REMARK 500 HIS K 202 N - CA - C ANGL. DEV. = -18.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 68 ANGLE DEVIATIONS. 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 SER L 7 -84.78 -53.48 REMARK 500 PRO L 15 126.06 -25.29 REMARK 500 SER L 28 131.16 -31.60 REMARK 500 THR L 50 -38.62 61.80 REMARK 500 SER L 51 20.07 -152.91 REMARK 500 SER L 66 135.11 -173.07 REMARK 500 THR L 68 -19.04 -142.00 REMARK 500 ALA L 82 109.23 -52.43 REMARK 500 ALA L 83 172.65 179.53 REMARK 500 PHE L 97 -152.01 -109.02 REMARK 500 ARG L 107 -149.58 -61.98 REMARK 500 ALA L 110 99.19 -167.64 REMARK 500 TYR L 139 122.26 -178.27 REMARK 500 PRO L 140 -166.75 -67.26 REMARK 500 ILE L 149 -102.38 -94.52 REMARK 500 LYS L 168 -71.89 -64.44 REMARK 500 LEU L 180 -165.14 -121.97 REMARK 500 LYS L 182 -71.30 -59.81 REMARK 500 GLU L 212 83.45 99.48 REMARK 500 PRO H 14 153.81 -34.44 REMARK 500 THR H 28 66.36 -5.33 REMARK 500 GLU H 42 -71.79 -65.75 REMARK 500 LYS H 67 118.34 -28.59 REMARK 500 ALA H 90 -32.27 -34.93 REMARK 500 ASP H 92 3.57 -55.32 REMARK 500 TRP H 101 -138.69 -90.98 REMARK 500 TRP H 106 97.00 -164.90 REMARK 500 SER H 115 135.64 177.34 REMARK 500 PRO H 121 155.27 -45.75 REMARK 500 SER H 131 27.90 -70.73 REMARK 500 ALA H 132 14.16 -172.15 REMARK 500 ALA H 133 160.32 -31.50 REMARK 500 ASN H 136 -150.41 -94.28 REMARK 500 SER H 159 44.36 32.90 REMARK 500 GLN H 174 -125.32 -108.92 REMARK 500 SER H 175 69.13 -58.19 REMARK 500 ASP H 176 38.01 28.78 REMARK 500 PRO H 192 30.86 -85.20 REMARK 500 PRO H 203 95.20 -39.19 REMARK 500 ALA H 204 -2.75 165.12 REMARK 500 SER H 205 12.64 50.25 REMARK 500 THR H 207 83.25 -173.02 REMARK 500 VAL H 209 55.56 -117.25 REMARK 500 PRO M 39 119.21 -22.65 REMARK 500 SER M 49 59.99 38.90 REMARK 500 THR M 50 -29.97 68.17 REMARK 500 SER M 51 -1.54 -153.56 REMARK 500 SER M 55 97.11 -64.80 REMARK 500 ALA M 59 27.47 -68.61 REMARK 500 SER M 69 76.34 -153.15 REMARK 500 SER M 71 125.24 178.61 REMARK 500 ALA M 79 -68.01 -24.84 REMARK 500 ALA M 82 104.57 -52.56 REMARK 500 ARG M 90 11.52 -153.03 REMARK 500 ARG M 107 -160.22 -78.61 REMARK 500 PRO M 119 158.35 -48.92 REMARK 500 SER M 121 -20.08 -26.82 REMARK 500 THR M 125 -5.36 -46.63 REMARK 500 CYS M 133 115.60 -171.93 REMARK 500 ASN M 137 72.22 56.37 REMARK 500 ILE M 149 -84.24 -74.46 REMARK 500 SER M 167 -36.93 -25.44 REMARK 500 ASN M 189 -33.40 -136.51 REMARK 500 TYR M 191 88.96 178.41 REMARK 500 PHE M 208 169.44 174.94 REMARK 500 PRO I 14 130.77 -22.26 REMARK 500 SER I 25 126.63 -173.61 REMARK 500 HIS I 58 26.79 47.21 REMARK 500 SER I 65 24.33 -49.04 REMARK 500 VAL I 66 -25.58 -160.63 REMARK 500 LYS I 67 81.71 -50.21 REMARK 500 ARG I 69 -67.74 -100.51 REMARK 500 THR I 71 77.43 -160.63 REMARK 500 SER I 77 -37.97 -30.30 REMARK 500 SER I 87 74.79 48.36 REMARK 500 TRP I 101 -117.31 -73.39 REMARK 500 SER I 131 -86.69 46.30 REMARK 500 ALA I 132 63.22 -107.83 REMARK 500 ASN I 136 -149.67 -138.91 REMARK 500 LEU I 141 -161.57 -120.75 REMARK 500 PRO I 150 -142.16 -103.30 REMARK 500 ASN I 158 92.14 59.74 REMARK 500 SER I 159 56.04 -10.52 REMARK 500 SER I 163 -5.40 -167.02 REMARK 500 GLN I 174 -123.67 -108.61 REMARK 500 SER I 175 66.86 -55.93 REMARK 500 ASP I 176 63.51 19.52 REMARK 500 VAL I 184 133.07 166.90 REMARK 500 SER I 189 -15.55 -48.76 REMARK 500 PRO I 192 30.11 -90.96 REMARK 500 SER I 193 -87.45 -48.76 REMARK 500 HIS I 202 117.06 -164.44 REMARK 500 ALA I 204 54.76 97.92 REMARK 500 SER I 205 34.17 -27.66 REMARK 500 THR I 207 78.12 -156.43 REMARK 500 LYS I 212 125.12 -39.04 REMARK 500 SER N 27 116.02 -168.55 REMARK 500 SER N 28 131.43 -15.71 REMARK 500 PRO N 39 122.34 -29.36 REMARK 500 LEU N 45 122.81 -22.76 REMARK 500 SER N 49 52.39 78.96 REMARK 500 THR N 50 -32.07 76.84 REMARK 500 SER N 51 -5.97 -155.24 REMARK 500 SER N 66 151.55 177.80 REMARK 500 TYR N 70 -164.58 -101.00 REMARK 500 SER N 71 121.99 156.88 REMARK 500 GLU N 80 -4.99 -54.85 REMARK 500 ALA N 83 177.22 178.63 REMARK 500 ARG N 90 22.30 -145.71 REMARK 500 ASP N 109 148.25 -31.67 REMARK 500 SER N 121 -70.95 -52.30 REMARK 500 GLU N 122 -33.61 -33.45 REMARK 500 THR N 125 -10.88 -41.72 REMARK 500 ASN N 137 89.30 -4.21 REMARK 500 PRO N 140 178.10 -57.81 REMARK 500 ILE N 149 -79.16 -95.96 REMARK 500 ASP N 150 30.69 -95.37 REMARK 500 GLN N 165 148.37 -38.06 REMARK 500 SER N 167 -49.89 -17.80 REMARK 500 ASP N 169 75.55 -164.42 REMARK 500 SER N 170 61.52 -47.16 REMARK 500 LYS N 182 -72.73 -41.01 REMARK 500 ASN N 189 -71.10 -139.68 REMARK 500 ARG N 210 -72.49 -71.90 REMARK 500 CYS J 22 86.18 -172.57 REMARK 500 PHE J 27 149.38 158.00 REMARK 500 THR J 28 99.79 -62.73 REMARK 500 SER J 30 -32.94 -3.86 REMARK 500 GLU J 42 -76.32 -40.95 REMARK 500 ARG J 52 164.36 -27.60 REMARK 500 VAL J 55 -29.79 -29.40 REMARK 500 ASN J 56 51.17 -119.23 REMARK 500 ASN J 57 51.67 37.85 REMARK 500 HIS J 58 12.09 55.67 REMARK 500 SER J 65 -54.04 -4.75 REMARK 500 ARG J 69 -52.85 -126.44 REMARK 500 THR J 71 107.56 -167.43 REMARK 500 SER J 87 68.95 31.37 REMARK 500 ARG J 89 -148.26 -67.59 REMARK 500 SER J 102 60.59 67.78 REMARK 500 SER J 115 116.11 -162.23 REMARK 500 ALA J 116 -79.96 11.97 REMARK 500 ALA J 117 156.99 -43.69 REMARK 500 SER J 131 -48.03 -2.07 REMARK 500 ALA J 133 170.96 56.71 REMARK 500 ASN J 136 -157.33 -69.06 REMARK 500 ASN J 158 37.85 39.74 REMARK 500 GLN J 174 -104.65 -106.17 REMARK 500 ASP J 176 50.82 26.53 REMARK 500 PRO J 192 0.96 -64.39 REMARK 500 SER J 193 -73.71 -34.28 REMARK 500 ALA J 204 13.44 121.18 REMARK 500 VAL J 214 118.45 -34.00 REMARK 500 ARG J 216 96.76 -16.49 REMARK 500 SER O 7 -88.43 -75.15 REMARK 500 CYS O 23 122.93 175.35 REMARK 500 TRP O 46 -75.31 -87.00 REMARK 500 THR O 50 -40.69 62.96 REMARK 500 SER O 51 32.81 -149.55 REMARK 500 SER O 55 110.38 -23.61 REMARK 500 SER O 71 109.88 -167.62 REMARK 500 GLU O 80 30.06 -82.73 REMARK 500 ARG O 107 -149.60 -86.98 REMARK 500 PRO O 112 132.83 -39.62 REMARK 500 SER O 121 -31.68 -31.97 REMARK 500 SER O 126 31.35 -79.31 REMARK 500 VAL O 131 78.00 -113.34 REMARK 500 ASN O 137 71.51 56.79 REMARK 500 PRO O 140 -171.37 -55.43 REMARK 500 ILE O 149 -98.10 -84.71 REMARK 500 ASP O 169 34.16 -159.31 REMARK 500 SER O 170 24.04 37.85 REMARK 500 MET O 174 133.30 -171.92 REMARK 500 TYR O 191 105.02 -160.69 REMARK 500 LYS O 198 -48.92 23.51 REMARK 500 PRO O 203 102.04 -27.94 REMARK 500 ILE O 204 94.14 -56.26 REMARK 500 GLU O 212 56.60 15.50 REMARK 500 PRO K 14 153.40 -31.07 REMARK 500 PHE K 27 111.82 141.46 REMARK 500 THR K 28 102.79 -12.06 REMARK 500 SER K 30 -26.89 -39.75 REMARK 500 PRO K 41 -5.83 -57.12 REMARK 500 GLU K 42 -79.27 -95.33 REMARK 500 VAL K 48 -62.88 -105.13 REMARK 500 ARG K 52 159.31 -49.32 REMARK 500 LYS K 54 -71.06 -40.31 REMARK 500 VAL K 55 -9.39 -43.30 REMARK 500 ASN K 57 45.30 114.16 REMARK 500 HIS K 58 17.18 37.17 REMARK 500 ALA K 59 144.59 -33.52 REMARK 500 SER K 65 -6.60 -34.70 REMARK 500 SER K 87 97.40 41.53 REMARK 500 ARG K 89 -160.45 -106.51 REMARK 500 ALA K 90 -61.42 -90.43 REMARK 500 GLU K 91 0.50 -52.33 REMARK 500 SER K 115 137.70 178.77 REMARK 500 ALA K 117 152.32 -32.22 REMARK 500 THR K 119 89.70 -60.88 REMARK 500 ALA K 133 141.92 -36.85 REMARK 500 ASN K 136 -81.74 -145.46 REMARK 500 SER K 159 66.49 23.73 REMARK 500 HIS K 167 88.78 -171.17 REMARK 500 GLN K 174 -106.07 -114.32 REMARK 500 ASP K 176 47.41 23.93 REMARK 500 PRO K 203 18.46 37.17 REMARK 500 ALA K 204 18.47 -173.51 REMARK 500 VAL V 11 -86.95 -48.86 REMARK 500 LEU V 16 -68.91 -29.07 REMARK 500 LEU V 22 -71.78 -58.48 REMARK 500 HIS V 23 -54.38 -27.89 REMARK 500 ARG V 25 -14.39 -49.95 REMARK 500 SER V 27 -39.79 -26.15 REMARK 500 PRO V 30 -166.45 -31.46 REMARK 500 GLU V 31 96.98 -46.17 REMARK 500 PRO V 34 -154.80 -62.52 REMARK 500 PRO V 38 139.73 -37.30 REMARK 500 ALA V 43 170.40 -42.12 REMARK 500 PHE V 46 -72.87 -107.80 REMARK 500 GLU V 50 -28.20 -28.56 REMARK 500 TRP V 51 -70.06 -72.10 REMARK 500 LYS V 52 -8.44 -59.64 REMARK 500 GLN V 54 155.35 138.86 REMARK 500 ALA V 76 -38.58 -30.37 REMARK 500 GLN V 80 -72.74 -2.71 REMARK 500 PRO V 83 22.00 -77.91 REMARK 500 SER V 87 -80.70 -18.39 REMARK 500 SER V 88 -8.53 -45.14 REMARK 500 ALA V 103 -51.82 4.29 REMARK 500 LEU V 129 -70.26 -42.60 REMARK 500 LYS V 138 -36.43 -26.01 REMARK 500 VAL V 139 -71.31 -65.46 REMARK 500 PHE V 141 -17.12 -44.70 REMARK 500 LEU V 144 -99.39 -69.94 REMARK 500 VAL V 145 94.99 -30.08 REMARK 500 SER V 148 55.70 -14.58 REMARK 500 THR V 149 -166.74 -68.91 REMARK 500 ARG X 10 -21.62 -34.88 REMARK 500 VAL X 11 -82.38 -51.54 REMARK 500 LEU X 22 -70.12 -58.89 REMARK 500 HIS X 23 -37.91 -36.70 REMARK 500 ARG X 25 -27.20 -35.76 REMARK 500 SER X 27 -80.34 -21.59 REMARK 500 PRO X 30 -176.03 -63.04 REMARK 500 GLU X 31 79.25 -21.66 REMARK 500 PRO X 34 -159.62 -59.38 REMARK 500 PRO X 36 -34.42 -32.16 REMARK 500 VAL X 44 99.76 -46.24 REMARK 500 THR X 53 48.50 -86.90 REMARK 500 GLN X 61 -77.46 -61.81 REMARK 500 ASP X 62 -61.10 -13.10 REMARK 500 SER X 87 -86.02 -54.63 REMARK 500 SER X 88 -7.42 -33.41 REMARK 500 LEU X 90 -38.92 -39.03 REMARK 500 LEU X 93 -72.98 -55.93 REMARK 500 ALA X 103 -70.68 -16.01 REMARK 500 ALA X 126 -4.39 -52.09 REMARK 500 LEU X 129 -81.92 -64.50 REMARK 500 SER X 130 -43.92 -15.25 REMARK 500 HIS X 133 -12.01 -44.42 REMARK 500 LYS X 138 -71.08 -15.68 REMARK 500 LEU X 144 -85.10 -73.01 REMARK 500 LEU Y 9 -5.06 -49.79 REMARK 500 SER Y 13 -103.63 -67.76 REMARK 500 LYS Y 14 -62.90 -17.60 REMARK 500 LEU Y 26 -71.36 -31.42 REMARK 500 SER Y 27 -8.57 -47.07 REMARK 500 GLU Y 31 55.94 4.60 REMARK 500 PRO Y 34 154.70 -42.61 REMARK 500 ALA Y 43 164.17 -34.78 REMARK 500 PHE Y 46 -60.89 -109.08 REMARK 500 GLN Y 54 -160.87 -111.68 REMARK 500 GLN Y 80 -12.07 -146.03 REMARK 500 PRO Y 83 48.50 -96.87 REMARK 500 CYS Y 85 -65.92 -5.99 REMARK 500 SER Y 88 -69.63 -28.15 REMARK 500 ASN Y 125 -34.10 -28.51 REMARK 500 ARG Y 140 -76.70 -46.27 REMARK 500 PHE Y 141 -34.48 -39.67 REMARK 500 LEU Y 144 -71.35 -72.59 REMARK 500 VAL Y 145 93.79 -56.74 REMARK 500 ARG Z 10 17.81 -63.11 REMARK 500 LYS Z 14 -52.43 -28.99 REMARK 500 SER Z 24 -71.14 -40.59 REMARK 500 ARG Z 25 -12.09 -44.06 REMARK 500 SER Z 27 -55.12 -26.85 REMARK 500 GLU Z 31 59.34 22.73 REMARK 500 LEU Z 48 45.72 -93.32 REMARK 500 GLU Z 50 -71.61 13.19 REMARK 500 GLU Z 56 -77.05 -33.50 REMARK 500 GLU Z 57 -66.70 -27.91 REMARK 500 GLN Z 92 -36.85 -30.84 REMARK 500 LEU Z 93 -71.24 -60.86 REMARK 500 SER Z 94 -65.71 -17.82 REMARK 500 THR Z 110 122.37 176.84 REMARK 500 GLN Z 111 161.68 -48.59 REMARK 500 PRO Z 114 109.50 -45.65 REMARK 500 ARG Z 117 130.47 -26.34 REMARK 500 LEU Z 129 -59.02 -20.80 REMARK 500 LYS Z 138 -75.88 8.20 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 PHE H 27 THR H 28 149.62 REMARK 500 SER H 99 GLY H 100 -144.30 REMARK 500 PHE M 61 ARG M 62 144.56 REMARK 500 ALA M 83 THR M 84 148.51 REMARK 500 SER I 7 GLY I 8 145.96 REMARK 500 MET I 138 VAL I 139 145.44 REMARK 500 SER I 175 ASP I 176 -146.70 REMARK 500 PRO I 203 ALA I 204 -102.11 REMARK 500 ALA I 204 SER I 205 -144.88 REMARK 500 GLY N 92 TYR N 93 149.44 REMARK 500 LYS N 168 ASP N 169 -148.12 REMARK 500 SER J 115 ALA J 116 129.03 REMARK 500 ALA J 133 GLN J 134 143.91 REMARK 500 PRO J 203 ALA J 204 -137.47 REMARK 500 GLY K 109 THR K 110 149.55 REMARK 500 HIS K 202 PRO K 203 75.39 REMARK 500 GLY X 49 GLU X 50 149.74 REMARK 500 THR Y 53 GLN Y 54 137.05 REMARK 500 GLY Z 49 GLU Z 50 140.07 REMARK 500 GLY Z 137 LYS Z 138 143.25 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1V7M RELATED DB: PDB REMARK 900 THE SAME PROTEIN IN WILD TYPE