REMARK 2 REMARK 2 RESOLUTION. 3.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.3 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) : 3.0 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 5840810 REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 66.2 REMARK 3 NUMBER OF REFLECTIONS : 39276 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) : 0.235 REMARK 3 FREE R VALUE : 0.309 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 1975 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.16 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 38.5 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3561 REMARK 3 BIN R VALUE (WORKING SET) : 0.282 REMARK 3 BIN FREE R VALUE : 0.366 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.4 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 203 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10529 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 233 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.2 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.5 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.39 REMARK 3 B22 (A**2) : -0.39 REMARK 3 B33 (A**2) : 0.78 REMARK 3 B12 (A**2) : 0.00 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40 REMARK 3 ESD FROM SIGMAA (A) : 0.44 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.55 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.80 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.6 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.8 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.50 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 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QLE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-99. REMARK 100 THE PDBE ID CODE IS EBI-4025. 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 : 8.00 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9875 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 : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64653 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 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 (%) : 95.2 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.11500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.6000 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: OTHER REMARK 200 SOFTWARE USED: CNS 0.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 75. REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 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 300 REMARK 300 DETAILS:THE CRYSTAL STRUCTURE SHOWS A CRYSTAL REMARK 300 PACKING ARRANGEMENT WHERETHERE IS CONTACT BETWEEN REMARK 300 CHAINS C AND H GIVING A CYCLICPACKING WITHCHAIN- REMARK 300 H ... (CHAIN-C...CHAIN-H) ... CHAIN-C(Y,-X,Z REMARK 300 ) ASU: X,Y,Z (-Y,X,Z) 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 24580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 61150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -229.6 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, H, L 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 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 CD1 LEU B 4 - CD1 TRP B 242 2.15 REMARK 500 O ASP B 159 - CD PRO B 161 2.18 REMARK 500 NZ LYS C 4 - OG1 THR D 7 2.03 REMARK 500 CE1 HIS C 6 - O TYR C 8 2.10 REMARK 500 OE1 GLU H 6 - SG CYS H 96 2.08 REMARK 500 OE1 GLU H 6 - N CYS H 96 1.66 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 TRP C 252 CB TRP C 252 CG 0.115 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 A 516 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES REMARK 500 MET C 35 CG - SD - CE ANGL. DEV. = 9.8 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 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 PHE A 18 91.60 -47.48 REMARK 500 PHE A 19 29.50 -59.59 REMARK 500 THR A 20 -35.34 -138.42 REMARK 500 THR A 26 2.22 -162.90 REMARK 500 VAL A 47 3.33 -64.17 REMARK 500 GLN A 63 -64.66 -96.49 REMARK 500 TYR A 64 -76.67 -69.24 REMARK 500 MET A 65 102.21 -57.59 REMARK 500 ASP A 75 78.65 -112.96 REMARK 500 PHE A 101 49.79 -144.02 REMARK 500 VAL A 102 -57.44 -161.00 REMARK 500 ASP A 124 -157.95 -167.59 REMARK 500 ALA A 126 -63.67 -21.00 REMARK 500 ASN A 131 -15.57 -48.59 REMARK 500 ASN A 155 89.48 -68.47 REMARK 500 ASP A 156 41.97 39.61 REMARK 500 LEU A 166 71.05 47.22 REMARK 500 GLU A 174 136.78 -33.69 REMARK 500 TYR A 177 7.07 -153.44 REMARK 500 MET A 207 45.57 -86.75 REMARK 500 THR A 213 -101.20 -66.46 REMARK 500 LEU A 214 -36.57 -135.47 REMARK 500 ASP A 248 12.12 -65.42 REMARK 500 GLU A 278 -75.89 -44.65 REMARK 500 VAL A 279 -11.39 -48.68 REMARK 500 THR A 296 -73.10 -60.90 REMARK 500 PRO A 301 172.16 -56.68 REMARK 500 VAL A 322 29.20 -159.77 REMARK 500 HIS A 325 5.35 -66.39 REMARK 500 TYR A 339 -74.42 -71.56 REMARK 500 SER A 366 71.82 56.27 REMARK 500 PHE A 369 64.13 -61.93 REMARK 500 LYS A 370 -161.15 -75.27 REMARK 500 VAL A 409 12.53 -67.89 REMARK 500 MET A 416 -85.44 -82.37 REMARK 500 SER A 417 -8.51 -57.33 REMARK 500 GLU A 442 -86.30 -8.88 REMARK 500 VAL A 480 -11.08 -44.65 REMARK 500 PHE A 512 -80.88 -65.03 REMARK 500 ARG A 516 131.85 -39.95 REMARK 500 TRP A 523 -81.04 -91.89 REMARK 500 GLU A 540 -37.97 -39.41 REMARK 500 ASP B 6 74.19 36.66 REMARK 500 ASN B 19 -157.25 -127.57 REMARK 500 ALA B 23 95.42 -63.24 REMARK 500 ARG B 62 -62.91 -19.84 REMARK 500 ALA B 64 4.23 -64.79 REMARK 500 ASN B 65 93.98 -177.87 REMARK 500 VAL B 67 79.14 -112.90 REMARK 500 PHE B 71 110.86 -162.15 REMARK 500 LEU B 112 88.68 -173.45 REMARK 500 GLN B 120 89.73 -62.55 REMARK 500 TRP B 121 -3.74 85.94 REMARK 500 GLU B 126 78.99 -168.49 REMARK 500 ASP B 135 -169.08 -127.11 REMARK 500 ALA B 136 115.84 -163.03 REMARK 500 ASP B 152 40.78 -65.55 REMARK 500 THR B 158 -153.95 -136.57 REMARK 500 ASP B 159 -97.41 -109.87 REMARK 500 ASN B 160 85.58 -52.78 REMARK 500 THR B 177 -20.08 -143.68 REMARK 500 HIS B 181 -167.33 -112.93 REMARK 500 ALA B 189 62.61 67.71 REMARK 500 SER B 217 56.58 -117.74 REMARK 500 GLU B 218 110.93 -176.14 REMARK 500 ASN B 223 50.79 -96.38 REMARK 500 PHE B 250 55.79 -141.90 REMARK 500 LYS C 4 93.79 -67.84 REMARK 500 ASN C 5 70.29 71.52 REMARK 500 HIS C 6 133.53 178.82 REMARK 500 TYR C 8 128.56 -33.60 REMARK 500 TRP C 34 -82.48 -72.16 REMARK 500 VAL C 45 42.15 -141.06 REMARK 500 TRP C 49 -51.18 -131.68 REMARK 500 HIS C 78 62.90 -67.82 REMARK 500 ALA C 107 11.48 -68.33 REMARK 500 PHE C 108 -51.79 -124.90 REMARK 500 HIS C 139 -74.88 -108.20 REMARK 500 VAL C 177 35.34 -85.17 REMARK 500 ALA C 178 -47.14 -147.00 REMARK 500 HIS C 195 59.98 -118.64 REMARK 500 LEU C 200 177.60 -59.98 REMARK 500 ASP C 202 -50.25 -131.62 REMARK 500 TYR C 205 -77.89 -65.79 REMARK 500 MET C 211 9.13 -69.14 REMARK 500 ALA C 212 -61.43 -126.08 REMARK 500 LEU C 235 20.45 -72.25 REMARK 500 GLN C 243 101.58 -166.59 REMARK 500 HIS C 244 44.64 -155.65 REMARK 500 ILE C 270 -92.99 -124.43 REMARK 500 ASP D 8 95.13 -63.98 REMARK 500 ALA D 47 6.30 -57.70 REMARK 500 ASN D 48 72.60 -171.57 REMARK 500 LEU H 18 148.75 178.91 REMARK 500 VAL H 48 -60.97 -120.89 REMARK 500 ARG H 67 -63.32 -128.11 REMARK 500 ASP H 73 80.13 -166.11 REMARK 500 ASN H 77 31.80 72.22 REMARK 500 LEU H 81 85.59 -151.55 REMARK 500 ALA H 92 -174.31 178.49 REMARK 500 TYR H 102 -113.23 78.83 REMARK 500 SER H 117 -146.18 -160.42 REMARK 500 LEU L 11 117.06 -163.65 REMARK 500 TYR L 30 -105.28 61.30 REMARK 500 TYR L 32 83.78 -68.37 REMARK 500 ASN L 50 33.20 76.04 REMARK 500 ALA L 51 -5.98 55.10 REMARK 500 LYS L 52 -27.70 -142.61 REMARK 500 THR L 69 -56.53 -120.43 REMARK 500 SER L 77 86.50 64.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ASP L 82 22.8 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CU Y 2 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 276 ND1 REMARK 620 2 HIS A 326 NE2 146.0 REMARK 620 3 HIS A 325 NE2 96.3 85.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA Z 1 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PRO A 60 O REMARK 620 2 GLU A 56 OE1 133.1 REMARK 620 3 GLY A 61 O 63.8 70.9 REMARK 620 4 GLN A 63 OE1 60.8 86.6 59.4 REMARK 620 5 GLU A 56 O 131.7 90.0 136.9 160.4 REMARK 620 6 HIS A 59 O 64.3 159.2 120.6 114.0 69.8 REMARK 620 7 GLN A 63 NE2 57.7 120.0 97.3 43.2 125.4 77.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN Z 2 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 403 NE2 REMARK 620 2 ASP A 404 OD1 80.7 REMARK 620 3 GLU B 218 OE2 137.1 128.2 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEA X 1 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 94 NE2 REMARK 620 2 HIS A 413 NE2 177.7 REMARK 620 3 HEA X 1 NA 93.7 84.3 REMARK 620 4 HEA X 1 NB 89.8 91.4 90.0 REMARK 620 5 HEA X 1 NC 90.7 91.3 175.4 88.5 REMARK 620 6 HEA X 1 ND 89.0 89.8 90.7 178.6 90.9 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEA X 2 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HEA X 2 NA REMARK 620 2 HEA X 2 NB 86.0 REMARK 620 3 HEA X 2 NC 149.7 86.2 REMARK 620 4 HEA X 2 ND 87.3 154.8 87.4 REMARK 620 5 HIS A 411 NE2 104.8 100.0 105.4 105.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CUA Y 1 CU1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 216 SG REMARK 620 2 CYS B 220 SG 111.7 REMARK 620 3 HIS B 224 ND1 121.1 127.0 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CUA Y 1 CU2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 181 ND1 REMARK 620 2 MET B 227 SD 101.1 REMARK 620 3 CYS B 216 SG 131.0 94.7 REMARK 620 4 CYS B 220 SG 109.4 112.1 106.7 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU Y 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Z 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN Z 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA X 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA X 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA Y 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 P 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 P 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AR1 RELATED DB: PDB REMARK 900 STRUCTURE AT 2.7 ANGSTROM RESOLUTION OF THE PARACOCCUS REMARK 900 DENITRIFICANS TWO-SUBUNIT CYTOCHROME C OXIDASE COMPLEXED REMARK 900 WITH AN ANTIBODY FV FRAGMENT REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF VH AND VL IS DESCRIBED IN THE FOLLOWING REMARK 999 REFERENCE, REMARK 999 OSTERMEIER C. ET AL. (1995) PROTEINS 21: 74-77. REMARK 999 THE NCBI REFERENCE LOCUS FOR CHAIN H IS 2914143 REMARK 999 THE NCBI REFERENCE LOCUS FOR CHAIN L IS 2914144