REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.C.KOVARI,C.MOMANY,M.G.ROSSMANN REMARK 1 TITL THE USE OF ANTIBODY FRAGMENTS FOR CRYSTALLIZATION REMARK 1 TITL 2 AND STRUCTURE DETERMINATIONS REMARK 1 REF STRUCTURE V. 3 1291 1995 REMARK 1 REFN ISSN 0969-2126 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.J.PRONGAY,T.J.SMITH,M.G.ROSSMANN,L.S.EHRLICH, REMARK 1 AUTH 2 C.A.CARTER,J.MCCLURE REMARK 1 TITL PREPARATION AND CRYSTALLIZATION OF A HUMAN REMARK 1 TITL 2 IMMUNODEFICIENCY VIRUS P24-FAB COMPLEX REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 87 9980 1990 REMARK 1 REFN ISSN 0027-8424 REMARK 1 REFERENCE 3 REMARK 1 AUTH L.S.EHRLICH,H.G.KRAUSSLICH,E.WIMMER,C.A.CARTER REMARK 1 TITL EXPRESSION IN ESCHERICHIA COLI AND PURIFICATION OF REMARK 1 TITL 2 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 CAPSID PROTEIN REMARK 1 TITL 3 (P24) REMARK 1 REF AIDS RES.HUM.RETROVIRUSES V. 6 1169 1990 REMARK 1 REFN ISSN 0889-2229 REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 29703 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) : 0.217 REMARK 3 FREE R VALUE : 0.324 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 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 : 11054 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.59 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.23 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 : RESTRAINTS 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: THE CARBOXY-TERMINAL RESIDUES 152 - REMARK 3 231 OF THE HIV-1 CAPSID PROTEIN ARE DISORDERED AND NOT VISIBLE REMARK 3 IN THE ELECTRON DENSITY MAPS. REMARK 4 REMARK 4 1AFV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : DEC-95 REMARK 200 TEMPERATURE (KELVIN) : 120 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : A1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.909 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : PRINCETON 2K REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29703 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 100.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.06400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 50.4 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.37000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT, REMARK 200 MULTIPLE ISOMORPHOUS REPLACEMENT, ANOMALOUS DISPERSION REMARK 200 SOFTWARE USED: X-PLOR 3.8 REMARK 200 STARTING MODEL: FAB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 3350, 50 MM BISTRIS-HCL, PH REMARK 280 7.0, 0.1% BETA-OCTYLGLUCOSIDE, 1 MM NAN3 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21 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 X+1/2,-Y,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,Z+1/2 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 1.000000 0.000000 0.000000 59.95000 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.65000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.95000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.65000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, H, M, K 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 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 OD1 ASN K 54 PB PB L 218 4555 1.64 REMARK 500 OD1 ASN H 54 PB PB M 218 4564 1.93 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 PRO A 122 C - N - CA ANGL. DEV. = 24.8 DEGREES REMARK 500 PRO A 122 C - N - CD ANGL. DEV. = -29.1 DEGREES REMARK 500 PRO B 122 C - N - CD ANGL. DEV. = -20.9 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ILE A 2 -45.79 -167.64 REMARK 500 VAL A 3 43.14 -82.97 REMARK 500 GLN A 4 -77.61 -67.39 REMARK 500 LEU A 6 -3.08 61.66 REMARK 500 GLN A 7 44.85 -81.21 REMARK 500 GLN A 9 -129.69 -90.58 REMARK 500 MET A 10 -1.56 -57.39 REMARK 500 ALA A 31 -151.34 57.72 REMARK 500 PHE A 32 32.63 -88.40 REMARK 500 GLU A 45 89.17 -41.65 REMARK 500 ALA A 64 -70.79 -55.69 REMARK 500 PRO A 85 -0.04 -56.21 REMARK 500 HIS A 87 80.02 7.95 REMARK 500 ALA A 88 17.26 81.08 REMARK 500 ALA A 92 113.35 74.34 REMARK 500 ARG A 97 153.91 64.61 REMARK 500 MET A 144 38.21 -86.82 REMARK 500 TYR A 145 96.49 162.37 REMARK 500 SER A 146 -65.78 -165.88 REMARK 500 THR A 148 -81.33 -97.80 REMARK 500 ILE B 2 -46.32 -169.67 REMARK 500 VAL B 3 42.92 -82.46 REMARK 500 GLN B 4 -81.56 -66.72 REMARK 500 LEU B 6 -4.66 60.05 REMARK 500 GLN B 7 45.66 -80.27 REMARK 500 GLN B 9 -131.75 -87.88 REMARK 500 MET B 10 -1.93 -56.13 REMARK 500 ALA B 31 -150.36 58.81 REMARK 500 PHE B 32 35.80 -90.01 REMARK 500 GLU B 45 88.37 -43.29 REMARK 500 ALA B 64 -71.81 -56.99 REMARK 500 PRO B 85 -0.72 -55.52 REMARK 500 HIS B 87 83.99 8.12 REMARK 500 ALA B 92 109.58 73.09 REMARK 500 ARG B 97 153.98 70.50 REMARK 500 PRO B 122 82.95 48.76 REMARK 500 MET B 144 37.14 -88.55 REMARK 500 TYR B 145 98.67 162.71 REMARK 500 SER B 146 -66.02 -166.35 REMARK 500 THR B 148 -81.59 -96.55 REMARK 500 SER L 7 -87.92 -45.51 REMARK 500 VAL L 29 42.34 -86.79 REMARK 500 ASN L 31 128.53 -175.68 REMARK 500 ALA L 55 -32.18 71.08 REMARK 500 SER L 56 -4.54 -140.91 REMARK 500 HIS L 80 124.83 -175.78 REMARK 500 ASP L 86 8.70 -69.00 REMARK 500 SER L 95 58.37 -101.88 REMARK 500 LYS L 96 -55.99 -120.82 REMARK 500 GLU L 158 95.93 -59.59 REMARK 500 LYS L 173 -66.63 -171.76 REMARK 500 SER L 175 18.65 46.41 REMARK 500 ASN L 194 -68.84 -136.25 REMARK 500 LYS L 203 -33.48 -22.27 REMARK 500 THR L 204 4.17 -65.50 REMARK 500 SER L 205 124.80 -176.34 REMARK 500 PRO H 7 137.37 -34.49 REMARK 500 ALA H 16 -158.76 -93.50 REMARK 500 CYS H 22 78.72 -172.88 REMARK 500 PHE H 29 -45.49 -26.63 REMARK 500 SER H 55 -18.13 -148.69 REMARK 500 ASP H 73 70.22 -151.50 REMARK 500 SER H 77 50.63 29.75 REMARK 500 SER H 85 57.02 35.54 REMARK 500 SER H 91 95.04 -66.97 REMARK 500 TYR H 106 164.54 177.12 REMARK 500 ALA H 121 151.48 -48.84 REMARK 500 SER H 135 -23.70 -168.84 REMARK 500 ALA H 137 93.85 -55.34 REMARK 500 ASN H 140 52.60 11.70 REMARK 500 PHE H 153 138.22 175.23 REMARK 500 SER H 167 -63.47 -96.83 REMARK 500 SER H 192 -66.86 11.54 REMARK 500 THR H 194 -83.46 -142.32 REMARK 500 SER H 197 29.78 -142.01 REMARK 500 SER M 7 -87.52 -41.73 REMARK 500 VAL M 29 43.22 -86.20 REMARK 500 ASN M 31 128.31 -176.73 REMARK 500 PRO M 48 171.60 -54.85 REMARK 500 ALA M 55 -32.21 66.79 REMARK 500 SER M 71 140.79 -171.07 REMARK 500 HIS M 80 125.36 -176.28 REMARK 500 SER M 95 56.37 -100.32 REMARK 500 LYS M 96 -53.92 -120.70 REMARK 500 SER M 120 119.75 -162.88 REMARK 500 GLU M 158 94.58 -60.95 REMARK 500 SER M 172 62.85 -66.95 REMARK 500 LYS M 173 -67.05 -169.23 REMARK 500 SER M 175 16.22 46.59 REMARK 500 LEU M 185 -169.72 -161.11 REMARK 500 ASN M 194 -68.24 -139.14 REMARK 500 LYS M 203 -32.06 -24.23 REMARK 500 THR M 204 1.47 -66.82 REMARK 500 SER M 205 125.25 -173.31 REMARK 500 PRO K 7 138.10 -36.21 REMARK 500 ALA K 16 -159.23 -91.02 REMARK 500 CYS K 22 78.37 -171.16 REMARK 500 SER K 55 -18.62 -148.61 REMARK 500 ASP K 73 69.77 -151.57 REMARK 500 SER K 76 40.79 -109.36 REMARK 500 SER K 77 47.74 29.33 REMARK 500 SER K 91 96.22 -63.51 REMARK 500 TYR K 106 163.17 177.06 REMARK 500 SER K 135 -22.86 -163.41 REMARK 500 ALA K 137 90.78 -55.18 REMARK 500 GLN K 138 12.53 -148.85 REMARK 500 ASN K 140 50.31 11.48 REMARK 500 PHE K 153 139.71 -178.81 REMARK 500 SER K 167 -66.09 -98.34 REMARK 500 SER K 179 70.22 51.58 REMARK 500 PRO K 191 90.36 -69.34 REMARK 500 SER K 192 -67.96 13.74 REMARK 500 THR K 194 -81.06 -136.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR H 101 0.07 SIDE_CHAIN REMARK 500 TYR K 101 0.09 SIDE_CHAIN 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: (11X,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 TRP H 195 24.5 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 PB L 218 PB REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU L 83 OE1 REMARK 620 2 GLU L 83 OE2 54.7 REMARK 620 3 ASN K 54 OD1 115.8 110.8 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 PB M 218 PB REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU M 83 OE1 REMARK 620 2 GLU M 83 OE2 58.5 REMARK 620 3 ASN H 54 OD1 104.8 113.2 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CP1 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CYCLOPHILIN BINDING SITE. REMARK 800 SITE_IDENTIFIER: CP2 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CYCLOPHILIN BINDING SITE. REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB L 218 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB M 218