REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.77 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 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) : 3.77 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.26 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.2 REMARK 3 NUMBER OF REFLECTIONS : 13950 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THOUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.249 REMARK 3 FREE R VALUE : 0.342 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL 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) : 3.77 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.94 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.20 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2490 REMARK 3 BIN FREE R VALUE : 0.3420 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 13950 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6420 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 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) : 87.70 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) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3D69 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-08. REMARK 100 THE RCSB ID CODE IS RCSB047644. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-SEP-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X12C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13950 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.770 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 82.2 REMARK 200 DATA REDUNDANCY : 1.500 REMARK 200 R MERGE (I) : 0.21700 REMARK 200 R SYM (I) : 0.00900 REMARK 200 FOR THE DATA SET : 141.4000 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 1NL0 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0M AMMONIUM SULFATE, 0.1M HEPES, REMARK 280 2%MPD, PH7.5, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y,X,Z+1/4 REMARK 290 4555 Y,-X,Z+3/4 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 32.68300 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 16.34150 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 49.02450 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.4 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3500 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.5 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H 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 GLN L 1 REMARK 465 SER L 2 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLN A 1 REMARK 465 SER A 2 REMARK 465 GLU A 211 REMARK 465 CYS A 212 REMARK 465 SER A 213 REMARK 465 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 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 LEU L 4 90.08 69.41 REMARK 500 ALA L 13 157.20 162.32 REMARK 500 PRO L 15 155.74 -43.93 REMARK 500 LYS L 18 173.39 -52.68 REMARK 500 ASN L 27B -133.61 -144.24 REMARK 500 ILE L 28 -72.16 10.67 REMARK 500 ASN L 30 -51.40 -132.75 REMARK 500 LYS L 42 -172.15 -41.57 REMARK 500 ASP L 50 75.39 44.72 REMARK 500 VAL L 51 -121.56 51.75 REMARK 500 PRO L 59 155.17 -47.00 REMARK 500 ARG L 61 4.75 -67.93 REMARK 500 LEU L 73 66.90 -119.22 REMARK 500 SER L 80 -53.85 -26.06 REMARK 500 ASP L 93 -31.26 -39.24 REMARK 500 SER L 95A 65.95 39.85 REMARK 500 LEU L 107 125.54 -33.26 REMARK 500 SER L 123 -70.75 -47.97 REMARK 500 ALA L 128 45.20 -72.00 REMARK 500 ASN L 129 68.39 32.35 REMARK 500 ASP L 139 78.78 60.07 REMARK 500 ALA L 144 69.10 -166.53 REMARK 500 ASP L 152 -139.73 64.96 REMARK 500 SER L 153 43.66 -92.20 REMARK 500 LYS L 157 -39.50 -134.20 REMARK 500 ALA L 158 74.72 -8.62 REMARK 500 ASN L 170 45.09 -72.10 REMARK 500 ALA L 174 114.48 -169.39 REMARK 500 LYS L 187 -81.22 -52.94 REMARK 500 LYS L 190 -71.87 -68.30 REMARK 500 GLU L 199 31.60 82.55 REMARK 500 VAL L 203 98.46 -64.67 REMARK 500 PRO L 209 -79.24 -40.30 REMARK 500 ARG H 16 -140.67 -78.82 REMARK 500 LEU H 18 136.78 176.27 REMARK 500 LYS H 43 160.36 -49.79 REMARK 500 VAL H 48 -73.43 -106.14 REMARK 500 SER H 55 -84.85 -79.58 REMARK 500 ASP H 61 23.43 -74.33 REMARK 500 LYS H 64 107.00 -35.63 REMARK 500 ASP H 72 64.67 -100.13 REMARK 500 ASN H 73 -42.32 -26.70 REMARK 500 ASN H 76 33.04 32.39 REMARK 500 LEU H 80 117.62 -167.07 REMARK 500 SER H 82B 64.48 62.67 REMARK 500 ALA H 84 -32.95 -33.77 REMARK 500 THR H 87 119.89 -38.74 REMARK 500 ALA H 88 -176.07 174.58 REMARK 500 SER H 96 145.11 -38.89 REMARK 500 ARG H 105 107.51 -58.10 REMARK 500 SER H 115 -141.07 -119.07 REMARK 500 PRO H 119 -164.66 -62.97 REMARK 500 SER H 120 75.76 -171.19 REMARK 500 THR H 135 -83.40 -127.81 REMARK 500 ALA H 136 103.08 -179.03 REMARK 500 ASP H 144 89.18 52.51 REMARK 500 SER H 156 -20.13 71.33 REMARK 500 LEU H 159 84.08 43.27 REMARK 500 ALA H 168 -167.09 -66.34 REMARK 500 SER H 173 2.71 -68.77 REMARK 500 GLN H 192 129.45 162.36 REMARK 500 ASN H 197 56.26 -102.94 REMARK 500 PRO H 202 -72.98 -43.96 REMARK 500 SER H 203 11.96 -58.88 REMARK 500 ASN H 204 70.52 37.81 REMARK 500 LEU A 4 78.56 73.50 REMARK 500 PRO A 15 40.73 -49.30 REMARK 500 SER A 26 170.98 173.17 REMARK 500 ASN A 27B -135.45 -124.85 REMARK 500 ILE A 28 -44.37 -7.66 REMARK 500 PRO A 40 -71.14 -35.45 REMARK 500 LEU A 46 109.93 -48.03 REMARK 500 MET A 47 -63.51 -92.03 REMARK 500 VAL A 51 -135.23 61.78 REMARK 500 SER A 52 67.47 -60.86 REMARK 500 PRO A 59 167.38 -48.75 REMARK 500 SER A 80 -39.26 -37.42 REMARK 500 GLU A 83 100.35 -40.30 REMARK 500 SER A 95A 79.23 44.51 REMARK 500 GLU A 95B 147.68 171.81 REMARK 500 LEU A 107 115.01 -31.24 REMARK 500 LYS A 111 172.43 -55.91 REMARK 500 THR A 117 66.34 -169.22 REMARK 500 GLU A 124 -85.08 -58.99 REMARK 500 GLU A 125 -46.80 -24.43 REMARK 500 ALA A 128 29.46 -69.55 REMARK 500 ASN A 129 64.54 38.42 REMARK 500 ALA A 148 147.42 -170.15 REMARK 500 ASP A 152 -145.17 60.69 REMARK 500 ALA A 158 84.99 -51.89 REMARK 500 PRO A 165 -177.44 -58.44 REMARK 500 SER A 166 121.12 -179.52 REMARK 500 SER A 169 -51.98 -23.33 REMARK 500 ASN A 170 22.57 -78.92 REMARK 500 ASN A 171 -9.37 74.74 REMARK 500 ALA A 174 123.40 -173.86 REMARK 500 LYS A 187 -72.76 -67.05 REMARK 500 SER A 188 -82.37 -34.47 REMARK 500 LYS A 190 5.55 -67.68 REMARK 500 VAL A 196 77.14 -109.85 REMARK 500 HIS A 198 109.41 -170.49 REMARK 500 GLU A 199 38.10 73.90 REMARK 500 ARG B 16 158.39 -49.63 REMARK 500 LEU B 18 137.01 -171.70 REMARK 500 SER B 25 76.06 -168.02 REMARK 500 PHE B 27 -160.00 175.89 REMARK 500 SER B 30 -13.64 -48.15 REMARK 500 SER B 52 -179.81 -65.22 REMARK 500 SER B 55 -79.76 -88.93 REMARK 500 ASP B 61 -34.92 -36.23 REMARK 500 SER B 62 -2.25 -47.25 REMARK 500 VAL B 63 -41.93 -158.67 REMARK 500 LYS B 64 85.49 -0.17 REMARK 500 ASN B 76 44.87 27.99 REMARK 500 ALA B 88 -160.75 177.29 REMARK 500 SER B 96 172.39 -42.76 REMARK 500 ALA B 99 79.87 -153.86 REMARK 500 THR B 116 129.47 -18.63 REMARK 500 VAL B 121 136.88 -39.30 REMARK 500 ALA B 136 161.31 -31.82 REMARK 500 ASP B 144 54.73 70.16 REMARK 500 VAL B 150 115.34 -165.64 REMARK 500 LEU B 159 88.03 40.42 REMARK 500 ALA B 168 -158.77 -69.37 REMARK 500 GLN B 171 174.30 -56.79 REMARK 500 SER B 173 17.28 -66.60 REMARK 500 SER B 186 -9.16 -54.55 REMARK 500 SER B 188 45.01 -103.72 REMARK 500 THR B 191 -27.34 -157.37 REMARK 500 ASN B 199 128.35 -172.54 REMARK 500 LYS B 214 79.87 -64.14 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 SER L 9 VAL L 11 140.99 REMARK 500 SER A 9 VAL A 11 123.47 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 GLU H 148 24.6 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN REMARK 999 DOES NOT CURRENTLY EXIST.