REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.51 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 17838 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) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.740 REMARK 3 FREE R VALUE TEST SET COUNT : 1024 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 : 9 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.76 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2821 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2533 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2654 REMARK 3 BIN R VALUE (WORKING SET) : 0.2497 REMARK 3 BIN FREE R VALUE : 0.3078 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.92 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 167 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 : 3480 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 26 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 73.69 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.19500 REMARK 3 B22 (A**2) : -1.19500 REMARK 3 B33 (A**2) : 2.39000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.44 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.56 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3592 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4884 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1182 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 82 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 519 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3592 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 470 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3993 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.28 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.24 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.20 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { L|1 - L|107 } REMARK 3 ORIGIN FOR THE GROUP (A): 1.7532 -10.6092 -20.9329 REMARK 3 T TENSOR REMARK 3 T11: -0.0656 T22: -0.0449 REMARK 3 T33: -0.0062 T12: -0.0837 REMARK 3 T13: 0.0399 T23: -0.0055 REMARK 3 L TENSOR REMARK 3 L11: 2.4694 L22: 2.0347 REMARK 3 L33: 2.3021 L12: 0.3656 REMARK 3 L13: 0.5399 L23: 0.8892 REMARK 3 S TENSOR REMARK 3 S11: -0.0305 S12: 0.2064 S13: 0.3266 REMARK 3 S21: -0.1780 S22: 0.0663 S23: -0.0122 REMARK 3 S31: -0.2142 S32: -0.1215 S33: -0.0358 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { L|108 - L|214 } REMARK 3 ORIGIN FOR THE GROUP (A): 23.8180 -10.6283 9.9719 REMARK 3 T TENSOR REMARK 3 T11: -0.1473 T22: 0.1728 REMARK 3 T33: -0.0628 T12: -0.1520 REMARK 3 T13: 0.0310 T23: -0.1520 REMARK 3 L TENSOR REMARK 3 L11: 2.8543 L22: 2.5215 REMARK 3 L33: 2.6745 L12: -0.8052 REMARK 3 L13: 1.5074 L23: -1.6418 REMARK 3 S TENSOR REMARK 3 S11: 0.1629 S12: -0.2239 S13: 0.0579 REMARK 3 S21: 0.2365 S22: -0.2112 S23: -0.0842 REMARK 3 S31: 0.0631 S32: 0.2787 S33: 0.0483 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { H|1 - H|113 } REMARK 3 ORIGIN FOR THE GROUP (A): 7.9834 -31.2527 -21.7111 REMARK 3 T TENSOR REMARK 3 T11: 0.0466 T22: -0.1112 REMARK 3 T33: -0.0362 T12: -0.1092 REMARK 3 T13: 0.0684 T23: -0.0806 REMARK 3 L TENSOR REMARK 3 L11: 2.9297 L22: 1.4523 REMARK 3 L33: 2.5104 L12: -0.5978 REMARK 3 L13: 0.3424 L23: -0.0998 REMARK 3 S TENSOR REMARK 3 S11: -0.2213 S12: 0.2333 S13: -0.3594 REMARK 3 S21: -0.0807 S22: 0.1256 S23: 0.0537 REMARK 3 S31: 0.4992 S32: 0.0665 S33: 0.0957 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { H|114 - H|216 } REMARK 3 ORIGIN FOR THE GROUP (A): 15.9156 -23.7517 10.0761 REMARK 3 T TENSOR REMARK 3 T11: -0.1528 T22: 0.1524 REMARK 3 T33: -0.0813 T12: -0.1272 REMARK 3 T13: 0.0278 T23: -0.0560 REMARK 3 L TENSOR REMARK 3 L11: 1.0812 L22: 1.2904 REMARK 3 L33: 4.1040 L12: -0.7175 REMARK 3 L13: -0.4737 L23: -0.8702 REMARK 3 S TENSOR REMARK 3 S11: 0.0913 S12: -0.1959 S13: -0.0139 REMARK 3 S21: 0.1468 S22: 0.0075 S23: 0.0926 REMARK 3 S31: 0.2831 S32: -0.1810 S33: -0.0987 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { A|412 - A|423 } REMARK 3 ORIGIN FOR THE GROUP (A): -5.7745 -26.1769 -36.8313 REMARK 3 T TENSOR REMARK 3 T11: 0.0364 T22: 0.1643 REMARK 3 T33: -0.1652 T12: -0.1520 REMARK 3 T13: -0.0073 T23: -0.1265 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.0000 REMARK 3 L33: 1.3753 L12: 1.2842 REMARK 3 L13: -0.0011 L23: 0.5943 REMARK 3 S TENSOR REMARK 3 S11: -0.0004 S12: 0.0363 S13: -0.0034 REMARK 3 S21: -0.0503 S22: 0.0360 S23: 0.1269 REMARK 3 S31: 0.0330 S32: -0.0166 S33: -0.0356 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4HS8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-12. REMARK 100 THE RCSB ID CODE IS RCSB075855. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-MAR-11 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17880 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09800 REMARK 200 FOR THE DATA SET : 19.0000 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: PHASER REMARK 200 STARTING MODEL: 1FVC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 6.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 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+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 90.69200 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.85800 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.85800 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.34600 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.85800 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.85800 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 136.03800 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.85800 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.85800 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 45.34600 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.85800 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.85800 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 136.03800 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 90.69200 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLY A 424 REMARK 465 SER A 425 REMARK 465 GLY A 426 REMARK 465 LYS A 427 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 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 H 101 C - N - CA ANGL. DEV. = 15.1 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 ASP H 65 -17.06 69.75 REMARK 500 SER H 127 82.86 62.60 REMARK 500 LYS H 129 -46.39 -146.43 REMARK 500 SER H 132 161.03 63.52 REMARK 500 ALA L 51 -48.50 63.86 REMARK 500 ASN L 138 80.28 53.03 REMARK 500 LYS L 169 -60.46 -107.69 REMARK 500 SER L 171 19.61 59.91 REMARK 500 LYS L 190 -64.35 -93.82 REMARK 500 GLU L 213 35.94 -97.72 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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE 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 VAL H 2 23.6 L L OUTSIDE RANGE REMARK 500 ASP H 65 23.4 L L OUTSIDE RANGE REMARK 500 MET L 4 21.7 L L OUTSIDE RANGE REMARK 500 VAL L 58 22.7 L L OUTSIDE RANGE REMARK 500 THR L 74 24.1 L L OUTSIDE RANGE REMARK 500 ILE L 106 22.6 L L OUTSIDE RANGE REMARK 500 LEU L 175 24.4 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 600 REMARK 600 HETEROGEN REMARK 600 E2-PEPTIDE IS BIOTINYLATED, WITH BIOTIN (BTN) ATTACHED TO THE SIDE REMARK 600 CHAIN OF THE C-TERMINAL LYS RESIDUE. HOWEVER, SOME RESIDUES AT THE REMARK 600 C-TERMINUS, INCLUDING BTN, ARE MISSING DUE TO DISORDER. REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 304 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4HS6 RELATED DB: PDB