HEADER IMMUNE SYSTEM 27-JUN-24 9CF7 TITLE GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN EODGT8 IN TITLE 2 COMPLEX WITH FAB EOD-PL01.1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN COMPND 3 EODGT8; COMPND 4 CHAIN: C; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB EOD-PL01.1 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: FAB EOD-PL01.1 KAPPA LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 8 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 17 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 26 EXPRESSION_SYSTEM_ORGAN: KIDNEY KEYWDS HIV, FAB, VACCINE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.SARKAR,R.L.STANFIELD,I.A.WILSON REVDAT 1 25-JUN-25 9CF7 0 JRNL AUTH T.SCHIFFNER,A.PALSER JRNL TITL DIVERSE COMPETITOR B CELL RESPONSES TO A GERMLINE-TARGETING JRNL TITL 2 PRIMING IMMUNOGEN IN HUMAN IG LOCI TRANSGENIC MICE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.55 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2 REMARK 3 NUMBER OF REFLECTIONS : 9825 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.265 REMARK 3 FREE R VALUE : 0.299 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.550 REMARK 3 FREE R VALUE TEST SET COUNT : 447 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) : 3.55 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.64 REMARK 3 REFLECTION IN BIN (WORKING SET) : 472 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.44 REMARK 3 BIN R VALUE (WORKING SET) : 0.4580 REMARK 3 BIN FREE R VALUE SET COUNT : 23 REMARK 3 BIN FREE R VALUE : 0.4520 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4477 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 28 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 166.0 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 162.6 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.11200 REMARK 3 B22 (A**2) : 1.11200 REMARK 3 B33 (A**2) : -3.60600 REMARK 3 B12 (A**2) : 0.55600 REMARK 3 B13 (A**2) : 0.00000 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): 0.764 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.630 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.694 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.860 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4617 ; 0.002 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6295 ; 0.994 ; 1.793 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 588 ; 6.478 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 18 ; 4.068 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 726 ;12.397 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 723 ; 0.067 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3522 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1879 ; 0.217 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3091 ; 0.303 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 111 ; 0.168 ; 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): 2367 ; 3.176 ;16.271 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2950 ; 5.699 ;29.257 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2250 ; 2.859 ;16.237 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3345 ; 5.203 ;29.973 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.10 REMARK 3 ION PROBE RADIUS : 1.00 REMARK 3 SHRINKAGE RADIUS : 1.00 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE NOT BEEN USED REMARK 4 REMARK 4 9CF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000285345. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JUN-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10327 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.550 REMARK 200 RESOLUTION RANGE LOW (A) : 38.550 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 9.500 REMARK 200 R MERGE (I) : 0.26000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.89 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 9.90 REMARK 200 R MERGE FOR SHELL (I) : 3.10000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM DIHYDROGEN PHOSPHATE, REMARK 280 20% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,Z+1/3 REMARK 290 6555 X-Y,X,Z+2/3 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+1/3 REMARK 290 11555 -X+Y,Y,-Z REMARK 290 12555 X,X-Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.56433 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.12867 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.56433 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.12867 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.56433 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 67.12867 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 33.56433 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 67.12867 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 APPLY THE FOLLOWING TO CHAINS: C, 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 GLU C -2 REMARK 465 THR C -1 REMARK 465 GLY C 0 REMARK 465 SER C 31 REMARK 465 ASN C 32 REMARK 465 ALA C 170 REMARK 465 SER C 171 REMARK 465 THR C 172 REMARK 465 GLY C 173 REMARK 465 THR C 174 REMARK 465 HIS C 175 REMARK 465 HIS C 176 REMARK 465 HIS C 177 REMARK 465 HIS C 178 REMARK 465 HIS C 179 REMARK 465 HIS C 180 REMARK 465 SER H 127 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 SER H 215 REMARK 465 CYS H 216 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ND2 ASN C 18 O5 NAG C 202 2.18 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 ASN C 34 30.16 71.11 REMARK 500 ILE C 53 37.31 -87.12 REMARK 500 GLN C 61 -60.55 68.58 REMARK 500 GLU C 70 -87.37 -80.10 REMARK 500 ASP C 79 112.85 -166.10 REMARK 500 ALA C 129 -155.56 -75.49 REMARK 500 LYS C 130 -36.65 -132.69 REMARK 500 HIS C 147 96.03 -59.61 REMARK 500 CYS C 151 107.10 -168.42 REMARK 500 ALA C 165 67.80 -161.89 REMARK 500 SER H 15 -45.43 82.61 REMARK 500 SER H 30 58.39 -99.97 REMARK 500 SER H 31 -135.38 -106.32 REMARK 500 ASP H 96 78.21 -160.82 REMARK 500 ASP H 97 44.83 73.23 REMARK 500 ILE H 98 13.35 35.88 REMARK 500 THR H 100 -82.19 54.07 REMARK 500 ASN H 101 -70.55 -68.77 REMARK 500 ASP H 144 79.41 66.77 REMARK 500 PRO H 149 -165.99 -100.96 REMARK 500 ASN H 204 71.63 39.52 REMARK 500 LYS H 206 53.43 -110.30 REMARK 500 ILE L 30 -121.65 49.41 REMARK 500 SER L 52 -24.25 -160.09 REMARK 500 SER L 67 109.72 178.98 REMARK 500 SER L 77 80.45 -157.75 REMARK 500 PHE L 83 107.20 -56.84 REMARK 500 SER L 91 -2.96 -152.49 REMARK 500 PRO L 96 108.42 -58.20 REMARK 500 ASN L 138 74.93 54.66 REMARK 500 TYR L 140 132.01 -173.01 REMARK 500 ASN L 152 -18.94 75.48 REMARK 500 ARG L 211 107.09 -56.99 REMARK 500 REMARK 500 REMARK: NULL DBREF 9CF7 C -2 180 PDB 9CF7 9CF7 -2 180 DBREF 9CF7 H 1 216 PDB 9CF7 9CF7 1 216 DBREF 9CF7 L 1 214 PDB 9CF7 9CF7 1 214 SEQRES 1 C 183 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 C 183 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 C 183 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 C 183 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 C 183 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 C 183 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 C 183 ARG SER GLU ASP TRP ARG ASP ASN ALA LYS SER ILE CYS SEQRES 8 C 183 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 C 183 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 C 183 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 C 183 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 C 183 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 C 183 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 C 183 THR TRP PHE ALA SER THR GLY THR HIS HIS HIS HIS HIS SEQRES 15 C 183 HIS SEQRES 1 H 222 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL GLU SEQRES 2 H 222 PRO SER GLY THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 222 GLY SER ILE SER SER THR ASN TRP TRP THR TRP VAL ARG SEQRES 4 H 222 GLN THR PRO GLY THR GLY LEU GLU TRP ILE GLY GLU ILE SEQRES 5 H 222 HIS HIS SER GLY ILE THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 H 222 SER ARG VAL THR ILE SER VAL ASP LYS SER LYS ASN GLN SEQRES 7 H 222 PHE SER LEU LYS LEU SER SER VAL ILE ALA ALA ASP THR SEQRES 8 H 222 ALA ALA TYR TYR CYS ALA ARG GLY ASP ASP ILE LEU THR SEQRES 9 H 222 GLY TYR ASN TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 H 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 H 222 CYS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN ASN ILE ILE ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE ASN ALA ALA SER SEQRES 5 L 214 SER LEU GLN SER GLY VAL PRO SER ARG VAL SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN SER GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 214 HIS SER THR PRO PRO THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET NAG C 201 14 HET NAG C 202 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 2(C8 H15 N O6) HELIX 1 AA1 PRO C 12 SER C 16 5 5 HELIX 2 AA2 ASP C 44 CYS C 51 1 8 HELIX 3 AA3 ARG C 109 GLY C 128 1 20 HELIX 4 AA4 ASP C 141 ASN C 146 1 6 HELIX 5 AA5 PRO H 61 LYS H 64 5 4 HELIX 6 AA6 ILE H 83 THR H 87 5 5 HELIX 7 AA7 SER H 156 ALA H 158 5 3 HELIX 8 AA8 SER H 187 LEU H 189 5 3 HELIX 9 AA9 GLN L 79 PHE L 83 5 5 HELIX 10 AB1 SER L 121 LYS L 126 1 6 HELIX 11 AB2 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 7 LEU C 62 LEU C 64 0 SHEET 2 AA1 7 SER C 17 ARG C 26 -1 N THR C 20 O PHE C 63 SHEET 3 AA1 7 VAL C 95 CYS C 99 -1 O VAL C 95 N ILE C 19 SHEET 4 AA1 7 HIS C 104 SER C 108 -1 O ALA C 106 N ALA C 98 SHEET 5 AA1 7 THR C 2 ARG C 8 -1 N LEU C 5 O CYS C 105 SHEET 6 AA1 7 GLU C 154 CYS C 158 -1 O TYR C 157 N ARG C 8 SHEET 7 AA1 7 HIS C 147 CYS C 151 -1 N PHE C 149 O PHE C 156 SHEET 1 AA2 6 VAL C 74 ARG C 76 0 SHEET 2 AA2 6 ILE C 87 GLN C 90 -1 O CYS C 88 N ARG C 76 SHEET 3 AA2 6 SER C 17 ARG C 26 -1 N LEU C 22 O VAL C 89 SHEET 4 AA2 6 THR C 35 PRO C 40 -1 O ARG C 39 N THR C 25 SHEET 5 AA2 6 THR C 131 PHE C 134 1 O ILE C 133 N PHE C 38 SHEET 6 AA2 6 SER C 166 TRP C 168 -1 O SER C 166 N PHE C 134 SHEET 1 AA3 4 GLN H 3 SER H 7 0 SHEET 2 AA3 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AA3 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AA3 4 VAL H 67 ASP H 72 -1 N THR H 68 O LYS H 81 SHEET 1 AA4 5 THR H 57 TYR H 59 0 SHEET 2 AA4 5 GLY H 44 HIS H 52 -1 N GLU H 50 O ASN H 58 SHEET 3 AA4 5 TRP H 34 THR H 40 -1 N THR H 40 O GLY H 44 SHEET 4 AA4 5 ALA H 88 ARG H 94 -1 O TYR H 91 N VAL H 37 SHEET 5 AA4 5 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA5 5 THR H 57 TYR H 59 0 SHEET 2 AA5 5 GLY H 44 HIS H 52 -1 N GLU H 50 O ASN H 58 SHEET 3 AA5 5 TRP H 34 THR H 40 -1 N THR H 40 O GLY H 44 SHEET 4 AA5 5 ALA H 88 ARG H 94 -1 O TYR H 91 N VAL H 37 SHEET 5 AA5 5 THR H 107 VAL H 109 -1 O THR H 107 N TYR H 90 SHEET 1 AA6 4 SER H 120 LEU H 124 0 SHEET 2 AA6 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA6 4 TYR H 176 PRO H 185 -1 O VAL H 182 N LEU H 138 SHEET 4 AA6 4 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA7 3 THR H 151 TRP H 154 0 SHEET 2 AA7 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AA7 3 THR H 205 VAL H 211 -1 O VAL H 211 N TYR H 194 SHEET 1 AA8 4 MET L 4 SER L 7 0 SHEET 2 AA8 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA8 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA8 4 VAL L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA9 6 SER L 10 SER L 14 0 SHEET 2 AA9 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AA9 6 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA9 6 LYS L 45 ASN L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA9 6 SER L 53 LEU L 54 -1 O SER L 53 N ASN L 49 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS C 7 CYS C 158 1555 1555 2.04 SSBOND 2 CYS C 15 CYS C 151 1555 1555 2.04 SSBOND 3 CYS C 51 CYS C 88 1555 1555 2.05 SSBOND 4 CYS C 99 CYS C 105 1555 1555 2.04 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 6 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 8 CYS L 134 CYS L 194 1555 1555 2.52 LINK ND2 ASN C 18 C1 NAG C 202 1555 1555 1.46 LINK ND2 ASN C 65 C1 NAG C 201 1555 1555 1.44 CISPEP 1 ARG C 8 PRO C 9 0 -1.28 CISPEP 2 PHE H 146 PRO H 147 0 -10.72 CISPEP 3 GLU H 148 PRO H 149 0 -8.04 CISPEP 4 SER L 7 PRO L 8 0 -8.15 CISPEP 5 THR L 94 PRO L 95 0 0.20 CISPEP 6 TYR L 140 PRO L 141 0 4.21 CRYST1 166.767 166.767 100.693 90.00 90.00 120.00 P 64 2 2 12 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.005996 0.003462 0.000000 0.00000 SCALE2 0.000000 0.006924 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009931 0.00000