HEADER IMMUNE SYSTEM 19-MAY-20 6X1U TITLE STRUCTURE OF PHIS FAB (SC39-4) IN COMPLEX WITH PHIS MIMETIC PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SC39-4 HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SC39-4 LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ACLYANA-3-PTZA PEPTIDE; COMPND 11 CHAIN: D, C; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_TAXID: 9986; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 9 ORGANISM_TAXID: 9986; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 16 ORGANISM_TAXID: 32630 KEYWDS ANTI-PHOSPHOHISTIDINE ANTIBODY, POST-TRANSLATIONAL MODIFICATION, KEYWDS 2 IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.KALAGIRI,R.STANFIELD,I.A.WILSON,T.HUNTER REVDAT 1 03-FEB-21 6X1U 0 JRNL AUTH R.KALAGIRI,R.L.STANFIELD,J.MEISENHELDER,J.J.LA CLAIR, JRNL AUTH 2 S.R.FUHS,I.A.WILSON,T.HUNTER JRNL TITL STRUCTURAL BASIS FOR DIFFERENTIAL RECOGNITION OF JRNL TITL 2 PHOSPHOHISTIDINE CONTAINING PEPTIDES BY 1-PHIS AND 3-PHIS JRNL TITL 3 MONOCLONAL ANTIBODIES JRNL REF PROC.NATL.ACAD.SCI.USA 2020 JRNL REFN ESSN 1091-6490 JRNL DOI 10.1073/PNAS.2010644118 REMARK 2 REMARK 2 RESOLUTION. 1.64 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.16_3549: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.80 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 3 NUMBER OF REFLECTIONS : 116780 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 5819 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 46.8000 - 5.0964 0.98 3979 211 0.1628 0.1665 REMARK 3 2 5.0964 - 4.0459 1.00 3874 213 0.1300 0.1558 REMARK 3 3 4.0459 - 3.5347 0.99 3782 220 0.1601 0.1871 REMARK 3 4 3.5347 - 3.2116 1.00 3813 194 0.1753 0.2012 REMARK 3 5 3.2116 - 2.9814 1.00 3812 207 0.1822 0.2361 REMARK 3 6 2.9814 - 2.8057 1.00 3756 216 0.1961 0.2360 REMARK 3 7 2.8057 - 2.6652 1.00 3792 196 0.1906 0.1936 REMARK 3 8 2.6652 - 2.5492 1.00 3791 191 0.1853 0.2465 REMARK 3 9 2.5492 - 2.4510 1.00 3768 201 0.1986 0.2580 REMARK 3 10 2.4510 - 2.3665 1.00 3780 198 0.1931 0.2371 REMARK 3 11 2.3665 - 2.2925 1.00 3731 195 0.1936 0.2288 REMARK 3 12 2.2925 - 2.2269 1.00 3717 200 0.2002 0.2531 REMARK 3 13 2.2269 - 2.1683 1.00 3748 186 0.1981 0.2262 REMARK 3 14 2.1683 - 2.1154 1.00 3787 189 0.1895 0.2606 REMARK 3 15 2.1154 - 2.0673 1.00 3744 184 0.1942 0.2377 REMARK 3 16 2.0673 - 2.0233 0.99 3702 187 0.1939 0.2125 REMARK 3 17 2.0233 - 1.9828 0.99 3709 204 0.1892 0.2420 REMARK 3 18 1.9828 - 1.9454 0.99 3746 178 0.2144 0.2695 REMARK 3 19 1.9454 - 1.9107 0.99 3712 190 0.2493 0.2759 REMARK 3 20 1.9107 - 1.8783 0.99 3674 205 0.2343 0.2808 REMARK 3 21 1.8783 - 1.8480 0.99 3662 206 0.2355 0.2935 REMARK 3 22 1.8480 - 1.8196 0.99 3696 179 0.2344 0.2696 REMARK 3 23 1.8196 - 1.7928 0.98 3685 164 0.2389 0.2893 REMARK 3 24 1.7928 - 1.7676 0.98 3672 172 0.2492 0.2986 REMARK 3 25 1.7676 - 1.7437 0.98 3700 188 0.2700 0.3271 REMARK 3 26 1.7437 - 1.7210 0.98 3602 196 0.2767 0.3352 REMARK 3 27 1.7210 - 1.6995 0.98 3710 187 0.2842 0.2991 REMARK 3 28 1.6995 - 1.6790 0.98 3568 219 0.2933 0.3620 REMARK 3 29 1.6790 - 1.6595 0.98 3704 192 0.3080 0.3581 REMARK 3 30 1.6595 - 1.6410 0.69 2545 151 0.3290 0.3488 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.020 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.012 6679 REMARK 3 ANGLE : 1.331 9161 REMARK 3 CHIRALITY : 0.082 1077 REMARK 3 PLANARITY : 0.008 1170 REMARK 3 DIHEDRAL : 15.657 2415 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6X1U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1000249319. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-JUL-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97741 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116971 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640 REMARK 200 RESOLUTION RANGE LOW (A) : 46.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 4.500 REMARK 200 R MERGE (I) : 0.88000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : 1.51000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 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: 5DTF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 20 % REMARK 280 PEG3000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-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 33.53050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.63500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.05550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.63500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.53050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.05550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, D 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 SER H 216 REMARK 465 HIS H 217 REMARK 465 HIS H 218 REMARK 465 HIS H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 SER A 216 REMARK 465 HIS A 217 REMARK 465 HIS A 218 REMARK 465 HIS A 219 REMARK 465 HIS A 220 REMARK 465 HIS A 221 REMARK 465 HIS A 222 REMARK 465 ALA D 1 REMARK 465 GLY D 2 REMARK 465 ALA D 3 REMARK 465 ALA D 8 REMARK 465 GLY D 9 REMARK 465 ALA C 1 REMARK 465 GLY C 2 REMARK 465 ALA C 3 REMARK 465 ALA C 8 REMARK 465 GLY C 9 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 CYS H 92 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 CYS H 195 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 CYS A 195 CA - CB - SG ANGL. DEV. = 8.9 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 SER H 96 93.38 -167.25 REMARK 500 CYS H 130 101.61 -57.71 REMARK 500 ASP H 132 8.79 -69.13 REMARK 500 ALA L 51 -34.73 64.22 REMARK 500 ALA L 84 175.55 179.44 REMARK 500 SER A 96 93.32 -167.24 REMARK 500 CYS A 130 108.99 -56.89 REMARK 500 ALA B 51 -34.46 66.83 REMARK 500 LYS B 138 71.33 52.18 REMARK 500 ALA D 6 5.78 -153.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 619 DISTANCE = 6.03 ANGSTROMS REMARK 525 HOH A 563 DISTANCE = 7.15 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ACT L 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ACT L 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY C 4 and UKD C 5 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide UKD C 5 and ALA C 6 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY D 4 and UKD D 5 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide UKD D 5 and ALA D 6 DBREF 6X1U H 2 222 PDB 6X1U 6X1U 2 222 DBREF 6X1U L 3 211 PDB 6X1U 6X1U 3 211 DBREF 6X1U A 2 222 PDB 6X1U 6X1U 2 222 DBREF 6X1U B 3 211 PDB 6X1U 6X1U 3 211 DBREF 6X1U D 1 9 PDB 6X1U 6X1U 1 9 DBREF 6X1U C 1 9 PDB 6X1U 6X1U 1 9 SEQRES 1 H 221 PCA SER VAL GLU GLU SER GLY GLY ARG LEU VAL THR PRO SEQRES 2 H 221 GLY GLY SER LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 H 221 SER LEU SER ARG TYR ASN MET GLY TRP VAL ARG GLN ALA SEQRES 4 H 221 PRO GLY LYS GLY LEU GLU TRP ILE GLY TRP ILE PRO PHE SEQRES 5 H 221 ARG GLY SER LEU LYS TYR ALA THR TRP ALA THR GLY ARG SEQRES 6 H 221 PHE THR ILE SER ARG THR SER THR THR VAL ASP LEU ARG SEQRES 7 H 221 MET THR GLY LEU THR ALA ALA ASP THR ALA THR TYR PHE SEQRES 8 H 221 CYS VAL ARG SER SER ASP GLY PHE ASP LEU TRP GLY PRO SEQRES 9 H 221 GLY THR LEU VAL THR ILE SER SER SER SER GLY GLN PRO SEQRES 10 H 221 LYS ALA PRO SER VAL PHE PRO LEU ALA PRO CYS CYS GLY SEQRES 11 H 221 ASP THR PRO SER SER THR VAL THR LEU GLY CYS LEU VAL SEQRES 12 H 221 LYS GLY TYR LEU PRO GLU PRO VAL THR VAL THR TRP ASN SEQRES 13 H 221 SER GLY THR LEU THR ASN GLY VAL ARG THR PHE PRO SER SEQRES 14 H 221 VAL ARG GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 H 221 VAL SER VAL THR SER SER SER GLN PRO VAL THR CYS ASN SEQRES 16 H 221 VAL ALA HIS PRO ALA THR ASN THR LYS VAL ASP LYS THR SEQRES 17 H 221 VAL ALA PRO SER THR CYS SER HIS HIS HIS HIS HIS HIS SEQRES 1 L 213 ASP MET THR GLN THR PRO ALA SER VAL GLU ALA VAL VAL SEQRES 2 L 213 GLY GLY THR VAL THR ILE LYS CYS GLN ALA SER ARG ASP SEQRES 3 L 213 THR GLY ASP GLY LEU ILE TRP TYR GLN GLN LYS PRO GLY SEQRES 4 L 213 GLN PRO PRO LYS ARG LEU ILE TYR LYS ALA SER THR VAL SEQRES 5 L 213 ALA SER GLY VAL PRO SER ARG PHE LYS GLY ARG GLY SER SEQRES 6 L 213 GLY THR ASP PHE THR LEU THR ILE SER ASP LEU GLU CYS SEQRES 7 L 213 ALA ASP ALA ALA THR TYR TYR CYS HIS SER ASN PHE TYR SEQRES 8 L 213 ASN ARG TRP THR TYR GLY ASN ALA PHE GLY GLY GLY THR SEQRES 9 L 213 GLU VAL VAL VAL LYS GLY ASP PRO VAL ALA PRO THR VAL SEQRES 10 L 213 LEU ILE PHE PRO PRO ALA ALA ASP GLN VAL ALA THR GLY SEQRES 11 L 213 THR VAL THR ILE VAL CYS VAL ALA ASN LYS TYR PHE PRO SEQRES 12 L 213 ASP VAL THR VAL THR TRP GLU VAL ASP GLY THR THR GLN SEQRES 13 L 213 THR THR GLY ILE GLU ASN SER LYS THR PRO GLN ASN SER SEQRES 14 L 213 ALA ASP CYS THR TYR ASN LEU SER SER THR LEU THR LEU SEQRES 15 L 213 THR SER THR GLN TYR ASN SER HIS LYS GLU TYR THR CYS SEQRES 16 L 213 LYS VAL THR GLN GLY THR THR SER VAL VAL GLN SER PHE SEQRES 17 L 213 ASN ARG GLY ASP CYS SEQRES 1 A 221 PCA SER VAL GLU GLU SER GLY GLY ARG LEU VAL THR PRO SEQRES 2 A 221 GLY GLY SER LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 A 221 SER LEU SER ARG TYR ASN MET GLY TRP VAL ARG GLN ALA SEQRES 4 A 221 PRO GLY LYS GLY LEU GLU TRP ILE GLY TRP ILE PRO PHE SEQRES 5 A 221 ARG GLY SER LEU LYS TYR ALA THR TRP ALA THR GLY ARG SEQRES 6 A 221 PHE THR ILE SER ARG THR SER THR THR VAL ASP LEU ARG SEQRES 7 A 221 MET THR GLY LEU THR ALA ALA ASP THR ALA THR TYR PHE SEQRES 8 A 221 CYS VAL ARG SER SER ASP GLY PHE ASP LEU TRP GLY PRO SEQRES 9 A 221 GLY THR LEU VAL THR ILE SER SER SER SER GLY GLN PRO SEQRES 10 A 221 LYS ALA PRO SER VAL PHE PRO LEU ALA PRO CYS CYS GLY SEQRES 11 A 221 ASP THR PRO SER SER THR VAL THR LEU GLY CYS LEU VAL SEQRES 12 A 221 LYS GLY TYR LEU PRO GLU PRO VAL THR VAL THR TRP ASN SEQRES 13 A 221 SER GLY THR LEU THR ASN GLY VAL ARG THR PHE PRO SER SEQRES 14 A 221 VAL ARG GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 A 221 VAL SER VAL THR SER SER SER GLN PRO VAL THR CYS ASN SEQRES 16 A 221 VAL ALA HIS PRO ALA THR ASN THR LYS VAL ASP LYS THR SEQRES 17 A 221 VAL ALA PRO SER THR CYS SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 213 ASP MET THR GLN THR PRO ALA SER VAL GLU ALA VAL VAL SEQRES 2 B 213 GLY GLY THR VAL THR ILE LYS CYS GLN ALA SER ARG ASP SEQRES 3 B 213 THR GLY ASP GLY LEU ILE TRP TYR GLN GLN LYS PRO GLY SEQRES 4 B 213 GLN PRO PRO LYS ARG LEU ILE TYR LYS ALA SER THR VAL SEQRES 5 B 213 ALA SER GLY VAL PRO SER ARG PHE LYS GLY ARG GLY SER SEQRES 6 B 213 GLY THR ASP PHE THR LEU THR ILE SER ASP LEU GLU CYS SEQRES 7 B 213 ALA ASP ALA ALA THR TYR TYR CYS HIS SER ASN PHE TYR SEQRES 8 B 213 ASN ARG TRP THR TYR GLY ASN ALA PHE GLY GLY GLY THR SEQRES 9 B 213 GLU VAL VAL VAL LYS GLY ASP PRO VAL ALA PRO THR VAL SEQRES 10 B 213 LEU ILE PHE PRO PRO ALA ALA ASP GLN VAL ALA THR GLY SEQRES 11 B 213 THR VAL THR ILE VAL CYS VAL ALA ASN LYS TYR PHE PRO SEQRES 12 B 213 ASP VAL THR VAL THR TRP GLU VAL ASP GLY THR THR GLN SEQRES 13 B 213 THR THR GLY ILE GLU ASN SER LYS THR PRO GLN ASN SER SEQRES 14 B 213 ALA ASP CYS THR TYR ASN LEU SER SER THR LEU THR LEU SEQRES 15 B 213 THR SER THR GLN TYR ASN SER HIS LYS GLU TYR THR CYS SEQRES 16 B 213 LYS VAL THR GLN GLY THR THR SER VAL VAL GLN SER PHE SEQRES 17 B 213 ASN ARG GLY ASP CYS SEQRES 1 D 9 ALA GLY ALA GLY UKD ALA GLY ALA GLY SEQRES 1 C 9 ALA GLY ALA GLY UKD ALA GLY ALA GLY HET PCA H 2 8 HET PCA A 2 8 HET UKD D 5 14 HET UKD C 5 14 HET EDO H 301 4 HET EDO L 301 4 HET ACT L 302 4 HET ACT L 303 7 HET EDO B 301 4 HET ACT B 302 4 HET ACT B 303 4 HET ACT B 304 4 HETNAM PCA PYROGLUTAMIC ACID HETNAM UKD 3-(4-PHOSPHONO-1H-1,2,3-TRIAZOL-1-YL)-L-ALANINE HETNAM EDO 1,2-ETHANEDIOL HETNAM ACT ACETATE ION HETSYN UKD PHIS HETSYN EDO ETHYLENE GLYCOL FORMUL 1 PCA 2(C5 H7 N O3) FORMUL 5 UKD 2(C5 H9 N4 O5 P) FORMUL 7 EDO 3(C2 H6 O2) FORMUL 9 ACT 5(C2 H3 O2 1-) FORMUL 15 HOH *979(H2 O) HELIX 1 AA1 THR H 83 THR H 87 5 5 HELIX 2 AA2 SER H 158 THR H 160 5 3 HELIX 3 AA3 THR H 187 GLN H 191 5 5 HELIX 4 AA4 PRO H 200 ASN H 203 5 4 HELIX 5 AA5 GLU L 79 ALA L 83 5 5 HELIX 6 AA6 GLN L 124 THR L 127 5 4 HELIX 7 AA7 SER L 182 SER L 187 1 6 HELIX 8 AA8 GLY L 209 CYS L 211 5 3 HELIX 9 AA9 THR A 83 THR A 87 5 5 HELIX 10 AB1 SER A 158 THR A 160 5 3 HELIX 11 AB2 THR A 187 GLN A 191 5 5 HELIX 12 AB3 PRO A 200 ASN A 203 5 4 HELIX 13 AB4 GLU B 79 ALA B 83 5 5 HELIX 14 AB5 GLN B 124 THR B 127 5 4 HELIX 15 AB6 SER B 182 SER B 187 1 6 HELIX 16 AB7 GLY B 209 CYS B 211 5 3 SHEET 1 AA1 4 SER H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 23 N GLU H 5 SHEET 3 AA1 4 THR H 75 MET H 80 -1 O MET H 80 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ARG H 71 -1 N THR H 68 O ARG H 79 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 ILE H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 ASN H 33 GLN H 39 -1 N VAL H 37 O PHE H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AA2 6 LYS H 58 TYR H 59 -1 O LYS H 58 N TRP H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 ILE H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 PHE H 99 TRP H 103 -1 O LEU H 102 N ARG H 94 SHEET 1 AA4 4 SER H 122 LEU H 126 0 SHEET 2 AA4 4 VAL H 138 TYR H 147 -1 O LEU H 143 N PHE H 124 SHEET 3 AA4 4 TYR H 178 VAL H 186 -1 O LEU H 180 N VAL H 144 SHEET 4 AA4 4 VAL H 165 THR H 167 -1 N ARG H 166 O VAL H 183 SHEET 1 AA5 4 SER H 122 LEU H 126 0 SHEET 2 AA5 4 VAL H 138 TYR H 147 -1 O LEU H 143 N PHE H 124 SHEET 3 AA5 4 TYR H 178 VAL H 186 -1 O LEU H 180 N VAL H 144 SHEET 4 AA5 4 VAL H 171 ARG H 172 -1 N VAL H 171 O SER H 179 SHEET 1 AA6 3 THR H 153 TRP H 156 0 SHEET 2 AA6 3 VAL H 193 HIS H 199 -1 O ASN H 196 N THR H 155 SHEET 3 AA6 3 THR H 204 VAL H 210 -1 O VAL H 206 N VAL H 197 SHEET 1 AA7 4 MET L 4 THR L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O LYS L 22 N THR L 7 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N LYS L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 VAL L 14 0 SHEET 2 AA8 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AA8 6 ALA L 84 SER L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 THR L 53 VAL L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA9 4 THR L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 TYR L 139 -1 O ASN L 137 N THR L 114 SHEET 3 AA9 4 TYR L 172 THR L 181 -1 O SER L 176 N CYS L 134 SHEET 4 AA9 4 ILE L 158 LYS L 162 -1 N SER L 161 O SER L 175 SHEET 1 AB1 4 THR L 152 THR L 153 0 SHEET 2 AB1 4 THR L 144 VAL L 149 -1 N VAL L 149 O THR L 152 SHEET 3 AB1 4 GLU L 190 GLN L 197 -1 O LYS L 194 N THR L 146 SHEET 4 AB1 4 THR L 200 ASN L 207 -1 O THR L 200 N GLN L 197 SHEET 1 AB2 4 SER A 3 SER A 7 0 SHEET 2 AB2 4 LEU A 18 SER A 25 -1 O THR A 23 N GLU A 5 SHEET 3 AB2 4 THR A 75 MET A 80 -1 O MET A 80 N LEU A 18 SHEET 4 AB2 4 PHE A 67 ARG A 71 -1 N THR A 68 O ARG A 79 SHEET 1 AB3 6 LEU A 11 VAL A 12 0 SHEET 2 AB3 6 THR A 107 ILE A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB3 6 ALA A 88 SER A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AB3 6 ASN A 33 GLN A 39 -1 N VAL A 37 O PHE A 91 SHEET 5 AB3 6 GLU A 46 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AB3 6 LYS A 58 TYR A 59 -1 O LYS A 58 N TRP A 50 SHEET 1 AB4 4 LEU A 11 VAL A 12 0 SHEET 2 AB4 4 THR A 107 ILE A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB4 4 ALA A 88 SER A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AB4 4 PHE A 99 TRP A 103 -1 O LEU A 102 N ARG A 94 SHEET 1 AB5 4 SER A 122 LEU A 126 0 SHEET 2 AB5 4 VAL A 138 TYR A 147 -1 O GLY A 141 N LEU A 126 SHEET 3 AB5 4 TYR A 178 VAL A 186 -1 O LEU A 180 N VAL A 144 SHEET 4 AB5 4 VAL A 165 THR A 167 -1 N ARG A 166 O VAL A 183 SHEET 1 AB6 4 SER A 122 LEU A 126 0 SHEET 2 AB6 4 VAL A 138 TYR A 147 -1 O GLY A 141 N LEU A 126 SHEET 3 AB6 4 TYR A 178 VAL A 186 -1 O LEU A 180 N VAL A 144 SHEET 4 AB6 4 VAL A 171 ARG A 172 -1 N VAL A 171 O SER A 179 SHEET 1 AB7 3 THR A 153 TRP A 156 0 SHEET 2 AB7 3 VAL A 193 HIS A 199 -1 O ASN A 196 N THR A 155 SHEET 3 AB7 3 THR A 204 VAL A 210 -1 O VAL A 206 N VAL A 197 SHEET 1 AB8 4 MET B 4 THR B 7 0 SHEET 2 AB8 4 VAL B 19 ALA B 25 -1 O LYS B 22 N THR B 7 SHEET 3 AB8 4 ASP B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AB8 4 PHE B 62 SER B 67 -1 N ARG B 65 O THR B 72 SHEET 1 AB9 6 SER B 10 VAL B 14 0 SHEET 2 AB9 6 THR B 102 LYS B 107 1 O VAL B 105 N VAL B 11 SHEET 3 AB9 6 ALA B 84 SER B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AB9 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AB9 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AB9 6 THR B 53 VAL B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AC1 4 THR B 114 PHE B 118 0 SHEET 2 AC1 4 THR B 129 TYR B 139 -1 O ASN B 137 N THR B 114 SHEET 3 AC1 4 TYR B 172 THR B 181 -1 O SER B 176 N CYS B 134 SHEET 4 AC1 4 ILE B 158 LYS B 162 -1 N GLU B 159 O THR B 177 SHEET 1 AC2 4 THR B 152 THR B 153 0 SHEET 2 AC2 4 THR B 144 VAL B 149 -1 N VAL B 149 O THR B 152 SHEET 3 AC2 4 GLU B 190 GLN B 197 -1 O LYS B 194 N THR B 146 SHEET 4 AC2 4 THR B 200 ASN B 207 -1 O THR B 200 N GLN B 197 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.02 SSBOND 2 CYS H 129 CYS L 211 1555 1555 2.03 SSBOND 3 CYS H 130 CYS H 215 1555 1555 2.04 SSBOND 4 CYS H 142 CYS H 195 1555 1555 2.04 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.18 SSBOND 6 CYS L 80 CYS L 170 1555 1555 2.08 SSBOND 7 CYS L 134 CYS L 193 1555 1555 1.99 SSBOND 8 CYS A 22 CYS A 92 1555 1555 2.14 SSBOND 9 CYS A 129 CYS B 211 1555 1555 2.03 SSBOND 10 CYS A 130 CYS A 215 1555 1555 2.04 SSBOND 11 CYS A 142 CYS A 195 1555 1555 2.04 SSBOND 12 CYS B 23 CYS B 88 1555 1555 2.20 SSBOND 13 CYS B 80 CYS B 170 1555 1555 2.08 SSBOND 14 CYS B 134 CYS B 193 1555 1555 2.00 LINK C PCA H 2 N SER H 3 1555 1555 1.33 LINK C PCA A 2 N SER A 3 1555 1555 1.34 LINK C GLY D 4 N UKD D 5 1555 1555 1.33 LINK C UKD D 5 N ALA D 6 1555 1555 1.32 LINK C GLY C 4 N UKD C 5 1555 1555 1.33 LINK C UKD C 5 N ALA C 6 1555 1555 1.33 CISPEP 1 LEU H 148 PRO H 149 0 -7.80 CISPEP 2 GLU H 150 PRO H 151 0 -1.49 CISPEP 3 GLN H 191 PRO H 192 0 -3.43 CISPEP 4 THR L 7 PRO L 8 0 -10.06 CISPEP 5 PHE L 140 PRO L 141 0 0.81 CISPEP 6 LEU A 148 PRO A 149 0 -10.10 CISPEP 7 GLU A 150 PRO A 151 0 0.70 CISPEP 8 GLN A 191 PRO A 192 0 7.73 CISPEP 9 THR B 7 PRO B 8 0 -10.62 CISPEP 10 PHE B 140 PRO B 141 0 2.78 SITE 1 AC1 8 PHE H 168 PRO H 169 SER H 179 LEU H 180 SITE 2 AC1 8 SER H 181 SER L 175 THR L 177 HOH L 497 SITE 1 AC2 4 GLN L 37 LYS L 45 PRO L 59 HOH L 431 SITE 1 AC3 4 ASP L 3 SER L 26 ARG L 27 TYR L 95C SITE 1 AC4 6 LYS H 58 HOH H 610 TYR L 93 ASN L 94 SITE 2 AC4 6 ARG L 95 TRP L 95A SITE 1 AC5 6 LYS A 58 TYR B 93 ASN B 94 ARG B 95 SITE 2 AC5 6 THR B 95B HOH B 429 SITE 1 AC6 4 ASP B 3 SER B 26 ARG B 27 TYR B 95C SITE 1 AC7 3 SER B 187 HOH B 405 ASN H 157 SITE 1 AC8 6 GLN B 37 LYS B 45 LEU B 47 PRO B 59 SITE 2 AC8 6 PHE B 62 HOH B 479 SITE 1 AC9 18 ASN A 33 TRP A 50 ARG A 54 SER A 95 SITE 2 AC9 18 SER A 96 ASP A 97 GLY A 98 ASN B 91 SITE 3 AC9 18 PHE B 92 TYR B 93 ASN B 94 ARG B 95 SITE 4 AC9 18 HOH B 414 ALA C 6 HOH C 101 HOH C 102 SITE 5 AC9 18 HOH C 103 HOH C 105 SITE 1 AD1 19 ASN A 33 TRP A 50 SER A 95 SER A 96 SITE 2 AD1 19 ASP A 97 GLY A 98 ASN B 91 PHE B 92 SITE 3 AD1 19 TYR B 93 ASN B 94 ARG B 95 HOH B 414 SITE 4 AD1 19 GLY C 4 GLY C 7 HOH C 101 HOH C 102 SITE 5 AD1 19 HOH C 103 HOH C 105 HOH C 106 SITE 1 AD2 17 ALA D 6 HOH D 101 HOH D 102 HOH D 104 SITE 2 AD2 17 HOH D 105 ASN H 33 TRP H 50 SER H 95 SITE 3 AD2 17 SER H 96 ASP H 97 GLY H 98 ASN L 91 SITE 4 AD2 17 PHE L 92 TYR L 93 ASN L 94 ARG L 95 SITE 5 AD2 17 HOH L 418 SITE 1 AD3 19 GLY D 4 GLY D 7 HOH D 101 HOH D 102 SITE 2 AD3 19 HOH D 104 HOH D 105 HOH D 106 ASN H 33 SITE 3 AD3 19 TRP H 50 SER H 95 SER H 96 ASP H 97 SITE 4 AD3 19 GLY H 98 ASN L 91 PHE L 92 TYR L 93 SITE 5 AD3 19 ASN L 94 ARG L 95 HOH L 418 CRYST1 67.061 86.111 167.270 90.00 90.00 90.00 P 21 21 21 8 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 0.014912 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011613 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005978 0.00000