HEADER HYDROLASE 17-AUG-17 5QCG
TITLE CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN S;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.22.27;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CTSS;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS D3R, CATHEPSIN S, LIGAND DOCKING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,S.K.BURLEY
REVDAT 5 17-NOV-21 5QCG 1 REMARK
REVDAT 4 10-FEB-21 5QCG 1 AUTHOR JRNL
REVDAT 3 06-JUN-18 5QCG 1 REMARK ATOM
REVDAT 2 21-FEB-18 5QCG 1 REMARK
REVDAT 1 20-DEC-17 5QCG 0
JRNL AUTH S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,
JRNL AUTH 2 S.K.BURLEY
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 14136
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) : 0.187
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 717
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 29.2715 - 4.6035 0.99 2757 144 0.1628 0.2292
REMARK 3 2 4.6035 - 3.6561 0.98 2727 151 0.1555 0.2485
REMARK 3 3 3.6561 - 3.1946 0.97 2677 149 0.1786 0.2988
REMARK 3 4 3.1946 - 2.9028 0.96 2720 128 0.2256 0.2964
REMARK 3 5 2.9028 - 2.6949 0.92 2538 145 0.2521 0.3545
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) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.009 3585
REMARK 3 ANGLE : 0.977 4867
REMARK 3 CHIRALITY : 0.059 483
REMARK 3 PLANARITY : 0.006 623
REMARK 3 DIHEDRAL : 12.715 2059
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 5QCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1001401773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14136
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.695
REMARK 200 RESOLUTION RANGE LOW (A) : 29.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> 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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE PH 4.5, 200MM
REMARK 280 AMMONIUM ACETATE, 25% PEG 8000. PROTEIN CONCENTRATION 7 MG/ML,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 4.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ILE A 0
REMARK 465 GLY A 220
REMARK 465 GLY A 221
REMARK 465 GLY A 222
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 LYS A 60 CD CE NZ
REMARK 470 LYS A 82 CE NZ
REMARK 470 LYS A 98 CG CD CE NZ
REMARK 470 LYS A 112 NZ
REMARK 470 ILE B 0 CG1 CG2 CD1
REMARK 470 LYS B 41 CG CD CE NZ
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 LYS B 60 CD CE NZ
REMARK 470 LYS B 82 CE NZ
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 470 LYS B 112 NZ
REMARK 470 ARG B 141 CG CD NE CZ NH1 NH2
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 O HIS A 205 O HOH A 901 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 THR A 58 -127.05 -125.55
REMARK 500 ASN A 163 16.11 -151.08
REMARK 500 ASN A 175 54.52 37.61
REMARK 500 THR B 58 -128.38 -127.88
REMARK 500 ASN B 163 14.53 -149.23
REMARK 500 ASN B 175 56.45 37.68
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 A 998 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B 998 DISTANCE = 6.18 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BJJ A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BJJ B 802
DBREF 5QCG A 0 217 UNP P25774 CATS_HUMAN 114 331
DBREF 5QCG B 0 217 UNP P25774 CATS_HUMAN 114 331
SEQADV 5QCG SER A 25 UNP P25774 CYS 139 ENGINEERED MUTATION
SEQADV 5QCG LEU A 218 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLN A 219 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLY A 220 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLY A 221 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLY A 222 UNP P25774 EXPRESSION TAG
SEQADV 5QCG SER B 25 UNP P25774 CYS 139 ENGINEERED MUTATION
SEQADV 5QCG LEU B 218 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLN B 219 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLY B 220 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLY B 221 UNP P25774 EXPRESSION TAG
SEQADV 5QCG GLY B 222 UNP P25774 EXPRESSION TAG
SEQRES 1 A 223 ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS
SEQRES 2 A 223 VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA SER
SEQRES 3 A 223 TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU
SEQRES 4 A 223 LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN
SEQRES 5 A 223 ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS
SEQRES 6 A 223 GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR
SEQRES 7 A 223 ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR
SEQRES 8 A 223 PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER
SEQRES 9 A 223 LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU
SEQRES 10 A 223 PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA
SEQRES 11 A 223 ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS
SEQRES 12 A 223 PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU
SEQRES 13 A 223 PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL
SEQRES 14 A 223 VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU
SEQRES 15 A 223 VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY
SEQRES 16 A 223 TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY
SEQRES 17 A 223 ILE ALA SER PHE PRO SER TYR PRO GLU ILE LEU GLN GLY
SEQRES 18 A 223 GLY GLY
SEQRES 1 B 223 ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS
SEQRES 2 B 223 VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA SER
SEQRES 3 B 223 TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU
SEQRES 4 B 223 LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN
SEQRES 5 B 223 ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS
SEQRES 6 B 223 GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR
SEQRES 7 B 223 ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR
SEQRES 8 B 223 PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER
SEQRES 9 B 223 LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU
SEQRES 10 B 223 PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA
SEQRES 11 B 223 ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS
SEQRES 12 B 223 PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU
SEQRES 13 B 223 PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL
SEQRES 14 B 223 VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU
SEQRES 15 B 223 VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY
SEQRES 16 B 223 TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY
SEQRES 17 B 223 ILE ALA SER PHE PRO SER TYR PRO GLU ILE LEU GLN GLY
SEQRES 18 B 223 GLY GLY
HET SO4 A 801 5
HET BJJ A 802 47
HET SO4 B 801 5
HET BJJ B 802 47
HETNAM SO4 SULFATE ION
HETNAM BJJ N-BENZYL-1-{2-CHLORO-5-[2-(2-CHLORO-5-{5-
HETNAM 2 BJJ (METHYLSULFONYL)-1-[3-(MORPHOLIN-4-YL)PROPYL]-4,5,6,7-
HETNAM 3 BJJ TETRAHYDRO-1H-PYRAZOLO[4,3-C]PYRIDIN-3-YL}PHENYL)
HETNAM 4 BJJ ETHYL]PHENYL}METHANAMINE
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 BJJ 2(C36 H43 CL2 N5 O3 S)
FORMUL 7 HOH *196(H2 O)
HELIX 1 AA1 ARG A 8 GLY A 11 5 4
HELIX 2 AA2 ALA A 24 GLY A 43 1 20
HELIX 3 AA3 SER A 49 SER A 57 1 9
HELIX 4 AA4 THR A 58 GLY A 62 5 5
HELIX 5 AA5 LYS A 64 GLY A 68 5 5
HELIX 6 AA6 PHE A 70 LYS A 82 1 13
HELIX 7 AA7 ASP A 102 LYS A 104 5 3
HELIX 8 AA8 ARG A 120 LYS A 131 1 12
HELIX 9 AA9 HIS A 142 TYR A 148 1 7
HELIX 10 AB1 ASN A 204 ILE A 208 5 5
HELIX 11 AB2 ALA B 24 GLY B 43 1 20
HELIX 12 AB3 SER B 49 SER B 57 1 9
HELIX 13 AB4 THR B 58 GLY B 62 5 5
HELIX 14 AB5 LYS B 64 GLY B 68 5 5
HELIX 15 AB6 PHE B 70 LYS B 82 1 13
HELIX 16 AB7 ASP B 102 LYS B 104 5 3
HELIX 17 AB8 ARG B 120 LYS B 131 1 12
HELIX 18 AB9 HIS B 142 TYR B 148 1 7
HELIX 19 AC1 ASN B 204 ILE B 208 5 5
SHEET 1 AA1 3 VAL A 5 ASP A 6 0
SHEET 2 AA1 3 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 AA1 3 VAL A 134 VAL A 138 -1 N VAL A 136 O VAL A 166
SHEET 1 AA2 5 VAL A 5 ASP A 6 0
SHEET 2 AA2 5 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 AA2 5 LYS A 177 LYS A 183 -1 O LYS A 183 N LEU A 167
SHEET 4 AA2 5 TYR A 195 ALA A 199 -1 O MET A 198 N TRP A 180
SHEET 5 AA2 5 VAL A 152 TYR A 153 1 N TYR A 153 O ARG A 197
SHEET 1 AA3 2 ILE A 84 ASP A 85 0
SHEET 2 AA3 2 ARG A 106 ALA A 108 -1 O ALA A 107 N ILE A 84
SHEET 1 AA4 2 LYS A 112 GLU A 115 0
SHEET 2 AA4 2 SER A 213 GLU A 216 -1 O GLU A 216 N LYS A 112
SHEET 1 AA5 3 VAL B 5 ASP B 6 0
SHEET 2 AA5 3 GLY B 165 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 AA5 3 VAL B 134 GLY B 137 -1 N VAL B 134 O VAL B 168
SHEET 1 AA6 5 VAL B 5 ASP B 6 0
SHEET 2 AA6 5 GLY B 165 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 AA6 5 LYS B 177 LYS B 183 -1 O LYS B 183 N LEU B 167
SHEET 4 AA6 5 TYR B 195 ALA B 199 -1 O MET B 198 N TRP B 180
SHEET 5 AA6 5 VAL B 152 TYR B 153 1 N TYR B 153 O ARG B 197
SHEET 1 AA7 2 ILE B 84 ASP B 85 0
SHEET 2 AA7 2 ARG B 106 ALA B 108 -1 O ALA B 107 N ILE B 84
SHEET 1 AA8 2 LYS B 112 GLU B 115 0
SHEET 2 AA8 2 SER B 213 GLU B 216 -1 O GLU B 216 N LYS B 112
SSBOND 1 CYS A 22 CYS A 66 1555 1555 2.03
SSBOND 2 CYS A 56 CYS A 99 1555 1555 2.03
SSBOND 3 CYS A 158 CYS A 206 1555 1555 2.03
SSBOND 4 CYS B 22 CYS B 66 1555 1555 2.04
SSBOND 5 CYS B 56 CYS B 99 1555 1555 2.07
SSBOND 6 CYS B 158 CYS B 206 1555 1555 2.01
SITE 1 AC1 8 GLN A 19 GLY A 23 ALA A 24 SER A 25
SITE 2 AC1 8 HIS A 164 BJJ A 802 HOH A 936 HOH A 953
SITE 1 AC2 15 PHE A 70 ARG A 141 ASN A 161 VAL A 162
SITE 2 AC2 15 ASN A 163 HIS A 164 GLY A 165 PHE A 211
SITE 3 AC2 15 SO4 A 801 HOH A 905 HOH A 918 HOH A 957
SITE 4 AC2 15 LYS B 41 THR B 42 TYR B 118
SITE 1 AC3 9 GLN B 19 GLY B 23 ALA B 24 SER B 25
SITE 2 AC3 9 ASN B 163 HIS B 164 BJJ B 802 HOH B 948
SITE 3 AC3 9 HOH B 965
SITE 1 AC4 16 LYS A 41 THR A 42 TYR A 118 PHE B 70
SITE 2 AC4 16 ALA B 140 ASN B 161 VAL B 162 ASN B 163
SITE 3 AC4 16 HIS B 164 GLY B 165 PHE B 211 SO4 B 801
SITE 4 AC4 16 HOH B 921 HOH B 923 HOH B 954 HOH B 957
CRYST1 53.789 53.645 53.905 106.95 110.21 93.54 P 1 2
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 0.018591 0.001151 0.007668 0.00000
SCALE2 0.000000 0.018677 0.006619 0.00000
SCALE3 0.000000 0.000000 0.020973 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
