HEADER HYDROLASE 26-JUN-16 5KMB
TITLE HUMAN HISTIDINE TRIAD NUCLEOTIDE BINDING PROTEIN 1 (HHINT1) H112N
TITLE 2 MUTANT NUCLEOSIDE L-TRP PHOSPHORAMIDATE SUBSTRATE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADENOSINE 5'-MONOPHOSPHORAMIDASE;
COMPND 5 EC: 3.-.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: HINT1, HINT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS HINT, HISTIDINE TRIAD, HIT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.MAIZE,B.C.FINZEL
REVDAT 5 27-SEP-23 5KMB 1 COMPND JRNL HETNAM
REVDAT 4 15-NOV-17 5KMB 1 JRNL
REVDAT 3 18-OCT-17 5KMB 1 JRNL
REVDAT 2 26-JUL-17 5KMB 1 JRNL
REVDAT 1 28-JUN-17 5KMB 0
JRNL AUTH K.M.MAIZE,R.SHAH,A.STROM,S.KUMARAPPERUMA,A.ZHOU,C.R.WAGNER,
JRNL AUTH 2 B.C.FINZEL
JRNL TITL A CRYSTAL STRUCTURE BASED GUIDE TO THE DESIGN OF HUMAN
JRNL TITL 2 HISTIDINE TRIAD NUCLEOTIDE BINDING PROTEIN 1 (HHINT1)
JRNL TITL 3 ACTIVATED PROTIDES.
JRNL REF MOL. PHARM. V. 14 3987 2017
JRNL REFN ESSN 1543-8392
JRNL PMID 28968488
JRNL DOI 10.1021/ACS.MOLPHARMACEUT.7B00664
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 29705
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.670
REMARK 3 FREE R VALUE TEST SET COUNT : 1388
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 34.3920 - 3.4461 0.96 2845 146 0.1408 0.1466
REMARK 3 2 3.4461 - 2.7356 0.98 2847 142 0.1574 0.1724
REMARK 3 3 2.7356 - 2.3899 0.99 2873 115 0.1655 0.1679
REMARK 3 4 2.3899 - 2.1714 0.99 2865 149 0.1472 0.1812
REMARK 3 5 2.1714 - 2.0158 0.99 2848 129 0.1510 0.1764
REMARK 3 6 2.0158 - 1.8970 0.99 2809 155 0.1537 0.1723
REMARK 3 7 1.8970 - 1.8020 0.99 2851 132 0.1576 0.2121
REMARK 3 8 1.8020 - 1.7235 0.98 2780 148 0.1698 0.1930
REMARK 3 9 1.7235 - 1.6572 0.98 2783 154 0.1735 0.2283
REMARK 3 10 1.6572 - 1.6000 0.97 2816 118 0.1703 0.2273
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.21
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 : 0.007 1860
REMARK 3 ANGLE : 1.204 2525
REMARK 3 CHIRALITY : 0.048 271
REMARK 3 PLANARITY : 0.005 328
REMARK 3 DIHEDRAL : 13.673 697
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 5KMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222230.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29718
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 63.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
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: PHASER 2.5.6
REMARK 200 STARTING MODEL: 3TW2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 33% PEG 8000, PH 6.7,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.91600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.15900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.91600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.15900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 396 LIES ON A SPECIAL POSITION.
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 A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 GLU A 4
REMARK 465 ILE A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 ALA A 8
REMARK 465 GLN A 9
REMARK 465 VAL A 10
REMARK 465 ALA A 11
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ASP B 3
REMARK 465 GLU B 4
REMARK 465 ILE B 5
REMARK 465 ALA B 6
REMARK 465 LYS B 7
REMARK 465 ALA B 8
REMARK 465 GLN B 9
REMARK 465 VAL B 10
REMARK 465 ALA B 11
REMARK 465 ARG B 12
REMARK 465 PRO B 13
REMARK 465 GLY B 14
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 ARG A 12 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 HOH A 384 O HOH B 372 2.11
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 B 35 -157.48 -137.53
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 410 DISTANCE = 6.62 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6UT A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TW2 RELATED DB: PDB
REMARK 900 RELATED ID: 5IPB RELATED DB: PDB
REMARK 900 RELATED ID: 5IPC RELATED DB: PDB
REMARK 900 RELATED ID: 5IPD RELATED DB: PDB
REMARK 900 RELATED ID: 5IPE RELATED DB: PDB
REMARK 900 RELATED ID: 5KLY RELATED DB: PDB
REMARK 900 RELATED ID: 5KLZ RELATED DB: PDB
REMARK 900 RELATED ID: 5KM0 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM1 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM2 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM3 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM4 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM5 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM6 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM7 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM8 RELATED DB: PDB
REMARK 900 RELATED ID: 5KM9 RELATED DB: PDB
REMARK 900 RELATED ID: 5KMA RELATED DB: PDB
REMARK 900 RELATED ID: 5KMC RELATED DB: PDB
DBREF 5KMB A 1 126 UNP P49773 HINT1_HUMAN 1 126
DBREF 5KMB B 1 126 UNP P49773 HINT1_HUMAN 1 126
SEQADV 5KMB SER A -2 UNP P49773 EXPRESSION TAG
SEQADV 5KMB ASN A -1 UNP P49773 EXPRESSION TAG
SEQADV 5KMB ALA A 0 UNP P49773 EXPRESSION TAG
SEQADV 5KMB ASN A 112 UNP P49773 HIS 112 ENGINEERED MUTATION
SEQADV 5KMB SER B -2 UNP P49773 EXPRESSION TAG
SEQADV 5KMB ASN B -1 UNP P49773 EXPRESSION TAG
SEQADV 5KMB ALA B 0 UNP P49773 EXPRESSION TAG
SEQADV 5KMB ASN B 112 UNP P49773 HIS 112 ENGINEERED MUTATION
SEQRES 1 A 129 SER ASN ALA MET ALA ASP GLU ILE ALA LYS ALA GLN VAL
SEQRES 2 A 129 ALA ARG PRO GLY GLY ASP THR ILE PHE GLY LYS ILE ILE
SEQRES 3 A 129 ARG LYS GLU ILE PRO ALA LYS ILE ILE PHE GLU ASP ASP
SEQRES 4 A 129 ARG CYS LEU ALA PHE HIS ASP ILE SER PRO GLN ALA PRO
SEQRES 5 A 129 THR HIS PHE LEU VAL ILE PRO LYS LYS HIS ILE SER GLN
SEQRES 6 A 129 ILE SER VAL ALA GLU ASP ASP ASP GLU SER LEU LEU GLY
SEQRES 7 A 129 HIS LEU MET ILE VAL GLY LYS LYS CYS ALA ALA ASP LEU
SEQRES 8 A 129 GLY LEU ASN LYS GLY TYR ARG MET VAL VAL ASN GLU GLY
SEQRES 9 A 129 SER ASP GLY GLY GLN SER VAL TYR HIS VAL ASN LEU HIS
SEQRES 10 A 129 VAL LEU GLY GLY ARG GLN MET HIS TRP PRO PRO GLY
SEQRES 1 B 129 SER ASN ALA MET ALA ASP GLU ILE ALA LYS ALA GLN VAL
SEQRES 2 B 129 ALA ARG PRO GLY GLY ASP THR ILE PHE GLY LYS ILE ILE
SEQRES 3 B 129 ARG LYS GLU ILE PRO ALA LYS ILE ILE PHE GLU ASP ASP
SEQRES 4 B 129 ARG CYS LEU ALA PHE HIS ASP ILE SER PRO GLN ALA PRO
SEQRES 5 B 129 THR HIS PHE LEU VAL ILE PRO LYS LYS HIS ILE SER GLN
SEQRES 6 B 129 ILE SER VAL ALA GLU ASP ASP ASP GLU SER LEU LEU GLY
SEQRES 7 B 129 HIS LEU MET ILE VAL GLY LYS LYS CYS ALA ALA ASP LEU
SEQRES 8 B 129 GLY LEU ASN LYS GLY TYR ARG MET VAL VAL ASN GLU GLY
SEQRES 9 B 129 SER ASP GLY GLY GLN SER VAL TYR HIS VAL ASN LEU HIS
SEQRES 10 B 129 VAL LEU GLY GLY ARG GLN MET HIS TRP PRO PRO GLY
HET 6UT A 201 39
HET CL B 201 1
HETNAM 6UT [(2~{R},3~{S},4~{R},5~{R})-5-(2-AZANYL-6-OXIDANYLIDENE-
HETNAM 2 6UT 1~{H}-PURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-
HETNAM 3 6UT YL]METHOXY-~{N}-[(2~ {S})-3-(1~{H}-INDOL-3-YL)-1-
HETNAM 4 6UT (METHYLAMINO)-1-OXIDANYLIDENE-PROPAN-2-
HETNAM 5 6UT YL]PHOSPHONAMIDIC ACID
HETNAM CL CHLORIDE ION
HETSYN 6UT L-TRP-G
FORMUL 3 6UT C22 H27 N8 O8 P
FORMUL 4 CL CL 1-
FORMUL 5 HOH *215(H2 O)
HELIX 1 AA1 THR A 17 ARG A 24 1 8
HELIX 2 AA2 GLN A 62 ALA A 66 5 5
HELIX 3 AA3 GLU A 67 ASP A 69 5 3
HELIX 4 AA4 ASP A 70 LEU A 88 1 19
HELIX 5 AA5 GLY A 101 GLY A 105 1 5
HELIX 6 AA6 THR B 17 ARG B 24 1 8
HELIX 7 AA7 GLN B 62 ALA B 66 5 5
HELIX 8 AA8 GLU B 67 ASP B 69 5 3
HELIX 9 AA9 ASP B 70 LEU B 88 1 19
SHEET 1 AA110 ILE A 31 GLU A 34 0
SHEET 2 AA110 CYS A 38 HIS A 42 -1 O ALA A 40 N ILE A 32
SHEET 3 AA110 THR A 50 PRO A 56 -1 O LEU A 53 N PHE A 41
SHEET 4 AA110 LEU A 113 GLY A 117 -1 O VAL A 115 N PHE A 52
SHEET 5 AA110 TYR A 94 GLU A 100 -1 N VAL A 97 O HIS A 114
SHEET 6 AA110 TYR B 94 GLU B 100 -1 O VAL B 98 N MET A 96
SHEET 7 AA110 LEU B 113 GLY B 117 -1 O HIS B 114 N VAL B 97
SHEET 8 AA110 THR B 50 PRO B 56 -1 N VAL B 54 O LEU B 113
SHEET 9 AA110 CYS B 38 HIS B 42 -1 N PHE B 41 O LEU B 53
SHEET 10 AA110 ILE B 31 GLU B 34 -1 N ILE B 32 O ALA B 40
CISPEP 1 TRP A 123 PRO A 124 0 -1.77
CISPEP 2 TRP B 123 PRO B 124 0 1.93
SITE 1 AC1 24 ILE A 18 PHE A 19 PHE A 41 HIS A 42
SITE 2 AC1 24 ASP A 43 ILE A 44 SER A 45 LEU A 53
SITE 3 AC1 24 ASN A 99 GLY A 105 GLN A 106 SER A 107
SITE 4 AC1 24 VAL A 108 ASN A 112 HIS A 114 HOH A 305
SITE 5 AC1 24 HOH A 332 HOH A 336 HOH A 342 HOH A 344
SITE 6 AC1 24 HOH A 352 ARG B 95 MET B 121 TRP B 123
SITE 1 AC2 5 ASN B 99 GLN B 106 SER B 107 ASN B 112
SITE 2 AC2 5 HIS B 114
CRYST1 77.832 46.318 64.077 90.00 94.47 90.00 C 1 2 1 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 0.012848 0.000000 0.001003 0.00000
SCALE2 0.000000 0.021590 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015654 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
