HEADER COMPLEX (SERINE PROTEASE/INHIBITOR) 27-DEC-94 1LHG
TITLE HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-
TITLE 2 BOROORNITHINE-OH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-THROMBIN;
COMPND 3 CHAIN: L;
COMPND 4 EC: 3.4.21.5;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ALPHA-THROMBIN;
COMPND 7 CHAIN: H;
COMPND 8 EC: 3.4.21.5;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HIRUDIN;
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: RESIDUES 54 - 65;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BLOOD;
SOURCE 6 TISSUE: BLOOD;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 ORGAN: BLOOD;
SOURCE 12 TISSUE: BLOOD;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 15 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 16 ORGANISM_TAXID: 6421
KEYWDS BLOOD COAGULATION, PLASMA, CALCIUM-BINDING, GLYCOPROTEIN,
KEYWDS 2 DUPLICATION, VITAMIN K, ZYMOGEN, GAMMA-CARBOXYGLUTAMIC ACID,
KEYWDS 3 ACUTE PHASE, LIVER, HYDROLASE, SERINE PROTEASE, KRINGLE,
KEYWDS 4 SIGNAL, DISEASE MUTATION, COMPLEX (SERINE
KEYWDS 5 PROTEASE/INHIBITOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.WEBER,S.L.LEE,F.A.LEWANDOWSKI,M.C.SCHADT,C.H.CHANG,
AUTHOR 2 C.A.KETTNER
REVDAT 2 24-FEB-09 1LHG 1 VERSN
REVDAT 1 08-NOV-96 1LHG 0
JRNL AUTH P.C.WEBER,S.L.LEE,F.A.LEWANDOWSKI,M.C.SCHADT,
JRNL AUTH 2 C.W.CHANG,C.A.KETTNER
JRNL TITL KINETIC AND CRYSTALLOGRAPHIC STUDIES OF THROMBIN
JRNL TITL 2 WITH AC-(D)PHE-PRO-BOROARG-OH AND ITS LYSINE,
JRNL TITL 3 AMIDINE, HOMOLYSINE, AND ORNITHINE ANALOGS.
JRNL REF BIOCHEMISTRY V. 34 3750 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7893672
JRNL DOI 10.1021/BI00011A033
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 11468
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 122
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.010 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.021 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.018 ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.173 ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LHG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 51.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 35.20000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.20000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.10000
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THROMBIN IS CLEAVED BETWEEN RESIDUES 15 AND 16. CHAIN
REMARK 400 IDENTIFIER *L* IS USED FOR RESIDUES 1H - 15 AND CHAIN
REMARK 400 IDENTIFIER *H* IS USED FOR RESIDUES 16 - 247. CHAIN
REMARK 400 IDENTIFIER *I* IS USED FOR THE 12-RESIDUE HIRUDIN PEPTIDE.
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 THR L -5
REMARK 465 PHE L -4
REMARK 465 GLY L -3
REMARK 465 SER L -2
REMARK 465 GLY L -1
REMARK 465 GLU L 0
REMARK 465 ILE L 15
REMARK 465 ASP L 16
REMARK 465 GLY L 17
REMARK 465 ARG L 18
REMARK 465 THR H 146A
REMARK 465 TRP H 146B
REMARK 465 THR H 146C
REMARK 465 ALA H 146D
REMARK 465 ASN H 146E
REMARK 465 VAL H 146F
REMARK 465 GLY H 146G
REMARK 465 LYS H 146H
REMARK 465 GLY H 246
REMARK 465 GLU H 247
REMARK 465 GLU I 61
REMARK 465 GLU I 62
REMARK 465 TYR I 63
REMARK 465 LEU I 64
REMARK 465 GLN I 65
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 NH1 ARG H 73 O HOH H 557 2.07
REMARK 500 O1 DI5 H 400 O HOH H 640 2.07
REMARK 500 O PHE H 114 O HOH H 604 2.11
REMARK 500 OE1 GLU H 97A NH1 ARG H 175 2.11
REMARK 500 NH2 ARG H 50 O LEU H 108 2.14
REMARK 500 NH2 ARG H 165 O THR H 177 2.17
REMARK 500 OE2 GLU L 8 NZ LYS H 202 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ARG H 35 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU H 46 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG H 75 CD - NE - CZ ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG H 75 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG H 93 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG H 93 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP H 116 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP H 116 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 CYS H 122 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG H 137 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG H 137 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG H 165 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG H 187 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG H 206 CD - NE - CZ ANGL. DEV. = 8.5 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 PHE L 7 -87.84 -123.04
REMARK 500 LYS H 36 -75.21 -53.90
REMARK 500 LEU H 41 -70.67 -78.93
REMARK 500 TYR H 60A 77.56 -160.09
REMARK 500 ASN H 60G 88.86 -162.92
REMARK 500 HIS H 71 -55.40 -130.38
REMARK 500 GLU H 77 83.22 -64.34
REMARK 500 ARG H 77A -66.65 -21.42
REMARK 500 ASN H 98 28.39 -142.41
REMARK 500 SER H 115 -160.17 -165.20
REMARK 500 ASP H 186A 43.84 -103.54
REMARK 500 ASP H 189 175.19 179.52
REMARK 500 ASP H 243 -72.68 -58.67
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 H 534 DISTANCE = 5.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DI5 H 400
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 CHYMOTRYPSIN NUMBERING (RATHER THAN SEQUENTIAL) SYSTEM IS
REMARK 999 USED, BASED ON THE TOPOLOGICAL ALIGNMENT WITH THE
REMARK 999 STRUCTURE OF CHYMOTRYPSIN (W.BODE ET AL., 1989, EMBO J. 8,
REMARK 999 3467-3475).
DBREF 1LHG L -5 18 UNP P00734 THRB_HUMAN 328 363
DBREF 1LHG H 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 1LHG I 54 65 PDB 1LHG 1LHG 54 65
SEQRES 1 L 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 2 L 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG
SEQRES 3 L 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG
SEQRES 1 H 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 H 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 H 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 H 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 H 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 H 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 H 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 H 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 H 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 H 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 H 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 H 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 H 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 H 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 H 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 H 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 H 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 H 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 H 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 H 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
SEQRES 1 I 12 GLY ASP PHE GLU GLU ILE PRO GLU GLU TYR LEU GLN
HET DI5 H 400 30
HETNAM DI5 AC-(D)PHE-PRO-BOROHOMOORNITHINE-OH
FORMUL 4 DI5 C20 H31 B N4 O5
FORMUL 5 HOH *122(H2 O)
HELIX 1 1 GLU L 8 LYS L 10 5 3
HELIX 2 2 GLU L 14C LEU L 14G 1 5
HELIX 3 3 ALA H 56 CYS H 58 5 3
HELIX 4 4 PRO H 60B TRP H 60D 5 3
HELIX 5 5 GLU H 61 ASP H 63 5 3
HELIX 6 6 ARG H 126 LEU H 129C 1 7
HELIX 7 7 ARG H 165 SER H 171 1 7
HELIX 8 8 LYS H 235 GLN H 244 1 10
SHEET 1 A 4 GLY H 43 SER H 45 0
SHEET 2 A 4 GLN H 30 ARG H 35 -1 N VAL H 31 O ALA H 44
SHEET 3 A 4 LEU H 64 ILE H 68 -1 N ARG H 67 O MET H 32
SHEET 4 A 4 LYS H 81 MET H 84 -1 N SER H 83 O VAL H 66
SHEET 1 B 3 TRP H 51 THR H 54 0
SHEET 2 B 3 ALA H 104 LEU H 108 -1 N MET H 106 O VAL H 52
SHEET 3 B 3 LEU H 85 ILE H 90 -1 N TYR H 89 O LEU H 105
SHEET 1 C 2 LYS H 135 GLY H 140 0
SHEET 2 C 2 GLN H 156 PRO H 161 -1 N LEU H 160 O GLY H 136
SHEET 1 D 4 MET H 180 ALA H 183 0
SHEET 2 D 4 GLY H 226 HIS H 230 -1 N TYR H 228 O PHE H 181
SHEET 3 D 4 TRP H 207 TRP H 215 -1 N TRP H 215 O PHE H 227
SHEET 4 D 4 PRO H 198 LYS H 202 -1 N MET H 201 O TYR H 208
SSBOND 1 CYS L 1 CYS H 122 1555 1555 2.04
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.10
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.01
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.04
LINK B1 DI5 H 400 OG SER H 195 1555 1555 1.57
CISPEP 1 SER H 36A PRO H 37 0 -0.27
SITE 1 AC1 17 HIS H 57 TRP H 60D GLU H 97A ILE H 174
SITE 2 AC1 17 ALA H 190 CYS H 191 GLU H 192 GLY H 193
SITE 3 AC1 17 ASP H 194 SER H 195 SER H 214 TRP H 215
SITE 4 AC1 17 GLY H 216 GLU H 217 GLY H 219 HOH H 508
SITE 5 AC1 17 HOH H 640
CRYST1 70.400 72.200 72.200 90.00 100.10 90.00 C 1 2 1 4
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 0.014205 0.000000 0.002530 0.00000
SCALE2 0.000000 0.013850 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014068 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
