HEADER HYDROLASE/HYDROLASE INHIBITOR 17-OCT-11 3U8R
TITLE HUMAN THROMBIN COMPLEXED WITH D-PHE-PRO-D-ARG-ILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN LIGHT CHAIN;
COMPND 3 CHAIN: L;
COMPND 4 SYNONYM: ALPHA-THROMBIN, PROTHROMBIN;
COMPND 5 EC: 3.4.21.5;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: THROMBIN HEAVY CHAIN;
COMPND 8 CHAIN: H;
COMPND 9 SYNONYM: ALPHA-THROMBIN, PROTHROMBIN;
COMPND 10 EC: 3.4.21.5;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: D-PHE-PRO-D-ARG-ILE DERIVED DIRECT THROMBIN INHIBITOR;
COMPND 13 CHAIN: I;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 MOL_ID: 3;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.FIGUEIREDO,C.C.CLEMENT,M.PHILIPP,P.J.B.PEREIRA
REVDAT 3 29-JUL-20 3U8R 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 05-JUN-13 3U8R 1 REMARK
REVDAT 1 23-MAY-12 3U8R 0
JRNL AUTH A.C.FIGUEIREDO,C.C.CLEMENT,S.ZAKIA,J.GINGOLD,M.PHILIPP,
JRNL AUTH 2 P.J.PEREIRA
JRNL TITL RATIONAL DESIGN AND CHARACTERIZATION OF
JRNL TITL 2 D-PHE-PRO-D-ARG-DERIVED DIRECT THROMBIN INHIBITORS.
JRNL REF PLOS ONE V. 7 34354 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22457833
JRNL DOI 10.1371/JOURNAL.PONE.0034354
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.2_869
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) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 56347
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.131
REMARK 3 R VALUE (WORKING SET) : 0.129
REMARK 3 FREE R VALUE : 0.161
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2860
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 43.8568 - 3.9982 1.00 2855 167 0.1688 0.1544
REMARK 3 2 3.9982 - 3.1738 1.00 2768 133 0.1342 0.1636
REMARK 3 3 3.1738 - 2.7727 1.00 2732 132 0.1414 0.1663
REMARK 3 4 2.7727 - 2.5192 1.00 2718 128 0.1298 0.1828
REMARK 3 5 2.5192 - 2.3387 1.00 2691 138 0.1203 0.1524
REMARK 3 6 2.3387 - 2.2008 1.00 2692 140 0.1170 0.1396
REMARK 3 7 2.2008 - 2.0906 1.00 2701 119 0.1161 0.1387
REMARK 3 8 2.0906 - 1.9996 1.00 2648 153 0.1129 0.1589
REMARK 3 9 1.9996 - 1.9226 1.00 2645 156 0.1107 0.1547
REMARK 3 10 1.9226 - 1.8562 1.00 2658 149 0.1102 0.1370
REMARK 3 11 1.8562 - 1.7982 1.00 2648 137 0.1105 0.1684
REMARK 3 12 1.7982 - 1.7468 1.00 2672 130 0.1064 0.1541
REMARK 3 13 1.7468 - 1.7008 1.00 2638 149 0.1043 0.1585
REMARK 3 14 1.7008 - 1.6593 1.00 2626 145 0.1081 0.1458
REMARK 3 15 1.6593 - 1.6216 1.00 2667 147 0.1117 0.1652
REMARK 3 16 1.6216 - 1.5871 1.00 2630 169 0.1148 0.1890
REMARK 3 17 1.5871 - 1.5553 1.00 2610 142 0.1166 0.1805
REMARK 3 18 1.5553 - 1.5260 1.00 2633 160 0.1272 0.1852
REMARK 3 19 1.5260 - 1.4987 1.00 2645 134 0.1380 0.2282
REMARK 3 20 1.4987 - 1.4733 0.99 2610 132 0.1454 0.2251
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 40.94
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.80290
REMARK 3 B22 (A**2) : -0.40240
REMARK 3 B33 (A**2) : -1.40040
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.010 2471
REMARK 3 ANGLE : 1.313 3347
REMARK 3 CHIRALITY : 0.085 351
REMARK 3 PLANARITY : 0.007 427
REMARK 3 DIHEDRAL : 14.322 953
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 3U8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068448.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56417
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 51.563
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.28600
REMARK 200 R SYM FOR SHELL (I) : 0.28600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS, 50MM BICINE, 30MM NAF, 30MM
REMARK 280 NABR, 30MM NAI, 11.5% MPD, 11.5% PEG-1000, 11.5% PEG-3350, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING 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 25.78150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.63000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.26350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.63000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.78150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.26350
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
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 THE D-PHENYLALANYL-L-PROLYL-N~5~-[AMINO(IMINIO)METHYL]-D-ORNITHYL-L-
REMARK 400 ISOLEUCINAMIDE IS PEPTIDE-LIKE, A MEMBER OF THROMBIN INHIBITOR
REMARK 400 CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: D-PHENYLALANYL-L-PROLYL-N~5~-[AMINO(IMINIO)METHYL]-D-
REMARK 400 ORNITHYL-L-ISOLEUCINAMIDE
REMARK 400 CHAIN: I
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 ASP L 318
REMARK 465 GLY L 319
REMARK 465 ARG L 320
REMARK 465 THR H 467
REMARK 465 TRP H 468
REMARK 465 THR H 469
REMARK 465 ALA H 470
REMARK 465 ASN H 471
REMARK 465 VAL H 472
REMARK 465 GLY H 473
REMARK 465 LYS H 474
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 H 908 O HOH H 928 1.80
REMARK 500 O HOH H 938 O HOH H 977 1.86
REMARK 500 N ALA L 291 O HOH L 435 1.92
REMARK 500 O HOH H 965 O HOH H 968 2.07
REMARK 500 O HOH H 902 O HOH H 937 2.13
REMARK 500 O HOH L 443 O HOH L 444 2.15
REMARK 500 O HOH H 960 O HOH H 986 2.15
REMARK 500 O HOH H 811 O HOH H 947 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH L 444 O HOH H 983 2555 1.66
REMARK 500 O HOH L 442 O HOH H 988 2555 1.87
REMARK 500 O HOH L 436 O HOH H 936 4445 1.94
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 DAR I 3 NE - CZ - NH2 ANGL. DEV. = -4.1 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 299 -87.36 -128.54
REMARK 500 TYR H 367 81.02 -150.41
REMARK 500 ASN H 373 83.72 -159.74
REMARK 500 HIS H 386 -59.97 -125.77
REMARK 500 ILE H 395 -58.48 -120.41
REMARK 500 GLU H 414 -74.49 -110.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA H 602 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG H 553 O
REMARK 620 2 LYS H 556 O 95.6
REMARK 620 3 HOH H 721 O 162.5 70.3
REMARK 620 4 HOH H 726 O 106.2 158.1 87.9
REMARK 620 5 HOH H 741 O 89.1 94.9 82.1 83.6
REMARK 620 6 HOH H 750 O 100.6 82.3 88.0 95.5 170.1
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U69 RELATED DB: PDB
REMARK 900 RELATED ID: 3U8O RELATED DB: PDB
REMARK 900 RELATED ID: 3U8T RELATED DB: PDB
DBREF 3U8R L 291 320 UNP P00734 THRB_HUMAN 334 363
DBREF 3U8R H 321 579 UNP P00734 THRB_HUMAN 364 622
DBREF 3U8R I 1 5 PDB 3U8R 3U8R 1 5
SEQRES 1 L 30 ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SER
SEQRES 2 L 30 LEU GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER TYR
SEQRES 3 L 30 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 5 DPN PRO DAR ILE NH2
MODRES 3U8R ASN H 373 ASN GLYCOSYLATION SITE
HET DPN I 1 21
HET DAR I 3 14
HET NH2 I 5 3
HET NAG H 601 14
HET NA H 602 1
HET IOD H 603 1
HET CL H 604 1
HET MPD H 605 22
HET MRD H 606 22
HETNAM DPN D-PHENYLALANINE
HETNAM DAR D-ARGININE
HETNAM NH2 AMINO GROUP
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM NA SODIUM ION
HETNAM IOD IODIDE ION
HETNAM CL CHLORIDE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 3 DPN C9 H11 N O2
FORMUL 3 DAR C6 H15 N4 O2 1+
FORMUL 3 NH2 H2 N
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 NA NA 1+
FORMUL 6 IOD I 1-
FORMUL 7 CL CL 1-
FORMUL 8 MPD C6 H14 O2
FORMUL 9 MRD C6 H14 O2
FORMUL 10 HOH *350(H2 O)
HELIX 1 1 PHE L 299 SER L 303 5 5
HELIX 2 2 THR L 308 TYR L 316 1 9
HELIX 3 3 ALA H 361 CYS H 364 5 4
HELIX 4 4 PRO H 368 ASP H 371 5 4
HELIX 5 5 THR H 375 ASN H 377 5 3
HELIX 6 6 ASP H 442 LEU H 450 1 9
HELIX 7 7 GLU H 489 SER H 496 1 8
HELIX 8 8 LYS H 511 GLY H 515 5 5
HELIX 9 9 LEU H 566 PHE H 577 1 12
SHEET 1 A 8 SER H 325 ASP H 326 0
SHEET 2 A 8 GLN H 481 VAL H 488 -1 O VAL H 482 N SER H 325
SHEET 3 A 8 MET H 505 ALA H 508 -1 O CYS H 507 N VAL H 488
SHEET 4 A 8 GLY H 558 HIS H 562 -1 O TYR H 560 N PHE H 506
SHEET 5 A 8 TRP H 539 TRP H 547 -1 N TRP H 547 O PHE H 559
SHEET 6 A 8 PRO H 528 LYS H 532 -1 N MET H 531 O TYR H 540
SHEET 7 A 8 LYS H 455 GLY H 460 -1 N ARG H 457 O VAL H 530
SHEET 8 A 8 GLN H 481 VAL H 488 -1 O VAL H 483 N VAL H 458
SHEET 1 B 7 LYS H 397 SER H 399 0
SHEET 2 B 7 LEU H 379 ILE H 383 -1 N ILE H 383 O LYS H 397
SHEET 3 B 7 GLN H 335 ARG H 340 -1 N PHE H 339 O LEU H 380
SHEET 4 B 7 GLU H 345 LEU H 352 -1 O GLU H 345 N ARG H 340
SHEET 5 B 7 TRP H 357 THR H 360 -1 O LEU H 359 N SER H 351
SHEET 6 B 7 ALA H 421 LEU H 425 -1 O MET H 423 N VAL H 358
SHEET 7 B 7 LEU H 401 ILE H 406 -1 N GLU H 402 O LYS H 424
SHEET 1 C 2 LEU H 366 TYR H 367 0
SHEET 2 C 2 LYS H 372 ASN H 373 -1 O LYS H 372 N TYR H 367
SSBOND 1 CYS L 293 CYS H 439 1555 1555 2.09
SSBOND 2 CYS H 348 CYS H 364 1555 1555 2.05
SSBOND 3 CYS H 493 CYS H 507 1555 1555 2.05
SSBOND 4 CYS H 521 CYS H 551 1555 1555 2.08
LINK ND2 ASN H 373 C1 NAG H 601 1555 1555 1.44
LINK C DPN I 1 N PRO I 2 1555 1555 1.34
LINK C PRO I 2 N DAR I 3 1555 1555 1.33
LINK C DAR I 3 N ILE I 4 1555 1555 1.34
LINK C ILE I 4 N NH2 I 5 1555 1555 1.44
LINK O ARG H 553 NA NA H 602 1555 1555 2.29
LINK O LYS H 556 NA NA H 602 1555 1555 2.36
LINK NA NA H 602 O HOH H 721 1555 1555 2.50
LINK NA NA H 602 O HOH H 726 1555 1555 2.51
LINK NA NA H 602 O HOH H 741 1555 1555 2.68
LINK NA NA H 602 O HOH H 750 1555 1555 2.41
CISPEP 1 SER H 342 PRO H 343 0 -4.03
CRYST1 51.563 76.527 83.260 90.00 90.00 90.00 P 21 21 21 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 0.019394 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012011 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
