HEADER TRANSPORT PROTEIN 20-JUN-13 4LB2
TITLE X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH IDARUBICIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERUM ALBUMIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 25-609
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PLASMA PROTEIN, CANCER, ONCOLOGY DRUG COMPLEX, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WANG,J.X.HO,J.RUBLE,J.P.ROSE,D.C.CARTER
REVDAT 3 19-FEB-14 4LB2 1 REMARK
REVDAT 2 23-OCT-13 4LB2 1 JRNL
REVDAT 1 24-JUL-13 4LB2 0
JRNL AUTH Z.M.WANG,J.X.HO,J.R.RUBLE,J.ROSE,F.RUKER,M.ELLENBURG,
JRNL AUTH 2 R.MURPHY,J.CLICK,E.SOISTMAN,L.WILKERSON,D.C.CARTER
JRNL TITL STRUCTURAL STUDIES OF SEVERAL CLINICALLY IMPORTANT ONCOLOGY
JRNL TITL 2 DRUGS IN COMPLEX WITH HUMAN SERUM ALBUMIN.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1830 5356 2013
JRNL REFN ISSN 0006-3002
JRNL PMID 23838380
JRNL DOI 10.1016/J.BBAGEN.2013.06.032
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.C.CARTER
REMARK 1 TITL CRYSTALLOGRAPHIC SURVEY OF ALBUMIN DRUG INTERACTION AND
REMARK 1 TITL 2 PRELIMINARY APPLICATIONS IN CANCER CHEMOTHERAPY
REMARK 1 REF BURGERS MEDICINAL CHEMISTRY 437 2010
REMARK 1 REF 2 DRUG DESIGN AND DEVELOPMENT,
REMARK 1 REF 3 7TH EDITION
REMARK 1 PUBL JOHN WILEY & SONS
REMARK 1 REFN
REMARK 1 DOI 10.1002/0471266949
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.C.CARTER,J.X.HO
REMARK 1 TITL STRUCTURE OF SERUM ALBUMIN
REMARK 1 REF ADV.PROTEIN CHEM. V. 45 153 1994
REMARK 1 REFN ISSN 0065-3233
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.C.CARTER,B.CHANG,J.X.HO,K.KEELING,Z.KRISHNASAMI
REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF FOUR CRYSTAL FORMS
REMARK 1 TITL 2 OF SERUM ALBUMIN.
REMARK 1 REF EUR.J.BIOCHEM. V. 226 1049 1994
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 7813459
REMARK 1 REFERENCE 4
REMARK 1 AUTH X.M.HO,D.C.CARTER
REMARK 1 TITL ERRATUM. ATOMIC STRUCTURE AND CHEMISTRY OF HUMAN SERUM
REMARK 1 TITL 2 ALBUMIN
REMARK 1 REF NATURE V. 364 362 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 5
REMARK 1 AUTH X.M.HE,D.C.CARTER
REMARK 1 TITL ATOMIC STRUCTURE AND CHEMISTRY OF HUMAN SERUM ALBUMIN.
REMARK 1 REF NATURE V. 358 209 1992
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 1630489
REMARK 1 DOI 10.1038/358209A0
REMARK 1 REFERENCE 6
REMARK 1 AUTH D.C.CARTER,X.M.HO
REMARK 1 TITL STRUCTURE OF HUMAN SERUM ALBUMIN
REMARK 1 REF SCIENCE V. 249 302 1990
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 7
REMARK 1 AUTH D.C.CARTER,X.M.HE,S.H.MUNSON,P.D.TWIGG,K.M.GERNERT,
REMARK 1 AUTH 2 M.B.BROOM,T.Y.MILLER
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF HUMAN SERUM ALBUMIN.
REMARK 1 REF SCIENCE V. 244 1195 1989
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 2727704
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 27905
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1399
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 28.1642 - 6.0148 0.96 2661 138 0.1768 0.2085
REMARK 3 2 6.0148 - 4.7817 0.98 2684 141 0.2041 0.2170
REMARK 3 3 4.7817 - 4.1795 0.97 2676 136 0.1670 0.2365
REMARK 3 4 4.1795 - 3.7984 0.97 2663 148 0.1732 0.2054
REMARK 3 5 3.7984 - 3.5267 0.97 2685 140 0.1907 0.2322
REMARK 3 6 3.5267 - 3.3191 0.96 2650 140 0.2140 0.2835
REMARK 3 7 3.3191 - 3.1531 0.96 2620 142 0.2409 0.2885
REMARK 3 8 3.1531 - 3.0160 0.96 2631 139 0.2396 0.2825
REMARK 3 9 3.0160 - 2.9000 0.96 2634 132 0.2580 0.3215
REMARK 3 10 2.9000 - 2.8000 0.94 2602 143 0.2679 0.3144
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.11
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 : 0.003 9570
REMARK 3 ANGLE : 1.207 12900
REMARK 3 CHIRALITY : 0.121 1430
REMARK 3 PLANARITY : 0.004 1656
REMARK 3 DIHEDRAL : 14.346 3566
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4LB2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-13.
REMARK 100 THE RCSB ID CODE IS RCSB080406.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CONFOCAL OPTICS
REMARK 200 OPTICS : CONFOCAL OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31105
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.42800
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: MERLOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, POTASSIUM PHOSPHATE,
REMARK 280 CRYSTALS OF THE COMPLEXES WERE OBTAINED BY STANDARD VAPOR
REMARK 280 EQUILIBRATION METHODS WITH CONDITIONS OPTIMIZED BY SCREENS
REMARK 280 VARYING PROTEIN CONCENTRATION, PH, DRUG MOLAR RATIOS, CENTERED ON
REMARK 280 THE ORIGINAL CRYSTALLIZATION HIT USING PROTOCOLS DESCRIBED
REMARK 280 PREVIOUSLY FOR THE MONOCLINIC [CARTER, ET AL., EUR. J.
REMARK 280 BIOCHEMISTRY (1994) 226: 1049-1052] AND TRICLINIC [SUGO, ET AL.,
REMARK 280 PROTEIN ENG (1999) 12: 439-446] CRYSTAL FORMS., PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 ASP A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 LYS A 4
REMARK 465 LEU A 583
REMARK 465 GLY A 584
REMARK 465 LEU A 585
REMARK 465 ASP B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 LYS B 4
REMARK 465 LEU B 583
REMARK 465 GLY B 584
REMARK 465 LEU B 585
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 718 O HOH A 719 1.86
REMARK 500 OE1 GLU A 37 O HOH A 714 1.87
REMARK 500 O ALA A 229 O HOH A 710 1.93
REMARK 500 OE1 GLN B 29 O HOH B 730 1.95
REMARK 500 O HOH B 705 O HOH B 724 2.02
REMARK 500 NE2 GLN A 204 O HOH A 732 2.04
REMARK 500 O THR A 467 O HOH A 706 2.11
REMARK 500 O HOH B 728 O HOH B 736 2.15
REMARK 500 O GLU B 17 O HOH B 734 2.18
REMARK 500 O LYS B 500 O HOH B 718 2.18
REMARK 500 OH TYR B 319 OE2 GLU B 358 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 PRO B 499 C - N - CA ANGL. DEV. = 9.8 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 ALA A 59 -150.34 -66.88
REMARK 500 GLU A 60 -87.17 -56.53
REMARK 500 GLU A 86 40.01 -84.10
REMARK 500 ASN A 109 77.05 -151.02
REMARK 500 PRO A 118 -168.50 -78.74
REMARK 500 ASP A 129 -70.44 -60.28
REMARK 500 TYR A 150 104.60 -59.55
REMARK 500 ILE A 271 -60.73 -130.25
REMARK 500 GLU A 277 -31.03 77.23
REMARK 500 LEU A 283 -70.95 -35.81
REMARK 500 PRO A 303 -155.21 -74.16
REMARK 500 VAL A 469 -20.20 -144.34
REMARK 500 PHE A 507 -27.23 -144.22
REMARK 500 PRO A 537 -92.91 -74.99
REMARK 500 LYS A 538 -113.57 37.93
REMARK 500 LYS A 541 -86.27 -148.93
REMARK 500 LYS A 560 40.09 -108.87
REMARK 500 LYS A 564 68.45 -100.53
REMARK 500 GLU A 565 0.53 54.15
REMARK 500 ALA A 581 91.30 -66.15
REMARK 500 GLU B 60 -86.19 -20.79
REMARK 500 THR B 79 -9.13 -56.48
REMARK 500 LEU B 80 93.57 -67.92
REMARK 500 GLU B 86 41.66 -81.09
REMARK 500 PRO B 118 -166.56 -78.27
REMARK 500 TYR B 150 104.42 -58.87
REMARK 500 ILE B 271 -60.59 -130.85
REMARK 500 PRO B 303 -154.31 -69.68
REMARK 500 VAL B 469 -19.84 -145.49
REMARK 500 PRO B 499 175.22 -41.72
REMARK 500 GLU B 501 -27.24 23.95
REMARK 500 PHE B 502 165.13 170.96
REMARK 500 ASN B 503 -24.07 -147.64
REMARK 500 ALA B 504 -30.58 67.92
REMARK 500 LYS B 538 -72.17 -45.75
REMARK 500 ALA B 539 -125.22 -92.98
REMARK 500 THR B 540 127.27 60.82
REMARK 500 LYS B 541 -87.71 -155.61
REMARK 500 ASP B 562 38.72 39.31
REMARK 500 GLU B 565 4.97 49.39
REMARK 500 ALA B 581 -174.25 -66.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU B 501 22.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DM5 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DM5 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DM5 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DM5 B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L8U RELATED DB: PDB
REMARK 900 RELATED ID: 4L9K RELATED DB: PDB
REMARK 900 RELATED ID: 4L9Q RELATED DB: PDB
REMARK 900 RELATED ID: 4LA0 RELATED DB: PDB
REMARK 900 RELATED ID: 4LB9 RELATED DB: PDB
DBREF 4LB2 A 1 585 UNP P02768 ALBU_HUMAN 25 609
DBREF 4LB2 B 1 585 UNP P02768 ALBU_HUMAN 25 609
SEQRES 1 A 585 ASP ALA HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP
SEQRES 2 A 585 LEU GLY GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA
SEQRES 3 A 585 PHE ALA GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS
SEQRES 4 A 585 VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR
SEQRES 5 A 585 CYS VAL ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER
SEQRES 6 A 585 LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA
SEQRES 7 A 585 THR LEU ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS
SEQRES 8 A 585 ALA LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN
SEQRES 9 A 585 HIS LYS ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG
SEQRES 10 A 585 PRO GLU VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN
SEQRES 11 A 585 GLU GLU THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA
SEQRES 12 A 585 ARG ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE
SEQRES 13 A 585 PHE ALA LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS
SEQRES 14 A 585 GLN ALA ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU
SEQRES 15 A 585 ASP GLU LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS
SEQRES 16 A 585 GLN ARG LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU
SEQRES 17 A 585 ARG ALA PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN
SEQRES 18 A 585 ARG PHE PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU
SEQRES 19 A 585 VAL THR ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS
SEQRES 20 A 585 GLY ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU
SEQRES 21 A 585 ALA LYS TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER
SEQRES 22 A 585 LYS LEU LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS
SEQRES 23 A 585 SER HIS CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO
SEQRES 24 A 585 ALA ASP LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER
SEQRES 25 A 585 LYS ASP VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL
SEQRES 26 A 585 PHE LEU GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS
SEQRES 27 A 585 PRO ASP TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS
SEQRES 28 A 585 THR TYR GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA
SEQRES 29 A 585 ASP PRO HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE
SEQRES 30 A 585 LYS PRO LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN
SEQRES 31 A 585 ASN CYS GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE
SEQRES 32 A 585 GLN ASN ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO
SEQRES 33 A 585 GLN VAL SER THR PRO THR LEU VAL GLU VAL SER ARG ASN
SEQRES 34 A 585 LEU GLY LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU
SEQRES 35 A 585 ALA LYS ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL
SEQRES 36 A 585 VAL LEU ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO
SEQRES 37 A 585 VAL SER ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU
SEQRES 38 A 585 VAL ASN ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP
SEQRES 39 A 585 GLU THR TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE
SEQRES 40 A 585 THR PHE HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU
SEQRES 41 A 585 ARG GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL
SEQRES 42 A 585 LYS HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA
SEQRES 43 A 585 VAL MET ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS
SEQRES 44 A 585 LYS ALA ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY
SEQRES 45 A 585 LYS LYS LEU VAL ALA ALA SER GLN ALA ALA LEU GLY LEU
SEQRES 1 B 585 ASP ALA HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP
SEQRES 2 B 585 LEU GLY GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA
SEQRES 3 B 585 PHE ALA GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS
SEQRES 4 B 585 VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR
SEQRES 5 B 585 CYS VAL ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER
SEQRES 6 B 585 LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA
SEQRES 7 B 585 THR LEU ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS
SEQRES 8 B 585 ALA LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN
SEQRES 9 B 585 HIS LYS ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG
SEQRES 10 B 585 PRO GLU VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN
SEQRES 11 B 585 GLU GLU THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA
SEQRES 12 B 585 ARG ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE
SEQRES 13 B 585 PHE ALA LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS
SEQRES 14 B 585 GLN ALA ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU
SEQRES 15 B 585 ASP GLU LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS
SEQRES 16 B 585 GLN ARG LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU
SEQRES 17 B 585 ARG ALA PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN
SEQRES 18 B 585 ARG PHE PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU
SEQRES 19 B 585 VAL THR ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS
SEQRES 20 B 585 GLY ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU
SEQRES 21 B 585 ALA LYS TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER
SEQRES 22 B 585 LYS LEU LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS
SEQRES 23 B 585 SER HIS CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO
SEQRES 24 B 585 ALA ASP LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER
SEQRES 25 B 585 LYS ASP VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL
SEQRES 26 B 585 PHE LEU GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS
SEQRES 27 B 585 PRO ASP TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS
SEQRES 28 B 585 THR TYR GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA
SEQRES 29 B 585 ASP PRO HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE
SEQRES 30 B 585 LYS PRO LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN
SEQRES 31 B 585 ASN CYS GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE
SEQRES 32 B 585 GLN ASN ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO
SEQRES 33 B 585 GLN VAL SER THR PRO THR LEU VAL GLU VAL SER ARG ASN
SEQRES 34 B 585 LEU GLY LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU
SEQRES 35 B 585 ALA LYS ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL
SEQRES 36 B 585 VAL LEU ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO
SEQRES 37 B 585 VAL SER ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU
SEQRES 38 B 585 VAL ASN ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP
SEQRES 39 B 585 GLU THR TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE
SEQRES 40 B 585 THR PHE HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU
SEQRES 41 B 585 ARG GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL
SEQRES 42 B 585 LYS HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA
SEQRES 43 B 585 VAL MET ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS
SEQRES 44 B 585 LYS ALA ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY
SEQRES 45 B 585 LYS LYS LEU VAL ALA ALA SER GLN ALA ALA LEU GLY LEU
HET DM5 A 601 36
HET DM5 A 602 36
HET DM5 B 601 36
HET DM5 B 602 36
HETNAM DM5 IDARUBICIN
HETSYN DM5 4-DEMETHOXY-DAUNORUBICIN
FORMUL 3 DM5 4(C26 H27 N O9)
FORMUL 7 HOH *75(H2 O)
HELIX 1 1 SER A 5 GLY A 15 1 11
HELIX 2 2 GLY A 15 LEU A 31 1 17
HELIX 3 3 PRO A 35 ASP A 56 1 22
HELIX 4 4 SER A 65 THR A 79 1 15
HELIX 5 5 LEU A 80 GLY A 85 1 6
HELIX 6 6 PRO A 96 HIS A 105 1 10
HELIX 7 7 GLU A 119 ASN A 130 1 12
HELIX 8 8 ASN A 130 HIS A 146 1 17
HELIX 9 9 TYR A 150 CYS A 169 1 20
HELIX 10 10 ASP A 173 PHE A 206 1 34
HELIX 11 11 GLY A 207 PHE A 223 1 17
HELIX 12 12 GLU A 227 HIS A 247 1 21
HELIX 13 13 ASP A 249 ASN A 267 1 19
HELIX 14 14 GLN A 268 ILE A 271 5 4
HELIX 15 15 SER A 272 LYS A 276 5 5
HELIX 16 16 PRO A 282 GLU A 292 1 11
HELIX 17 17 SER A 304 GLU A 311 1 8
HELIX 18 18 ASP A 314 ALA A 322 1 9
HELIX 19 19 ALA A 322 ARG A 337 1 16
HELIX 20 20 SER A 342 CYS A 361 1 20
HELIX 21 21 ASP A 365 TYR A 370 1 6
HELIX 22 22 LYS A 372 VAL A 415 1 44
HELIX 23 23 SER A 419 LYS A 432 1 14
HELIX 24 24 LYS A 432 CYS A 438 1 7
HELIX 25 25 PRO A 441 LYS A 466 1 26
HELIX 26 26 SER A 470 SER A 480 1 11
HELIX 27 27 ASN A 483 LEU A 491 1 9
HELIX 28 28 HIS A 510 LEU A 516 5 7
HELIX 29 29 SER A 517 LYS A 536 1 20
HELIX 30 30 LYS A 541 LYS A 560 1 20
HELIX 31 31 THR A 566 ALA A 581 1 16
HELIX 32 32 GLU B 6 LEU B 31 1 26
HELIX 33 33 PRO B 35 ASP B 56 1 22
HELIX 34 34 SER B 65 THR B 79 1 15
HELIX 35 35 LEU B 80 GLY B 85 1 6
HELIX 36 36 ALA B 88 LYS B 93 1 6
HELIX 37 37 PRO B 96 GLN B 104 1 9
HELIX 38 38 GLU B 119 ASN B 130 1 12
HELIX 39 39 ASN B 130 HIS B 146 1 17
HELIX 40 40 TYR B 150 CYS B 169 1 20
HELIX 41 41 ASP B 173 GLY B 207 1 35
HELIX 42 42 GLY B 207 PHE B 223 1 17
HELIX 43 43 GLU B 227 HIS B 247 1 21
HELIX 44 44 ASP B 249 ASN B 267 1 19
HELIX 45 45 GLN B 268 ILE B 271 5 4
HELIX 46 46 PRO B 282 GLU B 292 1 11
HELIX 47 47 SER B 304 VAL B 310 1 7
HELIX 48 48 ASP B 314 ALA B 322 1 9
HELIX 49 49 ALA B 322 ARG B 337 1 16
HELIX 50 50 SER B 342 CYS B 361 1 20
HELIX 51 51 ASP B 365 ALA B 371 1 7
HELIX 52 52 LYS B 372 GLY B 399 1 28
HELIX 53 53 GLY B 399 VAL B 415 1 17
HELIX 54 54 SER B 419 LYS B 432 1 14
HELIX 55 55 LYS B 432 CYS B 438 1 7
HELIX 56 56 PRO B 441 LYS B 466 1 26
HELIX 57 57 SER B 470 SER B 480 1 11
HELIX 58 58 ASN B 483 LEU B 491 1 9
HELIX 59 59 HIS B 510 THR B 515 5 6
HELIX 60 60 SER B 517 LYS B 536 1 20
HELIX 61 61 LYS B 541 LYS B 560 1 20
HELIX 62 62 THR B 566 ALA B 581 1 16
SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.03
SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.03
SSBOND 3 CYS A 90 CYS A 101 1555 1555 2.01
SSBOND 4 CYS A 124 CYS A 169 1555 1555 2.03
SSBOND 5 CYS A 168 CYS A 177 1555 1555 2.03
SSBOND 6 CYS A 200 CYS A 246 1555 1555 2.03
SSBOND 7 CYS A 245 CYS A 253 1555 1555 2.03
SSBOND 8 CYS A 265 CYS A 279 1555 1555 2.03
SSBOND 9 CYS A 278 CYS A 289 1555 1555 2.03
SSBOND 10 CYS A 316 CYS A 361 1555 1555 2.03
SSBOND 11 CYS A 360 CYS A 369 1555 1555 2.03
SSBOND 12 CYS A 392 CYS A 438 1555 1555 2.03
SSBOND 13 CYS A 437 CYS A 448 1555 1555 2.03
SSBOND 14 CYS A 461 CYS A 477 1555 1555 2.03
SSBOND 15 CYS A 476 CYS A 487 1555 1555 2.03
SSBOND 16 CYS A 514 CYS A 559 1555 1555 2.03
SSBOND 17 CYS A 558 CYS A 567 1555 1555 2.03
SSBOND 18 CYS B 53 CYS B 62 1555 1555 2.03
SSBOND 19 CYS B 75 CYS B 91 1555 1555 2.03
SSBOND 20 CYS B 90 CYS B 101 1555 1555 2.03
SSBOND 21 CYS B 124 CYS B 169 1555 1555 2.03
SSBOND 22 CYS B 168 CYS B 177 1555 1555 2.03
SSBOND 23 CYS B 200 CYS B 246 1555 1555 2.03
SSBOND 24 CYS B 245 CYS B 253 1555 1555 2.03
SSBOND 25 CYS B 265 CYS B 279 1555 1555 2.03
SSBOND 26 CYS B 278 CYS B 289 1555 1555 2.02
SSBOND 27 CYS B 316 CYS B 361 1555 1555 2.03
SSBOND 28 CYS B 360 CYS B 369 1555 1555 2.03
SSBOND 29 CYS B 392 CYS B 438 1555 1555 2.03
SSBOND 30 CYS B 437 CYS B 448 1555 1555 2.04
SSBOND 31 CYS B 461 CYS B 477 1555 1555 2.03
SSBOND 32 CYS B 476 CYS B 487 1555 1555 2.03
SSBOND 33 CYS B 514 CYS B 559 1555 1555 2.03
SSBOND 34 CYS B 558 CYS B 567 1555 1555 2.03
CISPEP 1 GLU A 95 PRO A 96 0 3.58
CISPEP 2 GLU B 95 PRO B 96 0 3.89
SITE 1 AC1 8 LEU A 115 VAL A 116 ARG A 117 LYS A 137
SITE 2 AC1 8 TYR A 138 GLU A 141 TYR A 161 DM5 A 602
SITE 1 AC2 7 PRO A 118 VAL A 122 MET A 123 PHE A 134
SITE 2 AC2 7 LYS A 137 TYR A 161 DM5 A 601
SITE 1 AC3 8 LEU B 115 VAL B 116 ARG B 117 PRO B 118
SITE 2 AC3 8 LYS B 137 TYR B 138 GLU B 141 DM5 B 602
SITE 1 AC4 8 PRO B 118 VAL B 122 MET B 123 ALA B 126
SITE 2 AC4 8 PHE B 134 LYS B 137 TYR B 161 DM5 B 601
CRYST1 57.952 58.199 96.085 74.74 88.63 76.58 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 0.017256 -0.004117 0.000704 0.00000
SCALE2 0.000000 0.017665 -0.004853 0.00000
SCALE3 0.000000 0.000000 0.010796 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
