HEADER INSULIN 08-MAR-04 1UZ9
TITLE CRYSTALLOGRAPHIC AND SOLUTION STUDIES OF N-LITHOCHOLYL INSULIN: A NEW
TITLE 2 GENERATION OF PROLONGED-ACTING INSULINS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: INSULIN A CHAIN, RESIDUES 90-110;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INSULIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: INSULIN B CHAIN, RESIDUES 25-53;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: PEPTIDE LINK BETWEEN B 29 SIDE CHAIN AND LITHOCHOLYL
COMPND 12 GROUP
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606
KEYWDS INSULIN, DIABETES MELLITUS, INSULIN FAMILY, HORMONE DISEASE MUTATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.WHITTINGHAM,I.JONASSEN,S.HAVELUND,S.M.ROBERTS,E.J.DODSON,
AUTHOR 2 C.S.VERMA,A.J.WILKINSON,G.G.DODSON
REVDAT 3 13-DEC-23 1UZ9 1 LINK
REVDAT 2 24-FEB-09 1UZ9 1 VERSN
REVDAT 1 03-MAR-05 1UZ9 0
JRNL AUTH J.L.WHITTINGHAM,I.JONASSEN,S.HAVELUND,S.M.ROBERTS,
JRNL AUTH 2 E.J.DODSON,C.S.VERMA,A.J.WILKINSON,G.G.DODSON
JRNL TITL CRYSTALLOGRAPHIC AND SOLUTION STUDIES OF N-LITHOCHOLYL
JRNL TITL 2 INSULIN: A NEW GENERATION OF PROLONGED-ACTING HUMAN INSULINS
JRNL REF BIOCHEMISTRY V. 43 5987 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15147182
JRNL DOI 10.1021/BI036163S
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 7336
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 353
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 530
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1480
REMARK 3 BIN FREE R VALUE SET COUNT : 21
REMARK 3 BIN FREE R VALUE : 0.2270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 388
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.52000
REMARK 3 B22 (A**2) : 0.52000
REMARK 3 B33 (A**2) : -0.78000
REMARK 3 B12 (A**2) : 0.26000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.480
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 456 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 403 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 626 ; 1.821 ; 2.073
REMARK 3 BOND ANGLES OTHERS (DEGREES): 946 ; 2.656 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 50 ; 5.716 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 72 ; 0.107 ; 0.200
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 484 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 93 ; 0.015 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 105 ; 0.250 ; 0.200
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 462 ; 0.243 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 258 ; 0.111 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 30 ; 0.460 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1 ; 0.007 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 18 ; 0.279 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 46 ; 0.225 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.463 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 252 ; 1.277 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 407 ; 2.231 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 204 ; 2.604 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 218 ; 3.872 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1290014744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8700
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7689
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 24.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.03400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.13900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1XDA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M TRIS-HCL PH 8.0 0.1M TRI-SODIUM
REMARK 280 CITRATE, 2MM ZINC ACETATE, 0.05% W/V M-CRESOL, PH 8.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.17000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 34.17000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 34.17000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 34.17000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 34.17000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 34.17000
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 300 REMARK: THE DODECAMER IS OF THE A-B HEXAMER TYPE
REMARK 300 WITH 6 A AND 6B CHAINS LINKED BY DISULFIDE
REMARK 300 BONDS THAT CAN BE GENERATEDBY APPLICATION OF
REMARK 300 SYMMETRY OPERATORS 2, 3, 10, 11 AND 12FROM
REMARK 300 REMARK 290 ABOVE.
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 51.79000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 25.89500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 44.85146
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 25.89500
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 44.85146
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 34.17000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 51.79000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 34.17000
REMARK 350 BIOMT1 6 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 34.17000
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 ZN ZN B1030 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL B1031 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2004 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2028 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 INSULIN DECREASES BLOOD GLUCOSE CONCENTRATION AND INCREASES
REMARK 400 CELL PERMEABILITY TO MONOSACCHARIDES, AMINO ACIDS AND
REMARK 400 FATTY ACIDS. IT ACCELERATES GLYCOLYSIS, THE PENTOSE PHOSPHATE
REMARK 400 CYCLE, AND GLYCOGEN SYNTHESIS IN LIVER.
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 LYS B 29
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 TYR A 14 CG CD1 CD2 CE1 CE2 CZ OH
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 OE2 GLU B 13 O HOH B 2014 1.20
REMARK 500 OE1 GLU B 21 O HOH B 2019 1.98
REMARK 500 OG SER A 9 O HOH A 2010 2.00
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 B 2008 O HOH B 2012 3665 1.66
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 ZN B1030 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 HIS B 10 NE2 106.9
REMARK 620 3 HIS B 10 NE2 106.7 107.3
REMARK 620 4 CL B1031 CL 111.7 112.0 111.9
REMARK 620 5 CL B1031 CL 111.4 112.3 111.8 0.4
REMARK 620 6 CL B1031 CL 111.4 112.0 112.2 0.4 0.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1030
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1031
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CRS A1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UZ9 B1029
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A7F RELATED DB: PDB
REMARK 900 INSULIN MUTANT B16 GLU, B24 GLY, DES-B30, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1AI0 RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (NON-SYMMETRIC), NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1B9E RELATED DB: PDB
REMARK 900 HUMAN INSULIN MUTANT SERB9GLU
REMARK 900 RELATED ID: 1BEN RELATED DB: PDB
REMARK 900 INSULIN COMPLEXED WITH 4-HYDROXYBENZAMIDE
REMARK 900 RELATED ID: 1EFE RELATED DB: PDB
REMARK 900 AN ACTIVE MINI-PROINSULIN, M2PI
REMARK 900 RELATED ID: 1EV3 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE RHOMBOHEDRAL FORM OF THE M-CRESOL/INSULIN R6
REMARK 900 HEXAMER
REMARK 900 RELATED ID: 1EV6 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MONOCLINIC FORM OF THE M -CRESOL/INSULIN R6 HEXAMER
REMARK 900 RELATED ID: 1EVR RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE RESORCINOL/INSULIN R6 HEXAMER
REMARK 900 RELATED ID: 1FU2 RELATED DB: PDB
REMARK 900 FIRST PROTEIN STRUCTURE DETERMINED FROM X- RAY POWDERDIFFRACTION
REMARK 900 DATA
REMARK 900 RELATED ID: 1FUB RELATED DB: PDB
REMARK 900 FIRST PROTEIN STRUCTURE DETERMINED FROM X- RAY POWDERDIFFRACTION
REMARK 900 DATA
REMARK 900 RELATED ID: 1G7A RELATED DB: PDB
REMARK 900 1.2 A STRUCTURE OF T3R3 HUMAN INSULIN AT 100 K
REMARK 900 RELATED ID: 1G7B RELATED DB: PDB
REMARK 900 1.3 A STRUCTURE OF T3R3 HUMAN INSULIN AT 100 K
REMARK 900 RELATED ID: 1GUJ RELATED DB: PDB
REMARK 900 INSULIN AT PH 2: STRUCTURAL ANALYSIS OF THE CONDITIONS PROMOTING
REMARK 900 INSULIN FIBRE FORMATION.
REMARK 900 RELATED ID: 1HIQ RELATED DB: PDB
REMARK 900 INSULIN (HUMAN) MUTANT WITH PHE B 24 REPLACED BY SER (F24S) (NMR,
REMARK 900 REPRESENTATIVE PLUS 9 STRUCTURES)
REMARK 900 RELATED ID: 1HIS RELATED DB: PDB
REMARK 900 INSULIN (HUMAN, DES-PENTAPEPTIDE (B 26 - B 30)) (NMR,
REMARK 900 REPRESENTATIVE PLUS 14 STRUCTURES)
REMARK 900 RELATED ID: 1HIT RELATED DB: PDB
REMARK 900 INSULIN (HUMAN) MUTANT WITH PHE B 24 REPLACED BY GLY (F24G) (NMR,
REMARK 900 REPRESENTATIVE PLUS 8 STRUCTURES)
REMARK 900 RELATED ID: 1HLS RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE HUMAN INSULIN-HIS(B16)
REMARK 900 RELATED ID: 1HTV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN
REMARK 900 RELATED ID: 1HUI RELATED DB: PDB
REMARK 900 INSULIN MUTANT (B1, B10, B16, B27)GLU, DES -B30, NMR, 25 STRUCTURES
REMARK 900 RELATED ID: 1IOG RELATED DB: PDB
REMARK 900 INSULIN MUTANT A3 GLY,(B1, B10, B16, B27) GLU, DES-B30, NMR, 19
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1IOH RELATED DB: PDB
REMARK 900 INSULIN MUTANT A8 HIS,(B1, B10, B16, B27) GLU, DES-B30, NMR, 26
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1J73 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN UNSTABLE INSULIN ANALOG WITH NATIVEACTIVITY.
REMARK 900 RELATED ID: 1JCA RELATED DB: PDB
REMARK 900 NON-STANDARD DESIGN OF UNSTABLE INSULIN ANALOGUES WITHENHANCED
REMARK 900 ACTIVITY
REMARK 900 RELATED ID: 1JCO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE MONOMERIC [THR(B27 )->PRO,PRO(B28)->THR]
REMARK 900 INSULIN MUTANT (PT INSULIN)
REMARK 900 RELATED ID: 1K3M RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE- A2-ALA, HIS-B10-ASP, PRO-
REMARK 900 B28-LYS, LYS- B29-PRO, 15 STRUCTURES
REMARK 900 RELATED ID: 1KMF RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE- A2-ALLO-ILE, HIS-B10-ASP,
REMARK 900 PRO-B28-LYS, LYS-B29-PRO, 15 STRUCTURES
REMARK 900 RELATED ID: 1LKQ RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE- A2-GLY, VAL-A3-GLY, HIS-
REMARK 900 B10-ASP, PRO- B28-LYS, LYS-B29-PRO, 20 STRUCTURES
REMARK 900 RELATED ID: 1LNP RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS- B10-ASP, PRO-B28-LYS,
REMARK 900 LYS-B29-PRO, 20 STRUCTURES
REMARK 900 RELATED ID: 1LPH RELATED DB: PDB
REMARK 900 LYS(B28)PRO(B29)-HUMAN INSULIN
REMARK 900 RELATED ID: 1MHI RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: INSULIN; CHAIN: A, B; ENGINEERED: YES MUTATION:
REMARK 900 S(B 9)D;
REMARK 900 RELATED ID: 1MHJ RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: INSULIN; CHAIN: A, B; ENGINEERED: YES MUTATION:
REMARK 900 DES-[PHE(B 25)];
REMARK 900 RELATED ID: 1MSO RELATED DB: PDB
REMARK 900 T6 HUMAN INSULIN AT 1.0 A RESOLUTION
REMARK 900 RELATED ID: 1OS3 RELATED DB: PDB
REMARK 900 DEHYDRATED T6 HUMAN INSULIN AT 100 K
REMARK 900 RELATED ID: 1OS4 RELATED DB: PDB
REMARK 900 DEHYDRATED T6 HUMAN INSULIN AT 295 K
REMARK 900 RELATED ID: 1Q4V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALLO-ILEA2-INSULIN, AN INACTIVE CHIRALANALOGUE:
REMARK 900 IMPLICATIONS FOR THE MECHANISM OF RECEPTOR
REMARK 900 RELATED ID: 1QIY RELATED DB: PDB
REMARK 900 HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR COMPLEXED
REMARK 900 WITH PHENOL
REMARK 900 RELATED ID: 1QIZ RELATED DB: PDB
REMARK 900 HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR COMPLEXED
REMARK 900 WITH RESORCINOL
REMARK 900 RELATED ID: 1QJ0 RELATED DB: PDB
REMARK 900 HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR
REMARK 900 RELATED ID: 1SJT RELATED DB: PDB
REMARK 900 MINI-PROINSULIN, TWO CHAIN INSULIN ANALOG MUTANT: DES B30, HIS(B 10)
REMARK 900 ASP, PRO(B 28)ASP, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1SJU RELATED DB: PDB
REMARK 900 MINI-PROINSULIN, SINGLE CHAIN INSULIN ANALOG MUTANT: DES B30, HIS(B
REMARK 900 10)ASP, PRO(B 28)ASP AND PEPTIDE BOND BETWEEN LYS B 29 AND GLY A 1,
REMARK 900 NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1TRZ RELATED DB: PDB
REMARK 900 INSULIN (T3R3) COMPLEX WITH TWO ZINC IONS
REMARK 900 RELATED ID: 1TYL RELATED DB: PDB
REMARK 900 INSULIN (T3R3) (PH 6.4, 0.75 M NACL) COMPLEXED WITH TWO ZINC IONS
REMARK 900 AND TYLENOL ( 4'-HYDROXYACETANILIDE)
REMARK 900 RELATED ID: 1TYM RELATED DB: PDB
REMARK 900 INSULIN (T3R3) (PH 5.6, 1.0 M NACL) COMPLEXED WITH TWO ZINC IONS
REMARK 900 AND TYLENOL ( 4'-HYDROXYACETANILIDE)
REMARK 900 RELATED ID: 1VKT RELATED DB: PDB
REMARK 900 HUMAN INSULIN TWO DISULFIDE MODEL, NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1XDA RELATED DB: PDB
REMARK 900 STRUCTURE OF INSULIN
REMARK 900 RELATED ID: 1XGL RELATED DB: PDB
REMARK 900 HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1ZEG RELATED DB: PDB
REMARK 900 STRUCTURE OF B28 ASP INSULIN IN COMPLEX WITH PHENOL
REMARK 900 RELATED ID: 1ZEH RELATED DB: PDB
REMARK 900 STRUCTURE OF INSULIN
REMARK 900 RELATED ID: 1ZNJ RELATED DB: PDB
REMARK 900 INSULIN, MONOCLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 2AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 2HIU RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETIC ACID, ZINC-FREE, 10
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 3AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, REFINED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 4AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 'GREEN' SUBSTATE,
REMARK 900 AVERAGE STRUCTURE
REMARK 900 RELATED ID: 5AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 'RED' SUBSTATE, AVERAGE
REMARK 900 STRUCTURE
DBREF 1UZ9 A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1UZ9 B 1 29 UNP P01308 INS_HUMAN 25 53
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 29 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 29 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 29 THR PRO LYS
HET CRS A1022 8
HET UZ9 B1029 36
HET ZN B1030 1
HET CL B1031 1
HETNAM CRS M-CRESOL
HETNAM UZ9 (2S)-2-AMINO-6-({(4R)-4-[(10R,13S)-10,13-DIMETHYL-3-
HETNAM 2 UZ9 OXOHEXADECAHYDRO-1H-CYCLOPENTA[A]PHENANTHREN-17-
HETNAM 3 UZ9 YL]PENTANOYL}AMINO)HEXANOIC ACID
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 3 CRS C7 H8 O
FORMUL 4 UZ9 C30 H50 N2 O4
FORMUL 5 ZN ZN 2+
FORMUL 6 CL CL 1-
FORMUL 7 HOH *50(H2 O)
HELIX 1 1 GLY A 1 CYS A 7 1 7
HELIX 2 2 SER A 12 GLU A 17 1 6
HELIX 3 3 PHE B 1 GLY B 20 1 20
HELIX 4 4 GLU B 21 GLY B 23 5 3
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.06
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.04
LINK C PRO B 28 N UZ9 B1029 1555 1555 1.34
LINK NE2 HIS B 10 ZN ZN B1030 2655 1555 2.06
LINK NE2 HIS B 10 ZN ZN B1030 3665 1555 2.05
LINK NE2 HIS B 10 ZN ZN B1030 1555 1555 2.05
LINK ZN ZN B1030 CL CL B1031 1555 1555 2.20
LINK ZN ZN B1030 CL CL B1031 1555 2655 2.20
LINK ZN ZN B1030 CL CL B1031 1555 3665 2.20
SITE 1 AC1 2 HIS B 10 CL B1031
SITE 1 AC2 2 HIS B 10 ZN B1030
SITE 1 AC3 5 CYS A 6 ILE A 10 CYS A 11 HIS B 5
SITE 2 AC3 5 LEU B 11
SITE 1 AC4 9 PHE B 1 TYR B 16 TYR B 26 THR B 27
SITE 2 AC4 9 PRO B 28 HOH B2019 HOH B2027 HOH B2028
SITE 3 AC4 9 HOH B2029
CRYST1 51.790 51.790 68.340 90.00 90.00 120.00 P 63 2 2 12
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 0.019309 0.011148 0.000000 0.00000
SCALE2 0.000000 0.022296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014633 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
