HEADER HORMONE 23-SEP-97 1ZNJ
TITLE INSULIN, MONOCLINIC CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: HEXAMER IN ASYMMETRIC UNIT, MONOCLINIC CRYSTAL FORM;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INSULIN;
COMPND 8 CHAIN: B, D, F, H, J, L;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: HEXAMER IN ASYMMETRIC UNIT, MONOCLINIC CRYSTAL FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 13 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS HORMONE, METABOLIC ROLE, CHEMICAL ACTIVITY, INSULIN GLUCOSE
KEYWDS 2 METABOLISM, DIABETES
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.W.TURKENBURG,J.L.WHITTINGHAM,J.P.TURKENBURG,G.G.DODSON,
AUTHOR 2 U.DEREWENDA,G.D.SMITH,E.J.DODSON,Z.S.DEREWENDA,B.XIAO
REVDAT 5 09-AUG-23 1ZNJ 1 REMARK
REVDAT 4 24-MAR-21 1ZNJ 1 REMARK LINK
REVDAT 3 13-JUL-11 1ZNJ 1 VERSN
REVDAT 2 24-FEB-09 1ZNJ 1 VERSN
REVDAT 1 28-JAN-98 1ZNJ 0
JRNL AUTH J.P.TURKENBURG,J.L.WHITTINGHAM,U.DEREWENDA,Z.S.DEREWENDA,
JRNL AUTH 2 E.J.DODSON,G.G.DODSON,G.D.SMITH,B.XIAO
JRNL TITL STRUCTURE DETERMINATION AND REFINEMENT OF TWO CRYSTAL FORMS
JRNL TITL 2 OF NATIVE INSULINS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.D.SMITH,G.G.DODSON
REMARK 1 TITL THE STRUCTURE OF A RHOMBOHEDRAL R6 INSULIN HEXAMER THAT
REMARK 1 TITL 2 BINDS PHENOL
REMARK 1 REF BIOPOLYMERS V. 32 441 1992
REMARK 1 REFN ISSN 0006-3525
REMARK 1 REFERENCE 2
REMARK 1 AUTH U.DEREWENDA,Z.DEREWENDA,E.J.DODSON,G.G.DODSON,C.D.REYNOLDS,
REMARK 1 AUTH 2 G.D.SMITH,C.SPARKS,D.SWENSON
REMARK 1 TITL PHENOL STABILIZES MORE HELIX IN A NEW SYMMETRICAL ZINC
REMARK 1 TITL 2 INSULIN HEXAMER
REMARK 1 REF NATURE V. 338 594 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH E.J.DODSON
REMARK 1 TITL MOLECULAR REPLACEMENT: THE METHOD AND ITS PROBLEMS (IN:
REMARK 1 TITL 2 MOLECULAR REPLACEMENT. PROCEEDINGS OF THE DARESBURY STUDY
REMARK 1 TITL 3 WEEKEND, 15-16 FEBRUARY, 1985. COMPILED BY P.A.MACHIN)
REMARK 1 REF DARESBURY LAB.[REP.]DL/SCI/R V. 23 33 1985
REMARK 1 REFN ISSN 0144-5677
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 22051
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.178
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) : 0.1780
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) : 22429
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2331
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 331
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) : 0.019 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.048 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.053 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.013 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.180 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.177 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.245 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : 0.286 ; 0.500
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) : 2.300 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 17.900; 20.000
REMARK 3 TRANSVERSE (DEGREES) : 15.400; 25.000
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 1ZNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177496.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-92
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.44
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, CCP4
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22429
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.22700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: 2ZINC INSULIN DIMER (PDB ENTRY 4INS)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BATCH, 1.7MG/ML INSULIN, 0.02 ZINC
REMARK 280 ACETATE, 0.7% (V/V) PHENOL, 0.34M SODIUM CHLORIDE, PH 7.44,
REMARK 280 BATCH METHOD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 30.82500
REMARK 290 SMTRY3 2 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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
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 THR D 30
REMARK 465 THR F 30
REMARK 465 THR H 30
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 TYR A 14 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 THR B 30 C O CB OG1 CG2
REMARK 470 PHE D 1 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 29 CD CE NZ
REMARK 470 PHE F 1 N CB CG CD1 CD2 CE1 CE2
REMARK 470 PHE F 1 CZ
REMARK 470 LYS F 29 CG CD CE NZ
REMARK 470 LYS H 29 CA C O CB CG CD CE
REMARK 470 LYS H 29 NZ
REMARK 470 LYS J 29 CG CD CE NZ
REMARK 470 THR J 30 C O CB OG1 CG2
REMARK 470 PHE L 1 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU L 21 CG CD OE1 OE2
REMARK 470 LYS L 29 CE NZ
REMARK 470 THR L 30 C O CB OG1 CG2
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 OE1 GLN G 5 OH TYR G 19 2.08
REMARK 500 OE1 GLN B 4 O HOH B 36 2.09
REMARK 500 O HOH H 38 O HOH H 53 2.10
REMARK 500 O HOH H 35 O HOH H 39 2.15
REMARK 500 O HOH F 46 O HOH L 44 2.16
REMARK 500 O SER F 9 O HOH F 37 2.16
REMARK 500 O HOH H 45 O HOH H 47 2.18
REMARK 500 OD1 ASN A 18 O HOH A 26 2.18
REMARK 500 O HOH L 51 O HOH L 54 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 ASN A 21 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 LEU B 6 CB - CG - CD2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLY B 8 CA - C - O ANGL. DEV. = -13.5 DEGREES
REMARK 500 VAL B 12 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TYR C 14 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 CYS C 20 CA - CB - SG ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLN D 4 CA - CB - CG ANGL. DEV. = -15.5 DEGREES
REMARK 500 TYR D 16 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG D 22 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG D 22 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 CYS E 11 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU E 13 CB - CA - C ANGL. DEV. = 11.7 DEGREES
REMARK 500 HIS F 10 CE1 - NE2 - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 LEU F 11 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES
REMARK 500 GLU F 13 OE1 - CD - OE2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLU F 13 CG - CD - OE2 ANGL. DEV. = -12.4 DEGREES
REMARK 500 TYR F 16 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG F 22 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TYR F 26 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLU G 4 CG - CD - OE1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG H 22 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 PHE H 25 N - CA - CB ANGL. DEV. = 13.7 DEGREES
REMARK 500 GLU I 17 OE1 - CD - OE2 ANGL. DEV. = 15.5 DEGREES
REMARK 500 GLU I 17 CG - CD - OE2 ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG J 22 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG J 22 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 CYS K 6 CB - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 SER K 9 N - CA - CB ANGL. DEV. = 14.6 DEGREES
REMARK 500 SER L 9 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 TYR L 16 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG L 22 CG - CD - NE ANGL. DEV. = 15.7 DEGREES
REMARK 500 ARG L 22 NH1 - CZ - NH2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG L 22 NE - CZ - NH1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG L 22 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 TYR L 26 CB - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TYR L 26 CB - CG - CD1 ANGL. DEV. = -4.0 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 LYS B 29 74.93 -49.07
REMARK 500 VAL J 2 38.49 -80.10
REMARK 500 LYS J 29 -67.07 -93.09
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 B 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 CL B 32 CL 108.5
REMARK 620 3 HIS F 10 NE2 107.5 112.6
REMARK 620 4 HIS J 10 NE2 122.6 104.2 101.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 10 NE2
REMARK 620 2 HIS H 10 NE2 110.0
REMARK 620 3 CL H 31 CL 111.2 109.8
REMARK 620 4 HIS L 10 NE2 98.0 119.8 107.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH A 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH C 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH E 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH G 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH I 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH K 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH B 33
DBREF 1ZNJ A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1ZNJ B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1ZNJ C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1ZNJ D 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1ZNJ E 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1ZNJ F 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1ZNJ G 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1ZNJ H 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1ZNJ I 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1ZNJ J 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1ZNJ K 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1ZNJ L 1 30 UNP P01308 INS_HUMAN 25 54
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 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 30 THR PRO LYS THR
SEQRES 1 C 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 C 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 D 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 D 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 D 30 THR PRO LYS THR
SEQRES 1 E 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 E 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 F 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 F 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 F 30 THR PRO LYS THR
SEQRES 1 G 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 G 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 H 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 H 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 H 30 THR PRO LYS THR
SEQRES 1 I 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 I 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 J 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 J 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 J 30 THR PRO LYS THR
SEQRES 1 K 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 K 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 L 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 L 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 L 30 THR PRO LYS THR
HET IPH A 22 7
HET ZN B 31 1
HET CL B 32 1
HET IPH B 33 7
HET IPH C 22 7
HET ZN D 31 1
HET IPH E 22 7
HET IPH G 22 7
HET CL H 31 1
HET IPH I 22 7
HET IPH K 22 7
HETNAM IPH PHENOL
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 13 IPH 7(C6 H6 O)
FORMUL 14 ZN 2(ZN 2+)
FORMUL 15 CL 2(CL 1-)
FORMUL 24 HOH *331(H2 O)
HELIX 1 1 ILE A 2 CYS A 6 1 5
HELIX 2 2 LEU A 13 TYR A 19 1 7
HELIX 3 3 VAL B 2 ARG B 22 1 21
HELIX 4 4 ILE C 2 CYS C 6 1 5
HELIX 5 5 LEU C 13 TYR C 19 1 7
HELIX 6 6 VAL D 2 ARG D 22 1 21
HELIX 7 7 ILE E 2 THR E 8 1 7
HELIX 8 8 LEU E 13 TYR E 19 1 7
HELIX 9 9 ASN F 3 ARG F 22 1 20
HELIX 10 10 ILE G 2 CYS G 6 1 5
HELIX 11 11 LEU G 13 TYR G 19 1 7
HELIX 12 12 VAL H 2 ARG H 22 1 21
HELIX 13 13 ILE I 2 CYS I 6 1 5
HELIX 14 14 LEU I 13 TYR I 19 1 7
HELIX 15 15 ASN J 3 ARG J 22 1 20
HELIX 16 16 ILE K 2 CYS K 6 1 5
HELIX 17 17 LEU K 13 TYR K 19 1 7
HELIX 18 18 VAL L 2 ARG L 22 1 21
SHEET 1 A 2 PHE B 24 TYR B 26 0
SHEET 2 A 2 PHE D 24 TYR D 26 -1 O PHE D 24 N TYR B 26
SHEET 1 B 2 PHE F 24 TYR F 26 0
SHEET 2 B 2 PHE H 24 TYR H 26 -1 O PHE H 24 N TYR F 26
SHEET 1 C 2 PHE J 24 TYR J 26 0
SHEET 2 C 2 PHE L 24 TYR L 26 -1 O PHE L 24 N TYR J 26
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.01
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 19 1555 1555 1.99
SSBOND 4 CYS C 6 CYS C 11 1555 1555 1.95
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.01
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.06
SSBOND 7 CYS E 6 CYS E 11 1555 1555 1.88
SSBOND 8 CYS E 7 CYS F 7 1555 1555 2.04
SSBOND 9 CYS E 20 CYS F 19 1555 1555 2.03
SSBOND 10 CYS G 6 CYS G 11 1555 1555 1.98
SSBOND 11 CYS G 7 CYS H 7 1555 1555 2.04
SSBOND 12 CYS G 20 CYS H 19 1555 1555 1.95
SSBOND 13 CYS I 6 CYS I 11 1555 1555 2.00
SSBOND 14 CYS I 7 CYS J 7 1555 1555 1.93
SSBOND 15 CYS I 20 CYS J 19 1555 1555 2.02
SSBOND 16 CYS K 6 CYS K 11 1555 1555 2.03
SSBOND 17 CYS K 7 CYS L 7 1555 1555 1.96
SSBOND 18 CYS K 20 CYS L 19 1555 1555 2.03
LINK NE2 HIS B 10 ZN ZN B 31 1555 1555 1.76
LINK ZN ZN B 31 CL CL B 32 1555 1555 2.33
LINK ZN ZN B 31 NE2 HIS F 10 1555 1555 2.18
LINK ZN ZN B 31 NE2 HIS J 10 1555 1555 2.01
LINK NE2 HIS D 10 ZN ZN D 31 1555 1555 2.21
LINK ZN ZN D 31 NE2 HIS H 10 1555 1555 1.82
LINK ZN ZN D 31 CL CL H 31 1555 1555 2.30
LINK ZN ZN D 31 NE2 HIS L 10 1555 1555 1.93
SITE 1 AC1 4 HIS B 10 CL B 32 HIS F 10 HIS J 10
SITE 1 AC2 4 HIS D 10 HIS H 10 CL H 31 HIS L 10
SITE 1 AC3 4 HIS B 10 ZN B 31 IPH B 33 HIS J 10
SITE 1 AC4 3 ZN D 31 HIS H 10 HIS L 10
SITE 1 AC5 6 CYS A 6 SER A 9 ILE A 10 CYS A 11
SITE 2 AC5 6 LEU B 11 HIS F 5
SITE 1 AC6 5 CYS C 6 ILE C 10 CYS C 11 LEU D 11
SITE 2 AC6 5 HIS L 5
SITE 1 AC7 6 CYS E 6 SER E 9 ILE E 10 CYS E 11
SITE 2 AC7 6 LEU F 11 HIS J 5
SITE 1 AC8 4 CYS G 6 SER G 9 ILE G 10 CYS G 11
SITE 1 AC9 5 HIS B 5 CYS I 6 ILE I 10 CYS I 11
SITE 2 AC9 5 LEU J 11
SITE 1 BC1 4 CYS K 6 ILE K 10 CYS K 11 HOH K 24
SITE 1 BC2 5 LEU B 6 CL B 32 LEU F 6 ASN J 3
SITE 2 BC2 5 LEU J 6
CRYST1 61.230 61.650 48.050 90.00 110.50 90.00 P 1 21 1 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 0.016332 0.000000 0.006106 0.00000
SCALE2 0.000000 0.016221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022219 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
