Header list of 1tu2.pdb file
Complete list - r 25 2 Bytes
HEADER ELECTRON TRANSPORT 24-JUN-04 1TU2
TITLE THE COMPLEX OF NOSTOC CYTOCHROME F AND PLASTOCYANIN DETERMIN WITH
TITLE 2 PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND
TITLE 3 PLASTOCYANIN, 10 STRUCTURES
CAVEAT 1TU2 THERE ARE SEVERAL CHIRALITY ERRORS IN CHAIN B.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASTOCYANIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: APOCYTOCHROME F;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: SOLUBLE DOMAIN;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP.;
SOURCE 3 ORGANISM_TAXID: 1168;
SOURCE 4 STRAIN: PCC 7119;
SOURCE 5 ORGANELLE: THYLACOID;
SOURCE 6 CELLULAR_LOCATION: THYLAKOID LUMEN;
SOURCE 7 GENE: PETE;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PEAP-WT;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: NOSTOC SP.;
SOURCE 16 ORGANISM_TAXID: 1168;
SOURCE 17 STRAIN: PCC 7119;
SOURCE 18 ORGANELLE: THYLACOID;
SOURCE 19 CELLULAR_LOCATION: THYLAKOID MEMBRANE;
SOURCE 20 GENE: PETA;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 23 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 24 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PEAF-WT
KEYWDS ELECTRON TRANSPORT, PARAMAGNETIC, CHEMICAL SHIFT, COMPLEX FORMATION,
KEYWDS 2 DYNAMIC COMPLEX, PHOTOSYNTHESIS, PSEUDOCONTACT SHIFT, ELECTRON
KEYWDS 3 TRANSPORT PROTEINS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR I.DIAZ-MORENO,A.DIAZ-QUINTANA,M.A.DE LA ROSA,M.UBBINK
REVDAT 3 13-JUL-11 1TU2 1 VERSN
REVDAT 2 24-FEB-09 1TU2 1 VERSN
REVDAT 1 01-MAR-05 1TU2 0
JRNL AUTH I.DIAZ-MORENO,A.DIAZ-QUINTANA,M.A.DE LA ROSA,M.UBBINK
JRNL TITL STRUCTURE OF THE COMPLEX BETWEEN PLASTOCYANIN AND CYTOCHROME
JRNL TITL 2 F FROM THE CYANOBACTERIUM NOSTOC SP. PCC 7119 AS DETERMINED
JRNL TITL 3 BY PARAMAGNETIC NMR. THE BALANCE BETWEEN ELECTROSTATIC AND
JRNL TITL 4 HYDROPHOBIC INTERACTIONS WITHIN THE TRANSIENT COMPLEX
JRNL TITL 5 DETERMINES THE RELATIVE ORIENTATION OF THE TWO PROTEINS.
JRNL REF J.BIOL.CHEM. V. 280 18908 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15705583
JRNL DOI 10.1074/JBC.M413298200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.P.MOLINA-HEREDIA,M.HERVAS,J.A.NAVARRO,M.A.DE LA ROSA
REMARK 1 TITL PLASTOCYANIN FROM NOSTOC SP. PCC 7119 USES THE SAME
REMARK 1 TITL 2 ELECTROSTATIC AND HYDROPHOBIC SURFACE AREAS FOR THE
REMARK 1 TITL 3 INTERACTION WITH BOTH CYTOCHROME F AND PHOTOSYSTEM I
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.P.MOLINA-HEREDIA,M.HERVAS,J.A.NAVARRO,M.A.DE LA ROSA
REMARK 1 TITL CLONING AND CORRECT EXPRESSION IN ESCHERICHIA COLI OF THE
REMARK 1 TITL 2 PETE AND PETJ GENES RESPECTIVELY ENCODING PLASTOCYANIN AND
REMARK 1 TITL 3 CYTOCHROME C6 FROM THE CYANOBACTERIUM ANABAENA SP. PCC 7119
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 243 302 1998
REMARK 1 REFN ISSN 0006-291X
REMARK 1 PMID 9473522
REMARK 1 DOI 10.1006/BBRC.1997.7953
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND BELOW
REMARK 3 AND IN THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1TU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB022902.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 10MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, AZARA 2.70, XWINNMR
REMARK 210 3.1
REMARK 210 METHOD USED : DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 5000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : REFER TO PUBLICATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: SYSTEM: 95% BUFFER (10 MM SODIUM PHOSPHATE) 5% D2O
REMARK 210 CADMIUM(II)-SUBSTITUTED 15N PLASTOCYANIN AND UNLABELED CYTOCHROME
REMARK 210 F WERE USED.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HD22 LEU A 64 HG2 PRO B 118 0.22
REMARK 500 HD21 LEU A 64 HG3 PRO B 118 0.95
REMARK 500 HE3 MET A 66 HD23 LEU B 119 0.97
REMARK 500 HE1 MET A 66 HD23 LEU B 119 1.00
REMARK 500 CE MET A 66 HD23 LEU B 119 1.01
REMARK 500 CD2 LEU A 64 HG2 PRO B 118 1.02
REMARK 500 HD22 LEU A 64 CG PRO B 118 1.04
REMARK 500 HZ1 LYS A 100 HG1 THR A 102 1.08
REMARK 500 HG13 VAL A 36 HE22 GLN B 104 1.22
REMARK 500 HD21 LEU A 14 HG23 VAL A 36 1.28
REMARK 500 HG LEU A 59 H SER A 60 1.33
REMARK 500 HG22 VAL A 42 HB2 TYR A 88 1.33
REMARK 500 HZ1 LYS A 62 HB2 GLN A 63 1.33
REMARK 500 H THR B 44 HG SER B 133 1.34
REMARK 500 HH TYR B 172 HG3 PRO B 212 1.43
REMARK 500 HD2 PRO A 37 CE2 TYR B 102 1.43
REMARK 500 HA VAL A 36 HE22 GLN B 104 1.44
REMARK 500 HD22 LEU A 14 HE2 MET A 97 1.46
REMARK 500 HE3 MET A 66 CD2 LEU B 119 1.49
REMARK 500 HB2 TYR A 85 HG23 ILE A 101 1.50
REMARK 500 HD11 LEU A 7 HB2 HIS A 39 1.51
REMARK 500 HD13 LEU A 55 HB2 ALA A 56 1.52
REMARK 500 HD2 PRO A 37 HE2 TYR B 102 1.52
REMARK 500 HE3 MET A 66 HD21 LEU B 119 1.55
REMARK 500 HA LEU A 32 HG SER A 71 1.58
REMARK 500 HD23 LEU A 64 HG2 PRO B 118 1.58
REMARK 500 CD2 LEU A 64 CG PRO B 118 1.59
REMARK 500 CE MET A 66 CD2 LEU B 119 2.06
REMARK 500 O PRO A 37 OH TYR B 102 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS A 39 NE2 HIS A 39 CD2 -0.089
REMARK 500 1 HIS A 92 NE2 HIS A 92 CD2 -0.081
REMARK 500 1 HIS B 26 CE1 HIS B 26 NE2 -0.067
REMARK 500 1 ILE B 115 CA ILE B 115 CB 0.209
REMARK 500 1 VAL B 116 CA VAL B 116 CB 0.182
REMARK 500 1 VAL B 116 CB VAL B 116 CG1 -0.208
REMARK 500 1 VAL B 116 CB VAL B 116 CG2 0.158
REMARK 500 1 VAL B 131 CA VAL B 131 CB 0.144
REMARK 500 2 HIS A 39 NE2 HIS A 39 CD2 -0.090
REMARK 500 2 HIS A 92 NE2 HIS A 92 CD2 -0.081
REMARK 500 2 ILE B 115 CA ILE B 115 CB 0.236
REMARK 500 2 VAL B 116 CA VAL B 116 CB 0.196
REMARK 500 3 HIS A 39 NE2 HIS A 39 CD2 -0.089
REMARK 500 3 HIS A 92 NE2 HIS A 92 CD2 -0.081
REMARK 500 3 HIS B 26 CE1 HIS B 26 NE2 -0.067
REMARK 500 3 ILE B 115 CA ILE B 115 CB 0.144
REMARK 500 3 VAL B 131 CA VAL B 131 CB 0.238
REMARK 500 3 VAL B 131 CB VAL B 131 CG2 -0.128
REMARK 500 4 HIS A 39 NE2 HIS A 39 CD2 -0.089
REMARK 500 4 HIS A 92 NE2 HIS A 92 CD2 -0.083
REMARK 500 4 VAL B 131 CA VAL B 131 CB 0.235
REMARK 500 4 VAL B 131 CB VAL B 131 CG1 -0.159
REMARK 500 4 VAL B 193 CA VAL B 193 CB 0.160
REMARK 500 5 HIS A 39 NE2 HIS A 39 CD2 -0.089
REMARK 500 5 HIS A 92 NE2 HIS A 92 CD2 -0.082
REMARK 500 5 HIS B 26 CE1 HIS B 26 NE2 -0.067
REMARK 500 5 ILE B 115 CA ILE B 115 CB 0.168
REMARK 500 5 VAL B 131 CA VAL B 131 CB 0.205
REMARK 500 5 VAL B 131 CB VAL B 131 CG1 0.132
REMARK 500 6 HIS A 39 NE2 HIS A 39 CD2 -0.089
REMARK 500 6 HIS A 92 NE2 HIS A 92 CD2 -0.085
REMARK 500 6 VAL B 131 CA VAL B 131 CB 0.236
REMARK 500 6 VAL B 131 CB VAL B 131 CG1 -0.158
REMARK 500 6 VAL B 193 CA VAL B 193 CB 0.163
REMARK 500 7 HIS A 39 NE2 HIS A 39 CD2 -0.093
REMARK 500 7 HIS A 92 NE2 HIS A 92 CD2 -0.086
REMARK 500 7 VAL B 34 CB VAL B 34 CG2 0.138
REMARK 500 7 VAL B 116 CB VAL B 116 CG2 0.150
REMARK 500 7 VAL B 225 CB VAL B 225 CG2 0.163
REMARK 500 8 HIS A 39 NE2 HIS A 39 CD2 -0.091
REMARK 500 8 HIS A 92 NE2 HIS A 92 CD2 -0.085
REMARK 500 8 VAL B 34 CB VAL B 34 CG2 0.137
REMARK 500 8 VAL B 116 CB VAL B 116 CG2 0.150
REMARK 500 8 VAL B 225 CB VAL B 225 CG2 0.164
REMARK 500 9 HIS A 39 NE2 HIS A 39 CD2 -0.093
REMARK 500 9 HIS A 92 NE2 HIS A 92 CD2 -0.086
REMARK 500 9 VAL B 34 CB VAL B 34 CG2 0.138
REMARK 500 9 VAL B 116 CB VAL B 116 CG2 0.150
REMARK 500 9 VAL B 225 CB VAL B 225 CG2 0.164
REMARK 500 10 HIS A 39 NE2 HIS A 39 CD2 -0.093
REMARK 500
REMARK 500 THIS ENTRY HAS 52 BOND DEVIATIONS.
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 1 TYR A 88 N - CA - C ANGL. DEV. = 21.6 DEGREES
REMARK 500 1 VAL B 34 CB - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 1 ILE B 84 CG1 - CB - CG2 ANGL. DEV. = 19.3 DEGREES
REMARK 500 1 ILE B 115 N - CA - CB ANGL. DEV. = -15.1 DEGREES
REMARK 500 1 ILE B 115 CG1 - CB - CG2 ANGL. DEV. = 17.1 DEGREES
REMARK 500 1 ILE B 115 CA - CB - CG1 ANGL. DEV. = -13.7 DEGREES
REMARK 500 1 ILE B 115 CA - CB - CG2 ANGL. DEV. = -14.9 DEGREES
REMARK 500 1 VAL B 116 CB - CA - C ANGL. DEV. = -14.7 DEGREES
REMARK 500 1 VAL B 116 N - CA - CB ANGL. DEV. = 13.3 DEGREES
REMARK 500 1 VAL B 116 CA - CB - CG2 ANGL. DEV. = -20.4 DEGREES
REMARK 500 1 VAL B 131 CG1 - CB - CG2 ANGL. DEV. = 11.6 DEGREES
REMARK 500 1 VAL B 131 CA - CB - CG1 ANGL. DEV. = -14.4 DEGREES
REMARK 500 1 VAL B 131 CA - CB - CG2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 1 ILE B 142 CG1 - CB - CG2 ANGL. DEV. = 16.5 DEGREES
REMARK 500 1 VAL B 149 CG1 - CB - CG2 ANGL. DEV. = 11.8 DEGREES
REMARK 500 1 VAL B 193 CG1 - CB - CG2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 1 ILE B 199 CG1 - CB - CG2 ANGL. DEV. = 18.7 DEGREES
REMARK 500 1 VAL B 225 CB - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 2 TYR A 88 N - CA - C ANGL. DEV. = 21.6 DEGREES
REMARK 500 2 VAL B 34 CB - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 2 ILE B 84 CG1 - CB - CG2 ANGL. DEV. = 20.0 DEGREES
REMARK 500 2 ILE B 115 CB - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 2 ILE B 115 N - CA - CB ANGL. DEV. = -20.7 DEGREES
REMARK 500 2 ILE B 115 CG1 - CB - CG2 ANGL. DEV. = 14.1 DEGREES
REMARK 500 2 ILE B 115 CA - CB - CG2 ANGL. DEV. = -25.2 DEGREES
REMARK 500 2 VAL B 116 CB - CA - C ANGL. DEV. = -15.7 DEGREES
REMARK 500 2 VAL B 116 CG1 - CB - CG2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 2 VAL B 116 CA - CB - CG1 ANGL. DEV. = -17.7 DEGREES
REMARK 500 2 VAL B 116 CA - CB - CG2 ANGL. DEV. = -11.3 DEGREES
REMARK 500 2 VAL B 131 CG1 - CB - CG2 ANGL. DEV. = 13.7 DEGREES
REMARK 500 2 VAL B 131 CA - CB - CG1 ANGL. DEV. = -9.8 DEGREES
REMARK 500 2 ILE B 142 CG1 - CB - CG2 ANGL. DEV. = 17.3 DEGREES
REMARK 500 2 VAL B 149 CG1 - CB - CG2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 2 VAL B 193 CG1 - CB - CG2 ANGL. DEV. = 14.3 DEGREES
REMARK 500 2 ILE B 199 CG1 - CB - CG2 ANGL. DEV. = 19.6 DEGREES
REMARK 500 2 VAL B 225 CB - CA - C ANGL. DEV. = -16.0 DEGREES
REMARK 500 3 TYR A 88 N - CA - C ANGL. DEV. = 21.6 DEGREES
REMARK 500 3 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 3 VAL B 34 CB - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 3 ILE B 84 CG1 - CB - CG2 ANGL. DEV. = 17.5 DEGREES
REMARK 500 3 ILE B 115 N - CA - CB ANGL. DEV. = -14.8 DEGREES
REMARK 500 3 ILE B 115 CA - CB - CG1 ANGL. DEV. = -19.5 DEGREES
REMARK 500 3 VAL B 116 CB - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 3 VAL B 116 CA - CB - CG1 ANGL. DEV. = -11.0 DEGREES
REMARK 500 3 VAL B 116 CA - CB - CG2 ANGL. DEV. = -17.0 DEGREES
REMARK 500 3 VAL B 131 CG1 - CB - CG2 ANGL. DEV. = 12.7 DEGREES
REMARK 500 3 VAL B 131 CA - CB - CG1 ANGL. DEV. = -21.7 DEGREES
REMARK 500 3 ILE B 142 CG1 - CB - CG2 ANGL. DEV. = 15.2 DEGREES
REMARK 500 3 VAL B 149 CG1 - CB - CG2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 VAL B 193 CA - CB - CG1 ANGL. DEV. = -11.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 178 ANGLE DEVIATIONS.
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 1 THR A 2 89.70 -61.55
REMARK 500 1 LYS A 6 65.38 -67.33
REMARK 500 1 LEU A 7 68.27 -29.52
REMARK 500 1 SER A 9 54.04 -1.00
REMARK 500 1 ASP A 10 -60.19 25.53
REMARK 500 1 LEU A 14 46.73 -74.80
REMARK 500 1 PHE A 16 75.35 -102.25
REMARK 500 1 ALA A 19 -44.23 9.73
REMARK 500 1 LYS A 20 71.66 -104.62
REMARK 500 1 PRO A 25 77.51 -52.18
REMARK 500 1 ASP A 27 92.09 -6.71
REMARK 500 1 THR A 28 35.91 -64.01
REMARK 500 1 VAL A 36 70.70 12.82
REMARK 500 1 ASP A 44 93.77 -53.47
REMARK 500 1 ALA A 50 67.41 -106.51
REMARK 500 1 SER A 52 56.89 -115.87
REMARK 500 1 ALA A 53 -48.00 -24.51
REMARK 500 1 ALA A 56 -27.63 -166.81
REMARK 500 1 LYS A 57 -55.59 65.04
REMARK 500 1 LYS A 62 155.19 152.43
REMARK 500 1 GLN A 63 65.99 105.52
REMARK 500 1 LEU A 64 84.29 38.13
REMARK 500 1 SER A 67 65.98 -112.61
REMARK 500 1 PRO A 68 81.63 -52.03
REMARK 500 1 ASP A 79 42.61 -79.13
REMARK 500 1 ALA A 82 77.66 -16.05
REMARK 500 1 TYR A 85 77.75 -62.07
REMARK 500 1 CYS A 89 82.19 -63.94
REMARK 500 1 GLU A 90 -72.43 -20.52
REMARK 500 1 ARG A 93 79.57 -25.25
REMARK 500 1 MET A 97 43.84 -108.46
REMARK 500 1 ALA A 104 -72.25 -12.39
REMARK 500 1 TYR B 9 53.06 -149.69
REMARK 500 1 THR B 12 54.39 -140.33
REMARK 500 1 ASP B 55 109.58 -58.76
REMARK 500 1 ASP B 100 48.68 -140.89
REMARK 500 1 TYR B 124 50.92 -116.26
REMARK 500 1 ASP B 139 94.25 -169.16
REMARK 500 1 ASN B 168 33.54 -89.16
REMARK 500 1 ALA B 176 145.48 -172.98
REMARK 500 1 ALA B 184 110.09 -165.78
REMARK 500 1 GLU B 189 -65.82 -134.91
REMARK 500 1 LYS B 200 80.17 -69.80
REMARK 500 1 PRO B 215 179.23 -59.81
REMARK 500 2 THR A 2 89.65 -61.52
REMARK 500 2 LYS A 6 65.40 -67.34
REMARK 500 2 LEU A 7 68.20 -29.49
REMARK 500 2 SER A 9 54.13 -1.09
REMARK 500 2 ASP A 10 -60.16 25.48
REMARK 500 2 LEU A 14 46.66 -74.80
REMARK 500
REMARK 500 THIS ENTRY HAS 440 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 93 0.16 SIDE CHAIN
REMARK 500 1 ARG B 19 0.12 SIDE CHAIN
REMARK 500 1 ARG B 155 0.09 SIDE CHAIN
REMARK 500 1 ARG B 254 0.13 SIDE CHAIN
REMARK 500 2 ARG A 93 0.15 SIDE CHAIN
REMARK 500 2 ARG B 19 0.12 SIDE CHAIN
REMARK 500 2 ARG B 155 0.09 SIDE CHAIN
REMARK 500 2 ARG B 254 0.13 SIDE CHAIN
REMARK 500 3 ARG A 93 0.15 SIDE CHAIN
REMARK 500 3 ARG B 19 0.12 SIDE CHAIN
REMARK 500 3 ARG B 155 0.08 SIDE CHAIN
REMARK 500 3 ARG B 254 0.12 SIDE CHAIN
REMARK 500 4 ARG A 93 0.16 SIDE CHAIN
REMARK 500 4 ARG B 19 0.12 SIDE CHAIN
REMARK 500 4 ARG B 155 0.09 SIDE CHAIN
REMARK 500 4 ARG B 254 0.13 SIDE CHAIN
REMARK 500 5 ARG A 93 0.15 SIDE CHAIN
REMARK 500 5 ARG B 19 0.12 SIDE CHAIN
REMARK 500 5 ARG B 155 0.09 SIDE CHAIN
REMARK 500 5 ARG B 254 0.13 SIDE CHAIN
REMARK 500 6 ARG A 93 0.16 SIDE CHAIN
REMARK 500 6 ARG B 19 0.12 SIDE CHAIN
REMARK 500 6 ARG B 155 0.09 SIDE CHAIN
REMARK 500 6 ARG B 254 0.13 SIDE CHAIN
REMARK 500 7 ARG A 93 0.17 SIDE CHAIN
REMARK 500 7 ARG B 19 0.15 SIDE CHAIN
REMARK 500 7 ARG B 155 0.12 SIDE CHAIN
REMARK 500 7 ARG B 254 0.15 SIDE CHAIN
REMARK 500 8 ARG A 93 0.18 SIDE CHAIN
REMARK 500 8 ARG B 19 0.15 SIDE CHAIN
REMARK 500 8 ARG B 155 0.12 SIDE CHAIN
REMARK 500 8 ARG B 254 0.16 SIDE CHAIN
REMARK 500 9 ARG A 93 0.18 SIDE CHAIN
REMARK 500 9 ARG B 19 0.15 SIDE CHAIN
REMARK 500 9 ARG B 155 0.12 SIDE CHAIN
REMARK 500 9 ARG B 254 0.16 SIDE CHAIN
REMARK 500 10 ARG A 93 0.15 SIDE CHAIN
REMARK 500 10 ARG B 19 0.12 SIDE CHAIN
REMARK 500 10 ARG B 155 0.09 SIDE CHAIN
REMARK 500 10 ARG B 254 0.12 SIDE CHAIN
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 1 ASP A 44 24.8 L L OUTSIDE RANGE
REMARK 500 1 TYR A 88 21.8 L L OUTSIDE RANGE
REMARK 500 1 VAL B 131 24.0 L L OUTSIDE RANGE
REMARK 500 2 ASP A 44 24.8 L L OUTSIDE RANGE
REMARK 500 2 TYR A 88 21.8 L L OUTSIDE RANGE
REMARK 500 2 ILE B 115 46.1 L L OUTSIDE RANGE
REMARK 500 2 VAL B 131 24.4 L L OUTSIDE RANGE
REMARK 500 3 ASP A 44 24.9 L L OUTSIDE RANGE
REMARK 500 3 TYR A 88 21.7 L L OUTSIDE RANGE
REMARK 500 4 ASP A 44 24.6 L L OUTSIDE RANGE
REMARK 500 4 TYR A 88 21.3 L L OUTSIDE RANGE
REMARK 500 5 ASP A 44 24.8 L L OUTSIDE RANGE
REMARK 500 5 TYR A 88 21.8 L L OUTSIDE RANGE
REMARK 500 5 VAL B 131 23.8 L L OUTSIDE RANGE
REMARK 500 6 ASP A 44 24.6 L L OUTSIDE RANGE
REMARK 500 6 TYR A 88 21.3 L L OUTSIDE RANGE
REMARK 500 7 ASP A 44 24.3 L L OUTSIDE RANGE
REMARK 500 7 TYR A 88 21.9 L L OUTSIDE RANGE
REMARK 500 7 ILE B 115 46.3 L L OUTSIDE RANGE
REMARK 500 7 VAL B 131 24.6 L L OUTSIDE RANGE
REMARK 500 7 VAL B 160 22.9 L L OUTSIDE RANGE
REMARK 500 8 ASP A 44 24.4 L L OUTSIDE RANGE
REMARK 500 8 TYR A 88 22.0 L L OUTSIDE RANGE
REMARK 500 8 ILE B 115 46.3 L L OUTSIDE RANGE
REMARK 500 8 VAL B 131 24.6 L L OUTSIDE RANGE
REMARK 500 8 VAL B 160 22.9 L L OUTSIDE RANGE
REMARK 500 9 ASP A 44 24.3 L L OUTSIDE RANGE
REMARK 500 9 TYR A 88 22.0 L L OUTSIDE RANGE
REMARK 500 9 ILE B 115 46.3 L L OUTSIDE RANGE
REMARK 500 9 VAL B 131 24.7 L L OUTSIDE RANGE
REMARK 500 9 VAL B 160 22.9 L L OUTSIDE RANGE
REMARK 500 10 ASP A 44 24.7 L L OUTSIDE RANGE
REMARK 500 10 TYR A 88 21.8 L L OUTSIDE RANGE
REMARK 500 10 ILE B 115 49.2 L L OUTSIDE RANGE
REMARK 500 10 VAL B 131 24.2 L L OUTSIDE RANGE
REMARK 500 10 VAL B 160 25.0 L L OUTSIDE RANGE
REMARK 500 7 ILE B 84 -3.2 S R CBETA WRONG HAND
REMARK 500 7 ILE B 142 -2.9 S R CBETA WRONG HAND
REMARK 500 7 ILE B 199 -1.0 S R CBETA WRONG HAND
REMARK 500 8 ILE B 84 -3.2 S R CBETA WRONG HAND
REMARK 500 8 ILE B 142 -2.8 S R CBETA WRONG HAND
REMARK 500 8 ILE B 199 -1.0 S R CBETA WRONG HAND
REMARK 500 9 ILE B 84 -3.3 S R CBETA WRONG HAND
REMARK 500 9 ILE B 142 -3.0 S R CBETA WRONG HAND
REMARK 500 9 ILE B 199 -1.1 S R CBETA WRONG HAND
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 1 CU A 106 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 ND1
REMARK 620 2 CYS A 89 SG 110.6
REMARK 620 3 HIS A 92 ND1 109.4 110.5
REMARK 620 4 MET A 97 SD 106.6 106.9 112.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 HEC B 255 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 1 N
REMARK 620 2 HEC B 255 NA 88.6
REMARK 620 3 HEC B 255 NB 94.6 89.5
REMARK 620 4 HEC B 255 NC 91.4 180.0 90.5
REMARK 620 5 HEC B 255 ND 88.2 91.3 177.1 88.7
REMARK 620 6 HIS B 26 NE2 176.8 88.6 86.9 91.4 90.4
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 CU A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 255
DBREF 1TU2 A 1 105 UNP P46444 PLAS_ANASP 35 139
DBREF 1TU2 B 1 254 UNP Q93SW9 CYF_ANASP 45 298
SEQRES 1 A 105 GLU THR TYR THR VAL LYS LEU GLY SER ASP LYS GLY LEU
SEQRES 2 A 105 LEU VAL PHE GLU PRO ALA LYS LEU THR ILE LYS PRO GLY
SEQRES 3 A 105 ASP THR VAL GLU PHE LEU ASN ASN LYS VAL PRO PRO HIS
SEQRES 4 A 105 ASN VAL VAL PHE ASP ALA ALA LEU ASN PRO ALA LYS SER
SEQRES 5 A 105 ALA ASP LEU ALA LYS SER LEU SER HIS LYS GLN LEU LEU
SEQRES 6 A 105 MET SER PRO GLY GLN SER THR SER THR THR PHE PRO ALA
SEQRES 7 A 105 ASP ALA PRO ALA GLY GLU TYR THR PHE TYR CYS GLU PRO
SEQRES 8 A 105 HIS ARG GLY ALA GLY MET VAL GLY LYS ILE THR VAL ALA
SEQRES 9 A 105 GLY
SEQRES 1 B 254 TYR PRO PHE TRP ALA GLN GLN THR TYR PRO GLU THR PRO
SEQRES 2 B 254 ARG GLU PRO THR GLY ARG ILE VAL CYS ALA ASN CYS HIS
SEQRES 3 B 254 LEU ALA ALA LYS PRO THR GLU VAL GLU VAL PRO GLN SER
SEQRES 4 B 254 VAL LEU PRO ASP THR VAL PHE LYS ALA VAL VAL LYS ILE
SEQRES 5 B 254 PRO TYR ASP THR SER VAL GLN GLN VAL GLY ALA ASP GLY
SEQRES 6 B 254 SER LYS VAL GLY LEU ASN VAL GLY ALA VAL LEU MET LEU
SEQRES 7 B 254 PRO GLU GLY PHE LYS ILE ALA PRO GLU ASP ARG ILE PRO
SEQRES 8 B 254 GLU GLU LEU LYS GLU GLU ILE GLY ASP VAL TYR PHE GLN
SEQRES 9 B 254 PRO TYR GLY GLU ASP LYS ASP ASN ILE VAL ILE VAL GLY
SEQRES 10 B 254 PRO LEU PRO GLY GLU GLN TYR GLN GLU ILE VAL PHE PRO
SEQRES 11 B 254 VAL LEU SER PRO ASN PRO ALA ASN ASP LYS ASN ILE HIS
SEQRES 12 B 254 PHE GLY LYS TYR SER VAL HIS VAL GLY GLY ASN ARG GLY
SEQRES 13 B 254 ARG GLY GLN VAL TYR PRO THR GLY GLU LYS SER ASN ASN
SEQRES 14 B 254 ASN LEU TYR SER ALA ALA ALA THR GLY THR ILE SER LYS
SEQRES 15 B 254 ILE ALA LYS GLN GLU GLY GLU ASP GLY SER VAL LYS TYR
SEQRES 16 B 254 LEU VAL ASP ILE LYS THR GLU SER GLY GLU VAL VAL SER
SEQRES 17 B 254 ASP THR ILE PRO ALA GLY PRO GLU LEU ILE VAL SER GLU
SEQRES 18 B 254 GLY GLN ALA VAL THR ALA GLY ASP ALA LEU THR ASN ASN
SEQRES 19 B 254 PRO ASN VAL GLY GLY PHE GLY GLN LEU ASP ALA GLU ILE
SEQRES 20 B 254 VAL LEU GLN ASP ALA ASN ARG
HET CU A 106 1
HET HEC B 255 75
HETNAM CU COPPER (II) ION
HETNAM HEC HEME C
FORMUL 3 CU CU 2+
FORMUL 4 HEC C34 H34 FE N4 O4
HELIX 1 1 SER A 52 ALA A 56 5 5
HELIX 2 2 PRO A 91 ARG A 93 5 3
HELIX 3 3 TYR B 1 TYR B 9 1 9
HELIX 4 4 VAL B 21 HIS B 26 1 6
HELIX 5 5 PRO B 86 ILE B 90 5 5
HELIX 6 6 PRO B 91 ILE B 98 1 8
HELIX 7 7 GLY B 121 GLN B 125 1 5
HELIX 8 8 ASN B 135 ASP B 139 5 5
SHEET 1 A 3 THR A 4 VAL A 5 0
SHEET 2 A 3 GLU A 30 LEU A 32 1 O LEU A 32 N VAL A 5
SHEET 3 A 3 SER A 71 SER A 73 -1 O THR A 72 N PHE A 31
SHEET 1 B 3 VAL A 41 PHE A 43 0
SHEET 2 B 3 GLY A 83 CYS A 89 -1 O TYR A 88 N VAL A 42
SHEET 3 B 3 VAL A 98 VAL A 103 -1 O GLY A 99 N PHE A 87
SHEET 1 C 3 GLU B 33 GLU B 35 0
SHEET 2 C 3 VAL B 45 LYS B 51 -1 O LYS B 51 N GLU B 33
SHEET 3 C 3 GLU B 126 LEU B 132 -1 O ILE B 127 N VAL B 50
SHEET 1 D 6 SER B 39 VAL B 40 0
SHEET 2 D 6 GLY B 239 LEU B 249 1 O VAL B 248 N VAL B 40
SHEET 3 D 6 LYS B 146 ARG B 155 -1 N GLY B 153 O GLY B 241
SHEET 4 D 6 ASN B 71 MET B 77 -1 N VAL B 75 O GLY B 152
SHEET 5 D 6 ILE B 113 PRO B 120 -1 O LEU B 119 N VAL B 72
SHEET 6 D 6 GLN B 104 PRO B 105 -1 N GLN B 104 O ILE B 115
SHEET 1 E 2 GLN B 60 VAL B 61 0
SHEET 2 E 2 LYS B 67 VAL B 68 -1 O VAL B 68 N GLN B 60
SHEET 1 F 3 GLU B 205 VAL B 207 0
SHEET 2 F 3 SER B 192 LYS B 200 -1 N LYS B 200 O GLU B 205
SHEET 3 F 3 THR B 210 ILE B 211 -1 O ILE B 211 N LYS B 194
SHEET 1 G 4 GLU B 205 VAL B 207 0
SHEET 2 G 4 SER B 192 LYS B 200 -1 N LYS B 200 O GLU B 205
SHEET 3 G 4 GLY B 178 GLU B 187 -1 N THR B 179 O ILE B 199
SHEET 4 G 4 ALA B 224 VAL B 225 -1 O VAL B 225 N GLY B 178
LINK CU CU A 106 ND1 HIS A 39 1555 1555 1.77
LINK CU CU A 106 SG CYS A 89 1555 1555 2.00
LINK CU CU A 106 ND1 HIS A 92 1555 1555 1.77
LINK CU CU A 106 SD MET A 97 1555 1555 2.06
LINK FE HEC B 255 N TYR B 1 1555 1555 2.06
LINK FE HEC B 255 NE2 HIS B 26 1555 1555 2.13
CISPEP 1 GLU A 17 PRO A 18 1 -9.65
CISPEP 2 PRO A 37 PRO A 38 1 -7.23
CISPEP 3 GLY B 117 PRO B 118 1 -2.29
CISPEP 4 GLU A 17 PRO A 18 2 -9.61
CISPEP 5 PRO A 37 PRO A 38 2 -7.15
CISPEP 6 GLY B 117 PRO B 118 2 -2.29
CISPEP 7 GLU A 17 PRO A 18 3 -9.67
CISPEP 8 PRO A 37 PRO A 38 3 -7.23
CISPEP 9 GLY B 117 PRO B 118 3 -2.29
CISPEP 10 GLU A 17 PRO A 18 4 -9.64
CISPEP 11 PRO A 37 PRO A 38 4 -7.28
CISPEP 12 GLY B 117 PRO B 118 4 -2.29
CISPEP 13 GLU A 17 PRO A 18 5 -9.74
CISPEP 14 PRO A 37 PRO A 38 5 -7.24
CISPEP 15 GLY B 117 PRO B 118 5 -2.29
CISPEP 16 GLU A 17 PRO A 18 6 -9.70
CISPEP 17 PRO A 37 PRO A 38 6 -7.19
CISPEP 18 GLY B 117 PRO B 118 6 -2.29
CISPEP 19 GLU A 17 PRO A 18 7 -9.66
CISPEP 20 PRO A 37 PRO A 38 7 -7.21
CISPEP 21 GLY B 117 PRO B 118 7 -2.29
CISPEP 22 GLU A 17 PRO A 18 8 -9.69
CISPEP 23 PRO A 37 PRO A 38 8 -7.38
CISPEP 24 GLY B 117 PRO B 118 8 -2.29
CISPEP 25 GLU A 17 PRO A 18 9 -9.66
CISPEP 26 PRO A 37 PRO A 38 9 -7.16
CISPEP 27 GLY B 117 PRO B 118 9 -2.29
CISPEP 28 GLU A 17 PRO A 18 10 -9.68
CISPEP 29 PRO A 37 PRO A 38 10 -7.22
CISPEP 30 GLY B 117 PRO B 118 10 -2.29
SITE 1 AC1 4 HIS A 39 CYS A 89 HIS A 92 MET A 97
SITE 1 AC2 19 TYR B 1 PRO B 2 TRP B 4 CYS B 22
SITE 2 AC2 19 CYS B 25 HIS B 26 GLN B 60 LEU B 70
SITE 3 AC2 19 ASN B 71 VAL B 72 GLY B 73 ALA B 74
SITE 4 AC2 19 VAL B 75 ASN B 154 GLY B 156 ARG B 157
SITE 5 AC2 19 GLY B 158 VAL B 160 TYR B 161
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 25 2 Bytes