Header list of 1a1t.pdb file
Complete list - b 16 2 Bytes
HEADER VIRAL PROTEIN/RNA 15-DEC-97 1A1T
TITLE STRUCTURE OF THE HIV-1 NUCLEOCAPSID PROTEIN BOUND TO THE SL3 PSI-RNA
TITLE 2 RECOGNITION ELEMENT, NMR, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SL3 STEM-LOOP RNA;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: NUCLEOCAPSID PROTEIN;
COMPND 7 CHAIN: A;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 5 ORGANISM_TAXID: 11676;
SOURCE 6 STRAIN: NL4-3;
SOURCE 7 CELL_LINE: BL21;
SOURCE 8 GENE: NC;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSE;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PET-3A;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PRD2;
SOURCE 14 EXPRESSION_SYSTEM_GENE: NC
KEYWDS NUCLEOCAPSID PROTEIN, COMPLEX (NUCLEOCAPSID PROTEIN-RNA), STEM-LOOP
KEYWDS 2 RNA, VIRAL PROTEIN-RNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR R.N.DE GUZMAN,Z.R.WU,C.C.STALLING,L.PAPPALARDO,P.N.BORER,M.F.SUMMERS
REVDAT 3 16-FEB-22 1A1T 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1A1T 1 VERSN
REVDAT 1 17-JUN-98 1A1T 0
JRNL AUTH R.N.DE GUZMAN,Z.R.WU,C.C.STALLING,L.PAPPALARDO,P.N.BORER,
JRNL AUTH 2 M.F.SUMMERS
JRNL TITL STRUCTURE OF THE HIV-1 NUCLEOCAPSID PROTEIN BOUND TO THE SL3
JRNL TITL 2 PSI-RNA RECOGNITION ELEMENT.
JRNL REF SCIENCE V. 279 384 1998
JRNL REFN ISSN 0036-8075
JRNL PMID 9430589
JRNL DOI 10.1126/SCIENCE.279.5349.384
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE COORDINATES FOR THE 25 MODELS WHICH
REMARK 3 WERE SUBMITTED TO SCIENCE REPRESENT THE BEST-FIT SUPERPOSITION
REMARK 3 OF THE BACKBONE C, CA AND N ATOMS OF HIV-1 NUCLEOCAPSID PROTEIN
REMARK 3 (FROM LYS 3 - GLU 51) AND ALL HEAVY ATOMS OF SL3 RNA RECOGNITION
REMARK 3 ELEMENT (FROM C 4 - G17). THE STRUCTURES WERE GENERATED WITH A
REMARK 3 TOTAL OF 719 EXPERIMENTAL DISTANCE RESTRAINTS WITH THE USE OF
REMARK 3 THE PROGRAM DYANA. HYDROGEN BOND RESTRAINTS WERE USED TO IMPROVE
REMARK 3 CONVERGENCE OF THE STRUCTURES, BUT NOT ALTER THE GLOBAL FOLD.
REMARK 4
REMARK 4 1A1T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170287.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; TRIPLE-RESONANCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600; DRX800; GE OMEGA PSG 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 800
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST TOTAL PENALTY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: B, 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 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
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 G B 201 O4' G B 201 C4' -0.089
REMARK 500 1 A B 203 O4' A B 203 C4' -0.161
REMARK 500 1 C B 204 O4' C B 204 C4' -0.353
REMARK 500 1 U B 205 O4' U B 205 C4' -0.179
REMARK 500 1 A B 206 O4' A B 206 C4' -0.264
REMARK 500 1 C B 208 O4' C B 208 C4' -0.332
REMARK 500 1 G B 209 O4' G B 209 C4' -0.197
REMARK 500 1 G B 210 O4' G B 210 C4' -0.117
REMARK 500 1 G B 212 O4' G B 212 C4' -0.341
REMARK 500 1 G B 213 O4' G B 213 C4' -0.135
REMARK 500 1 C B 214 O4' C B 214 C4' -0.137
REMARK 500 1 U B 215 O4' U B 215 C4' -0.260
REMARK 500 1 A B 216 O4' A B 216 C4' -0.164
REMARK 500 1 G B 217 O4' G B 217 C4' -0.146
REMARK 500 1 U B 218 O4' U B 218 C4' -0.101
REMARK 500 1 C B 219 O4' C B 219 C4' -0.088
REMARK 500 2 A B 203 O4' A B 203 C4' -0.131
REMARK 500 2 U B 205 O4' U B 205 C4' -0.240
REMARK 500 2 A B 206 O4' A B 206 C4' -0.187
REMARK 500 2 G B 207 O4' G B 207 C4' -0.171
REMARK 500 2 G B 210 O4' G B 210 C4' -0.080
REMARK 500 2 G B 213 O4' G B 213 C4' -0.162
REMARK 500 2 U B 215 O4' U B 215 C4' -0.269
REMARK 500 2 A B 216 O4' A B 216 C4' -0.157
REMARK 500 3 A B 203 O4' A B 203 C4' -0.182
REMARK 500 3 C B 204 O4' C B 204 C4' -0.097
REMARK 500 3 U B 205 O4' U B 205 C4' -0.248
REMARK 500 3 A B 206 O4' A B 206 C4' -0.233
REMARK 500 3 G B 207 O4' G B 207 C4' -0.172
REMARK 500 3 C B 208 O4' C B 208 C4' -0.086
REMARK 500 3 G B 209 O4' G B 209 C4' -0.084
REMARK 500 3 G B 210 O4' G B 210 C4' -0.370
REMARK 500 3 G B 212 O4' G B 212 C4' -0.369
REMARK 500 3 G B 213 O4' G B 213 C4' -0.221
REMARK 500 3 U B 215 O4' U B 215 C4' -0.327
REMARK 500 3 A B 216 O4' A B 216 C4' -0.154
REMARK 500 3 G B 217 O4' G B 217 C4' -0.089
REMARK 500 3 U B 218 O4' U B 218 C4' -0.145
REMARK 500 4 A B 203 O4' A B 203 C4' -0.098
REMARK 500 4 C B 204 O4' C B 204 C4' -0.372
REMARK 500 4 U B 205 O4' U B 205 C4' -0.081
REMARK 500 4 A B 206 O4' A B 206 C4' -0.267
REMARK 500 4 G B 207 O4' G B 207 C4' -0.092
REMARK 500 4 C B 208 O4' C B 208 C4' -0.149
REMARK 500 4 G B 209 O4' G B 209 C4' -0.098
REMARK 500 4 G B 210 O4' G B 210 C4' -0.375
REMARK 500 4 A B 211 O4' A B 211 C4' -0.163
REMARK 500 4 G B 212 O4' G B 212 C4' -0.331
REMARK 500 4 G B 213 O4' G B 213 C4' -0.243
REMARK 500 4 U B 215 O4' U B 215 C4' -0.338
REMARK 500
REMARK 500 THIS ENTRY HAS 339 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 G B 201 C5' - C4' - O4' ANGL. DEV. = 12.3 DEGREES
REMARK 500 1 G B 201 C1' - O4' - C4' ANGL. DEV. = 7.5 DEGREES
REMARK 500 1 G B 201 C6 - N1 - C2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 G B 201 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 201 C5 - C6 - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 G B 202 C5' - C4' - O4' ANGL. DEV. = 22.4 DEGREES
REMARK 500 1 G B 202 C1' - O4' - C4' ANGL. DEV. = 7.2 DEGREES
REMARK 500 1 G B 202 C6 - N1 - C2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 G B 202 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 202 C5 - C6 - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 A B 203 C1' - O4' - C4' ANGL. DEV. = 9.7 DEGREES
REMARK 500 1 C B 204 C5' - C4' - O4' ANGL. DEV. = 27.9 DEGREES
REMARK 500 1 C B 204 C1' - O4' - C4' ANGL. DEV. = 11.6 DEGREES
REMARK 500 1 U B 205 C5' - C4' - O4' ANGL. DEV. = 26.3 DEGREES
REMARK 500 1 U B 205 C1' - O4' - C4' ANGL. DEV. = 9.9 DEGREES
REMARK 500 1 A B 206 C5' - C4' - O4' ANGL. DEV. = 24.4 DEGREES
REMARK 500 1 A B 206 C1' - O4' - C4' ANGL. DEV. = 11.6 DEGREES
REMARK 500 1 G B 207 O4' - C4' - C3' ANGL. DEV. = -8.0 DEGREES
REMARK 500 1 G B 207 C5' - C4' - O4' ANGL. DEV. = 22.7 DEGREES
REMARK 500 1 G B 207 C1' - O4' - C4' ANGL. DEV. = 7.9 DEGREES
REMARK 500 1 G B 207 C6 - N1 - C2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 G B 207 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 207 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 C B 208 C5' - C4' - O4' ANGL. DEV. = 26.9 DEGREES
REMARK 500 1 C B 208 C1' - O4' - C4' ANGL. DEV. = 10.3 DEGREES
REMARK 500 1 G B 209 C5' - C4' - O4' ANGL. DEV. = 34.8 DEGREES
REMARK 500 1 G B 209 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 209 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 209 C5 - C6 - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 G B 210 O4' - C4' - C3' ANGL. DEV. = -8.3 DEGREES
REMARK 500 1 G B 210 C5' - C4' - O4' ANGL. DEV. = 40.1 DEGREES
REMARK 500 1 G B 210 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 210 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 210 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 A B 211 C5' - C4' - O4' ANGL. DEV. = 32.9 DEGREES
REMARK 500 1 A B 211 C1' - O4' - C4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 G B 212 C1' - O4' - C4' ANGL. DEV. = 10.5 DEGREES
REMARK 500 1 G B 212 C6 - N1 - C2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 G B 212 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 212 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 G B 213 C5' - C4' - O4' ANGL. DEV. = 13.9 DEGREES
REMARK 500 1 G B 213 C1' - O4' - C4' ANGL. DEV. = 6.6 DEGREES
REMARK 500 1 G B 213 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 213 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 213 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 C B 214 C5' - C4' - O4' ANGL. DEV. = 16.4 DEGREES
REMARK 500 1 C B 214 C1' - O4' - C4' ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 U B 215 C5' - C4' - O4' ANGL. DEV. = -9.0 DEGREES
REMARK 500 1 U B 215 C1' - O4' - C4' ANGL. DEV. = 7.9 DEGREES
REMARK 500 1 A B 216 O4' - C4' - C3' ANGL. DEV. = -6.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 1622 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 GLN A 2 106.64 77.18
REMARK 500 1 LYS A 3 68.47 82.19
REMARK 500 1 THR A 12 48.17 35.99
REMARK 500 1 VAL A 13 154.75 -37.99
REMARK 500 1 ASN A 17 -63.98 -97.03
REMARK 500 1 ARG A 32 106.99 -55.06
REMARK 500 1 LYS A 34 51.76 -144.36
REMARK 500 1 TRP A 37 39.46 -83.70
REMARK 500 1 LYS A 38 -49.14 -133.83
REMARK 500 1 GLU A 51 -70.35 -96.79
REMARK 500 1 GLN A 53 170.85 -54.46
REMARK 500 1 ALA A 54 76.39 -104.34
REMARK 500 2 GLN A 2 55.88 32.33
REMARK 500 2 LYS A 3 68.61 -178.61
REMARK 500 2 THR A 12 49.22 36.69
REMARK 500 2 VAL A 13 154.21 -37.17
REMARK 500 2 ARG A 32 108.32 -57.03
REMARK 500 2 TRP A 37 36.23 -84.21
REMARK 500 2 LYS A 38 -49.42 -132.78
REMARK 500 2 GLU A 51 -60.62 -93.14
REMARK 500 2 GLN A 53 61.54 -179.61
REMARK 500 2 ALA A 54 176.65 179.76
REMARK 500 3 LYS A 3 59.53 71.61
REMARK 500 3 THR A 12 48.46 36.34
REMARK 500 3 VAL A 13 154.44 -37.63
REMARK 500 3 ASN A 17 -67.49 -91.08
REMARK 500 3 ARG A 32 106.22 -54.74
REMARK 500 3 LYS A 34 51.89 -144.52
REMARK 500 3 TRP A 37 36.97 -82.98
REMARK 500 3 LYS A 38 -49.58 -132.55
REMARK 500 3 GLU A 51 -92.07 174.91
REMARK 500 3 ARG A 52 178.65 168.56
REMARK 500 3 GLN A 53 144.14 177.89
REMARK 500 4 LYS A 3 64.50 77.36
REMARK 500 4 LYS A 11 -85.84 -108.82
REMARK 500 4 THR A 12 45.55 -179.85
REMARK 500 4 VAL A 13 154.66 -40.15
REMARK 500 4 ASN A 17 -61.96 -94.96
REMARK 500 4 ARG A 32 104.97 -56.67
REMARK 500 4 LYS A 34 54.64 -147.93
REMARK 500 4 TRP A 37 32.50 -83.77
REMARK 500 4 LYS A 38 -49.03 -131.61
REMARK 500 4 GLN A 53 60.13 -167.35
REMARK 500 5 LYS A 3 64.50 77.34
REMARK 500 5 THR A 12 47.79 35.60
REMARK 500 5 VAL A 13 154.48 -40.07
REMARK 500 5 ARG A 32 105.91 -57.38
REMARK 500 5 LYS A 34 54.66 -149.62
REMARK 500 5 TRP A 37 32.71 -83.95
REMARK 500 5 ARG A 52 98.05 52.28
REMARK 500
REMARK 500 THIS ENTRY HAS 246 RAMACHANDRAN OUTLIERS.
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 A 56 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 18 SG 93.4
REMARK 620 3 HIS A 23 NE2 93.4 113.8
REMARK 620 4 CYS A 28 SG 93.8 146.5 98.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 57 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 36 SG
REMARK 620 2 CYS A 39 SG 97.0
REMARK 620 3 HIS A 44 NE2 101.2 83.6
REMARK 620 4 CYS A 49 SG 107.2 129.5 131.5
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 A 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 57
DBREF 1A1T A 1 55 UNP Q75677 Q75677_9HIV1 378 432
DBREF 1A1T B 201 220 PDB 1A1T 1A1T 201 220
SEQADV 1A1T MET A 1 UNP Q75677 ILE 378 CONFLICT
SEQRES 1 B 20 G G A C U A G C G G A G G
SEQRES 2 B 20 C U A G U C C
SEQRES 1 A 55 MET GLN LYS GLY ASN PHE ARG ASN GLN ARG LYS THR VAL
SEQRES 2 A 55 LYS CYS PHE ASN CYS GLY LYS GLU GLY HIS ILE ALA LYS
SEQRES 3 A 55 ASN CYS ARG ALA PRO ARG LYS LYS GLY CYS TRP LYS CYS
SEQRES 4 A 55 GLY LYS GLU GLY HIS GLN MET LYS ASP CYS THR GLU ARG
SEQRES 5 A 55 GLN ALA ASN
HET ZN A 56 1
HET ZN A 57 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 GLY A 4 LYS A 11 5 8
HELIX 2 2 ALA A 25 ASN A 27 5 3
HELIX 3 3 MET A 46 ASP A 48 5 3
LINK SG CYS A 15 ZN ZN A 56 1555 1555 2.40
LINK SG CYS A 18 ZN ZN A 56 1555 1555 2.35
LINK NE2 HIS A 23 ZN ZN A 56 1555 1555 2.12
LINK SG CYS A 28 ZN ZN A 56 1555 1555 2.30
LINK SG CYS A 36 ZN ZN A 57 1555 1555 2.41
LINK SG CYS A 39 ZN ZN A 57 1555 1555 2.32
LINK NE2 HIS A 44 ZN ZN A 57 1555 1555 2.07
LINK SG CYS A 49 ZN ZN A 57 1555 1555 2.30
SITE 1 AC1 4 CYS A 15 CYS A 18 HIS A 23 CYS A 28
SITE 1 AC2 4 CYS A 36 CYS A 39 HIS A 44 CYS A 49
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 - b 16 2 Bytes